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Conserved domains on  [gi|1036600687|gb|OBA08816|]
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cell division protein FtsA [Bacillus subtilis]

Protein Classification

cell division protein FtsA( domain architecture ID 11436667)

cell division protein FtsA may serve as a membrane anchor for the Z ring

CATH:  3.30.420.40|3.90.640.10|3.30.1490.110
Gene Ontology:  GO:0051301|GO:0043093
PubMed:  22473211

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FtsA COG0849
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
2-394 4.46e-180

Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 440610 [Multi-domain]  Cd Length: 402  Bit Score: 508.13  E-value: 4.46e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   2 NNNELYVSLDIGTSNTKVIVGEMTDD-SLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVN 80
Cdd:COG0849     1 AKSNIIVGLDIGTSKVVALVGEVDPDgKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  81 GNYINIQDTNGVVAVSseNKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLIT 160
Cdd:COG0849    81 GGHIKSQNSRGVVAIS--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 161 GSKTILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKD 240
Cdd:COG0849   159 GPKTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITND 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 241 ISIGLRTSTEEAERVKKQFGHAYYDEASEDEVFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEELRSMGITD-LP 319
Cdd:COG0849   239 IAIGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKELKRSGYEEkLP 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 320 GGFVLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQFACRNARIQGRKIGFKMPEEAVQEI 394
Cdd:COG0849   319 AGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGglpeaVRDPAYATAVGLLLYAAKNQEERFEPVKEKKKGGLFGRI 398
 
Name Accession Description Interval E-value
FtsA COG0849
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
2-394 4.46e-180

Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440610 [Multi-domain]  Cd Length: 402  Bit Score: 508.13  E-value: 4.46e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   2 NNNELYVSLDIGTSNTKVIVGEMTDD-SLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVN 80
Cdd:COG0849     1 AKSNIIVGLDIGTSKVVALVGEVDPDgKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  81 GNYINIQDTNGVVAVSseNKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLIT 160
Cdd:COG0849    81 GGHIKSQNSRGVVAIS--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 161 GSKTILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKD 240
Cdd:COG0849   159 GPKTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITND 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 241 ISIGLRTSTEEAERVKKQFGHAYYDEASEDEVFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEELRSMGITD-LP 319
Cdd:COG0849   239 IAIGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKELKRSGYEEkLP 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 320 GGFVLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQFACRNARIQGRKIGFKMPEEAVQEI 394
Cdd:COG0849   319 AGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGglpeaVRDPAYATAVGLLLYAAKNQEERFEPVKEKKKGGLFGRI 398
ftsA TIGR01174
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ...
 6-370 2.19e-172

cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division]


Pssm-ID: 273483 [Multi-domain]  Cd Length: 371  Bit Score: 487.53  E-value: 2.19e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   6 LYVSLDIGTSNTKVIVGEMTDDS-LNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNYI 84
Cdd:TIGR01174   1 LIVGLDIGTSKICAIVAEVLEDGeLNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  85 NIQDTNGVVAVSSenKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSKT 164
Cdd:TIGR01174  81 KSQNSIGVVAIKD--KEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSST 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 165 ILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIG 244
Cdd:TIGR01174 159 ILRNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 245 LRTSTEEAERVKKQFGHAYYDEASEDEVFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVS-EELRSMGI-TDLPGGF 322
Cdd:TIGR01174 239 LRTPLEEAERIKIKYGCASIPLEGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKqKELRKSGFkEELNGGI 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1036600687 323 VLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQF 370
Cdd:TIGR01174 319 VLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGgltedVNDPEYSTAVGLLLY 371
ASKHA_NBD_FtsA cd24048
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ...
 5-370 4.09e-166

nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.


Pssm-ID: 466898 [Multi-domain]  Cd Length: 372  Bit Score: 471.63  E-value: 4.09e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   5 ELYVSLDIGTSNTKVIVGEMT-DDSLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNY 83
Cdd:cd24048     1 NIIVGLDIGTSKICALVGEVSeDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  84 INIQDTNGVVAVSSENkEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSK 163
Cdd:cd24048    81 IRSVNSRGVIAISDKD-EITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGSS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 164 TILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISI 243
Cdd:cd24048   160 SAIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 244 GLRTSTEEAERVKKQFGHAYYDEASEDEVFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEELRSMGITD-LPGGF 322
Cdd:cd24048   240 GLNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKELKESGYEDlLPGGI 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1036600687 323 VLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQF 370
Cdd:cd24048   320 VLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGglpeeVNDPAYATAVGLLLY 372
ftsA PRK09472
cell division protein FtsA; Reviewed
 6-371 1.30e-75

cell division protein FtsA; Reviewed


Pssm-ID: 181887 [Multi-domain]  Cd Length: 420  Bit Score: 242.00  E-value: 1.30e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   6 LYVSLDIGTSNTKVIVGEMTDDS-LNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNYI 84
Cdd:PRK09472    9 LVVGLEIGTAKVAALVGEVLPDGmVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  85 NIQDTNGVVAVSSEnkEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSKT 164
Cdd:PRK09472   89 SCQNEIGMVPISEE--EVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHND 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 165 ILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIG 244
Cdd:PRK09472  167 MAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 245 LRTSTEEAERVKKQFGHAYYDEASEDEVFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEE-------LRSMGIT- 316
Cdd:PRK09472  247 FGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEilqlqeqLRQQGVKh 326

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 317 DLPGGFVLTGGQAAMPGVMSLAQDVLQNNVRVASP-NYIG----VRDPQYMTGVGLIQFA 371
Cdd:PRK09472  327 HLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPlNITGltdyAQEPYYSTAVGLLHYG 386
FtsA smart00842
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
 7-194 5.70e-73

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains.


Pssm-ID: 214850  Cd Length: 187  Bit Score: 227.36  E-value: 5.70e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687    7 YVSLDIGTSNTKVIVGEMTDD-SLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNYIN 85
Cdd:smart00842   1 IVGLDIGTSKIKALVAEVDEDgEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   86 IQDTNGVVAVssENKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSKTI 165
Cdd:smart00842  81 SVNVSGVVAI--PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKSA 158

                          170       180
                   ....*....|....*....|....*....
gi 1036600687  166 LHNLLRCVERAGIEITDICLQPLAAGSAA 194
Cdd:smart00842 159 IQNLEKCVERAGLEVDGIVLEPLASAEAV 187
FtsA pfam14450
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
 205-366 3.53e-54

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.


Pssm-ID: 464177 [Multi-domain]  Cd Length: 167  Bit Score: 177.91  E-value: 3.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 205 ALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIGLRTSTEEAERVKKQFGHAYYDEASEDevfEVTVIGTNQKQ 284
Cdd:pfam14450   1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADED---EVPGVGGREPR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 285 TFTQQEAANIIEARVEEILEIVSEELRSMG--------ITDLPGGFVLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIGV 356
Cdd:pfam14450  78 EISRKELAEIIEARVEEILELVRAELEDREvlpgeyvrLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIGG 157

                         170
                  ....*....|
gi 1036600687 357 RDPQYMTGVG 366
Cdd:pfam14450 158 RNPAYATALG 167
 
Name Accession Description Interval E-value
FtsA COG0849
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
2-394 4.46e-180

Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440610 [Multi-domain]  Cd Length: 402  Bit Score: 508.13  E-value: 4.46e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   2 NNNELYVSLDIGTSNTKVIVGEMTDD-SLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVN 80
Cdd:COG0849     1 AKSNIIVGLDIGTSKVVALVGEVDPDgKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  81 GNYINIQDTNGVVAVSseNKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLIT 160
Cdd:COG0849    81 GGHIKSQNSRGVVAIS--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 161 GSKTILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKD 240
Cdd:COG0849   159 GPKTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITND 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 241 ISIGLRTSTEEAERVKKQFGHAYYDEASEDEVFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEELRSMGITD-LP 319
Cdd:COG0849   239 IAIGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKELKRSGYEEkLP 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 320 GGFVLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQFACRNARIQGRKIGFKMPEEAVQEI 394
Cdd:COG0849   319 AGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGglpeaVRDPAYATAVGLLLYAAKNQEERFEPVKEKKKGGLFGRI 398
ftsA TIGR01174
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ...
 6-370 2.19e-172

cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division]


Pssm-ID: 273483 [Multi-domain]  Cd Length: 371  Bit Score: 487.53  E-value: 2.19e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   6 LYVSLDIGTSNTKVIVGEMTDDS-LNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNYI 84
Cdd:TIGR01174   1 LIVGLDIGTSKICAIVAEVLEDGeLNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  85 NIQDTNGVVAVSSenKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSKT 164
Cdd:TIGR01174  81 KSQNSIGVVAIKD--KEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSST 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 165 ILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIG 244
Cdd:TIGR01174 159 ILRNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 245 LRTSTEEAERVKKQFGHAYYDEASEDEVFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVS-EELRSMGI-TDLPGGF 322
Cdd:TIGR01174 239 LRTPLEEAERIKIKYGCASIPLEGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKqKELRKSGFkEELNGGI 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1036600687 323 VLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQF 370
Cdd:TIGR01174 319 VLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGgltedVNDPEYSTAVGLLLY 371
ASKHA_NBD_FtsA cd24048
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ...
 5-370 4.09e-166

nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.


Pssm-ID: 466898 [Multi-domain]  Cd Length: 372  Bit Score: 471.63  E-value: 4.09e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   5 ELYVSLDIGTSNTKVIVGEMT-DDSLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNY 83
Cdd:cd24048     1 NIIVGLDIGTSKICALVGEVSeDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  84 INIQDTNGVVAVSSENkEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSK 163
Cdd:cd24048    81 IRSVNSRGVIAISDKD-EITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGSS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 164 TILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISI 243
Cdd:cd24048   160 SAIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 244 GLRTSTEEAERVKKQFGHAYYDEASEDEVFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEELRSMGITD-LPGGF 322
Cdd:cd24048   240 GLNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKELKESGYEDlLPGGI 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1036600687 323 VLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQF 370
Cdd:cd24048   320 VLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGglpeeVNDPAYATAVGLLLY 372
ftsA PRK09472
cell division protein FtsA; Reviewed
 6-371 1.30e-75

cell division protein FtsA; Reviewed


Pssm-ID: 181887 [Multi-domain]  Cd Length: 420  Bit Score: 242.00  E-value: 1.30e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   6 LYVSLDIGTSNTKVIVGEMTDDS-LNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNYI 84
Cdd:PRK09472    9 LVVGLEIGTAKVAALVGEVLPDGmVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  85 NIQDTNGVVAVSSEnkEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSKT 164
Cdd:PRK09472   89 SCQNEIGMVPISEE--EVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHND 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 165 ILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIG 244
Cdd:PRK09472  167 MAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 245 LRTSTEEAERVKKQFGHAYYDEASEDEVFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEE-------LRSMGIT- 316
Cdd:PRK09472  247 FGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEilqlqeqLRQQGVKh 326

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 317 DLPGGFVLTGGQAAMPGVMSLAQDVLQNNVRVASP-NYIG----VRDPQYMTGVGLIQFA 371
Cdd:PRK09472  327 HLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPlNITGltdyAQEPYYSTAVGLLHYG 386
FtsA smart00842
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
 7-194 5.70e-73

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains.


Pssm-ID: 214850  Cd Length: 187  Bit Score: 227.36  E-value: 5.70e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687    7 YVSLDIGTSNTKVIVGEMTDD-SLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNYIN 85
Cdd:smart00842   1 IVGLDIGTSKIKALVAEVDEDgEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   86 IQDTNGVVAVssENKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSKTI 165
Cdd:smart00842  81 SVNVSGVVAI--PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKSA 158

                          170       180
                   ....*....|....*....|....*....
gi 1036600687  166 LHNLLRCVERAGIEITDICLQPLAAGSAA 194
Cdd:smart00842 159 IQNLEKCVERAGLEVDGIVLEPLASAEAV 187
FtsA pfam14450
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
 205-366 3.53e-54

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.


Pssm-ID: 464177 [Multi-domain]  Cd Length: 167  Bit Score: 177.91  E-value: 3.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 205 ALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIGLRTSTEEAERVKKQFGHAYYDEASEDevfEVTVIGTNQKQ 284
Cdd:pfam14450   1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADED---EVPGVGGREPR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 285 TFTQQEAANIIEARVEEILEIVSEELRSMG--------ITDLPGGFVLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIGV 356
Cdd:pfam14450  78 EISRKELAEIIEARVEEILELVRAELEDREvlpgeyvrLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIGG 157

                         170
                  ....*....|
gi 1036600687 357 RDPQYMTGVG 366
Cdd:pfam14450 158 RNPAYATALG 167
ASKHA_NBD_PilM-like cd24004
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ...
 8-368 1.07e-40

nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466854 [Multi-domain]  Cd Length: 282  Bit Score: 146.28  E-value: 1.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   8 VSLDIGTSNTKVIVGEMTDDSLNIIGVGNVPSEGL--KKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGvngnyin 85
Cdd:cd24004     1 FALDIGTRSIKGLVLEEDDENIEVLAFSSEEHPERamGDGQIHDISKVAESIKELLKELEEKLGSKLKDVVIA------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  86 iqdtngvvavssenkeiqvedvrrvmeaaqvvsvpheqlivdvIPKqfIVDGrdeitdpkkmlgvrlevegtlitgskti 165
Cdd:cd24004    74 -------------------------------------------IAK--VVES---------------------------- 80

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 166 lhnLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIGL 245
Cdd:cd24004    81 ---LLNVLEKAGLEPVGLTLEPFAAANLLIPYDMRDLNIALVDIGAGTTDIALIRNGGIEAYRMVPLGGDDFTKAIAEGF 157

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 246 RTSTEEAERVKKQFGHAYYDEASEDEVFEVTVIgtnqkqtftqqEAANIIEARVEEILEIVSEELRSM-GITDLPGGFVL 324
Cdd:cd24004   158 LISFEEAEKIKRTYGIFLLIEAKDQLGFTINKK-----------EVYDIIKPVLEELASGIANAIEEYnGKFKLPDAVYL 226

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1036600687 325 TGGQAAMPGVMSLAQDVLQNNV-RVASPNYIGV----------RDPQYMTGVGLI 368
Cdd:cd24004   227 VGGGSKLPGLNEALAEKLGLPVeRIAPRNIGAIsditdetskaKGPEFVTPLGIA 281
ASKHA_NBD_PilM cd24049
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ...
 8-351 1.06e-33

nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.


Pssm-ID: 466899 [Multi-domain]  Cd Length: 339  Bit Score: 128.94  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   8 VSLDIGTSNTKVIVGEMTDDSLNIIGVG--NVPSEGLKKGSIVDIDETVHSIRKAFDQAermvGFPLRKAIVGVNGNYIN 85
Cdd:cd24049     1 LGIDIGSSSIKAVELKRSGGGLVLVAFAiiPLPEGAIVDGEIADPEALAEALKKLLKEN----KIKGKKVVVALPGSDVI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  86 IQDTNgvVAVSSEnKEIQvEDVRrvMEAAQVVSVPHEQLIVDvipkqFIVDGRDEITDPKkmlgvrleVEGTLITGSKTI 165
Cdd:cd24049    77 VRTIK--LPKMPE-KELE-EAIR--FEAEQYLPFPLEEVVLD-----YQILGEVEEGGEK--------LEVLVVAAPKEI 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 166 LHNLLRCVERAGIEITDICLQPLAAGSA--ALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISI 243
Cdd:cd24049   138 VESYLELLKEAGLKPVAIDVESFALARAleYLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRSIPVGGNDITEAIAK 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 244 GLRTSTEEAERVKKQFGHAYYDEASEDEVFEVTVigtnqkqtftqQEAANIIEARVEEILEIVSEELRSMGITDLpggfV 323
Cdd:cd24049   218 ALGLSFEEAEELKREYGLLLEGEEGELKKVAEAL-----------RPVLERLVSEIRRSLDYYRSQNGGEPIDKI----Y 282

                         330       340
                  ....*....|....*....|....*...
gi 1036600687 324 LTGGQAAMPGVMSLAQDVLQNNVRVASP 351
Cdd:cd24049   283 LTGGGSLLPGLDEYLSERLGIPVEILNP 310
SHS2_FTSA pfam02491
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes ...
 87-160 6.16e-21

SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. The SHS2 domain is inserted in to the RNAseH fold of FtsA, and is involved in protein-protein interaction.


Pssm-ID: 460571 [Multi-domain]  Cd Length: 73  Bit Score: 86.01  E-value: 6.16e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1036600687  87 QDTNGVVAVSseNKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLIT 160
Cdd:pfam02491   2 QNSSGVVAIS--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEADVHVVT 73
PilM COG4972
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];
7-233 1.34e-17

Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];


Pssm-ID: 443997 [Multi-domain]  Cd Length: 294  Bit Score: 82.98  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   7 YVSLDIGTSNTKVIVGEMTDDSLNIIGVG--NVPSEGLKKGSIVDIDETVHSIRKAFDQAermvGFPLRKAIVGVNGNYI 84
Cdd:COG4972     4 LVGIDIGSSSIKLVELSKSGGGYRLERYAeePLPEGAVVDGNIVDPEAVAEALKELLKRL----KIKTKRVAIAVPGSSV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  85 NIQDTNgVVAVSSENKEIQVEdvrrvMEAAQVVSVPHEQLIVDvipkqFIVDGRDEiTDPKKMlgvrlEVegtLITGS-K 163
Cdd:COG4972    80 ITRKIT-LPALSEKELEEAIE-----FEAEQYIPFPLEEVVLD-----FQVLGPSE-EGPEKV-----EV---LLVAArK 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1036600687 164 TILHNLLRCVERAGIEITDICLQPLAAGSAA--LSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLG 233
Cdd:COG4972   140 EVVEDYVELLEAAGLKPVVVDVEPFALLRALelLPPSGPDETVALVDIGASSTTLSVLSNGKPIFTREIPFG 211
ASKHA_NBD_MreB-like cd10225
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ...
 173-349 7.44e-15

nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466824 [Multi-domain]  Cd Length: 317  Bit Score: 75.20  E-value: 7.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 173 VERAGIeiTDICL--QPLAAGSAA-LSKDEKNlGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDIS------- 242
Cdd:cd10225   114 AEHAGA--REVYLieEPMAAAIGAgLPIEEPR-GSMVVDIGGGTTEIAVISLGGIVTSRSVRVAGDEMDEAIInyvrrky 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 243 ---IGLRTsteeAERVKKQFGHAYYDEasEDEVFEVT----VIGTNQKQTFTQQEAANIIEARVEEILEIVSEELRSM-- 313
Cdd:cd10225   191 nllIGERT----AERIKIEIGSAYPLD--EELSMEVRgrdlVTGLPRTIEITSEEVREALEEPVNAIVEAVRSTLERTpp 264

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1036600687 314 ----GITDlpGGFVLTGGQAAMPGVMSLAQDVLQNNVRVA 349
Cdd:cd10225   265 elaaDIVD--RGIVLTGGGALLRGLDELLREETGLPVHVA 302
ASKHA_NBD_EutJ cd24047
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ...
 92-367 1.01e-14

nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.


Pssm-ID: 466897 [Multi-domain]  Cd Length: 241  Bit Score: 73.45  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  92 VVAVSSENKEIQVEdvrrvMEAAQVVsvpHEQLIVDVIPKQFIVdgRDEITDPKKMLGVRLEVE------GTLITGSKTI 165
Cdd:cd24047    14 LVVVDEEGQPVAGA-----LERADVV---RDGIVVDYIGAIRIV--RKLKETLEKKLGVELTSAatafppGTGERDARAI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 166 LHnllrCVERAGIEITDICLQPLAAGSAalskdeknLGV---ALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDIS 242
Cdd:cd24047    84 RN----VLEGAGLEVSNVVDEPTAANAV--------LGIrdgAVVDIGGGTTGIAVLKDGKVVYTADEPTGGTHLSLVLA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 243 IGLRTSTEEAERVKKqfghayyDEASEDEVFEvtvigtnqkqtftqqeaanIIEARVEEILEIVSEELRSMGITDLpggf 322
Cdd:cd24047   152 GNYGISFEEAEIIKR-------DPARHKELLP-------------------VVRPVIEKMASIVKRHIKGYKVKDL---- 201

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1036600687 323 VLTGGQAAMPGVMSLAQDVLQNNVRVASpnyigvrDPQYMTGVGL 367
Cdd:cd24047   202 YLVGGTCCLPGIEEVFEKETGLPVYKPS-------NPLLVTPLGI 239
PRK13930 PRK13930
rod shape-determining protein MreB; Provisional
 207-349 3.11e-11

rod shape-determining protein MreB; Provisional


Pssm-ID: 237564 [Multi-domain]  Cd Length: 335  Bit Score: 64.38  E-value: 3.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 207 IDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDI----------SIGLRTsteeAERVKKQFGHAYYDEasEDEVFEVT 276
Cdd:PRK13930  157 VDIGGGTTEVAVISLGGIVYSESIRVAGDEMDEAIvqyvrrkynlLIGERT----AEEIKIEIGSAYPLD--EEESMEVR 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 277 ----VIGTNQKQTFTQQEAANIIEARVEEILEIVSEELR------SMGITDlpGGFVLTGGQAAMPGVMSLAQDVLQNNV 346
Cdd:PRK13930  231 grdlVTGLPKTIEISSEEVREALAEPLQQIVEAVKSVLEktppelAADIID--RGIVLTGGGALLRGLDKLLSEETGLPV 308


                  ...
gi 1036600687 347 RVA 349
Cdd:PRK13930  309 HIA 311
pilM TIGR01175
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV ...
 8-367 6.37e-11

type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV fimbria in Pseudomonas aeruginosa responsible for twitching motility, and for a similar pilus-like structure in Synechocystis. It is also found in species such as Deinococcus described as having natural transformation (for which a type IV pilus-like structure is proposed) but not fimbria.


Pssm-ID: 273484 [Multi-domain]  Cd Length: 348  Bit Score: 63.65  E-value: 6.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687   8 VSLDIGTSNTKVIVGEMTDDSLNIIGVGN--VPSEGLKKGSIVDIDETVHSIRKAFDQAermvGFPLRKAIVGVNGNYIN 85
Cdd:TIGR01175   6 VGIDIGSTSVKVAQLKRSGDRYKLEHYAVepLPAGIFTEGHIVEYQAVAEALKELLSEL----GINTKKAATAVPGSAVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  86 IQdtngVVAVSSENKEIQVEDVRRVmEAAQVVSVPHEQLIVDVipkqfivdgrDEITDPKKMLGVRLEVegtLITGSKT- 164
Cdd:TIGR01175  82 TK----VIPVPAGLDERELEFAVYI-EASHYIPYPIEEVSLDF----------EKLGLKANNPESTVQV---LLAATRKe 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 165 ILHNLLRCVERAGIEITDICLQPLAA------GSAALSKDEKNL-GVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENI 237
Cdd:TIGR01175 144 VVDSRLHALKLAGLEPKVVDVESFALlrawrlLGEQLASRTYRLtDAALVDIGATSSTLNLLHPGRMLFTREVPFGTRQL 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 238 TKDISIGLRTSTEEAERVKKQFGHayydeaSEDEVFEVTvigTNQKQTFTQQEAANIiearveEILEIVSEELRSmgitd 317
Cdd:TIGR01175 224 TSELSRAYGLNPEEAGEAKQQGGL------PLLYDPEVL---RRFKGELVDEIRRSL------QFFTAQSGTNSL----- 283

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1036600687 318 lpGGFVLTGGQAAMPGVMSLAQDVLQNNVRVASP------------NYIGVRDPQYMTGVGL 367
Cdd:TIGR01175 284 --DGLVLAGGGATLSGLDAAIYQRLGLPTEVANPfalmaldakvdaGRLAVDAPALMTALGL 343
MreB COG1077
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ...
 207-349 2.66e-10

Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 440695 [Multi-domain]  Cd Length: 339  Bit Score: 61.63  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 207 IDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDI----------SIGLRTsteeAERVKKQFGHAYYDEasEDEVFEVT 276
Cdd:COG1077   156 VDIGGGTTEVAVISLGGIVVSRSIRVAGDELDEAIiqyvrkkynlLIGERT----AEEIKIEIGSAYPLE--EELTMEVR 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 277 ----VIGTNQKQTFTQQEAANIIEARVEEILEIVSE-------ELRSmGITDlpGGFVLTGGQAAMPGVMSLAQDVLQNN 345
Cdd:COG1077   230 grdlVTGLPKTITITSEEIREALEEPLNAIVEAIKSvlektppELAA-DIVD--RGIVLTGGGALLRGLDKLLSEETGLP 306


                  ....
gi 1036600687 346 VRVA 349
Cdd:COG1077   307 VHVA 310
PRK15080 PRK15080
ethanolamine utilization protein EutJ; Provisional
 92-372 4.01e-10

ethanolamine utilization protein EutJ; Provisional


Pssm-ID: 237904 [Multi-domain]  Cd Length: 267  Bit Score: 60.23  E-value: 4.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  92 VVAVSSENKEIqvedVRRVMEAAQVVsvpHEQLIVDVIPKQFIVdgRDEITDPKKMLGVRLEVEGTLI-----TGSKTIL 166
Cdd:PRK15080   37 VLAVLDEDGQP----VAGALEWADVV---RDGIVVDFIGAVTIV--RRLKATLEEKLGRELTHAATAIppgtsEGDPRAI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 167 HNLlrcVERAGIEITDICLQPLAAGSAalskdeknLGV---ALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISI 243
Cdd:PRK15080  108 INV---VESAGLEVTHVLDEPTAAAAV--------LGIdngAVVDIGGGTTGISILKDGKVVYSADEPTGGTHMSLVLAG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 244 GLRTSTEEAERVKKqfghayyDEASEDEVFEVtvigtnqkqtftqqeaaniIEARVEEILEIVSEELRSMGITDLpggfV 323
Cdd:PRK15080  177 AYGISFEEAEQYKR-------DPKHHKEIFPV-------------------VKPVVEKMASIVARHIEGQDVEDI----Y 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1036600687 324 LTGGQAAMPGVMSLAQDVLQnnVRVASPNYigvrdPQYMTGVGlIQFAC 372
Cdd:PRK15080  227 LVGGTCCLPGFEEVFEKQTG--LPVHKPQH-----PLFVTPLG-IALSC 267
PilM_2 pfam11104
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for ...
 10-351 4.71e-10

Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for competency and pilus biogenesis. It binds to PilN and ATP.


Pssm-ID: 431656 [Multi-domain]  Cd Length: 340  Bit Score: 60.77  E-value: 4.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  10 LDIGTSNTKVIVGEMTDDSLNI--IGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAermvGFPLRKAIVGVNGNYINIQ 87
Cdd:pfam11104   2 IDISSSAIKLVELSKKKGGYRLerYAIEPLPKGAVVDGNIENIDAVSEALRRAVKKS----GTRLKNVAIAVPGSAVITK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  88 DTNGVVAVSSENKEIQVEdvrrvMEAAQVVSVPHEQLIVDvipkqFIVDGRDeITDPKKMlgvrlEVegtLITGSKT-IL 166
Cdd:pfam11104  78 KIILPAGLSEEELEAQVE-----IEANQYIPFPLDEVSLD-----FEVLGPN-AANPDDV-----DV---LLAAARKeKV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 167 HNLLRCVERAGI--EITDICLQPLAAGSA----ALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKD 240
Cdd:pfam11104 139 EDRVDLLEAAGLkpKVVDVESYALERAFErivsQLPNDGKDKCVAIVDIGANMTTLSVLRNGEIIYTREQAFGGAQLTQE 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 241 ISIGLRTSTEEAERVKK--QFGHAYydeasEDEVFEVTVIGTNQK-----QTFTQQEAANiieaRVEEIleivseelrsm 313
Cdd:pfam11104 219 IVRRYGMSYEEAEIAKRngDLPEDY-----ESEVLEPFVEALAQQisralQFFFTSTPYN----KVDYI----------- 278

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1036600687 314 gitdlpggfVLTGGQAAMPGVMSLAQDVLQNNVRVASP 351
Cdd:pfam11104 279 ---------VLAGGCANIPGLAELVTERLGFSTTVANP 307
MreB_Mbl pfam06723
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ...
 207-349 1.24e-08

MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.


Pssm-ID: 399596 [Multi-domain]  Cd Length: 327  Bit Score: 56.41  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 207 IDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDI----------SIGLRTsteeAERVKKQFGHAYYDEasedEVFEVT 276
Cdd:pfam06723 150 VDIGGGTTEVAVISLGGIVTSKSVRVAGDEFDEAIikyirkkynlLIGERT----AERIKIEIGSAYPTE----EEEKME 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 277 VIGTNQ------KQTFTQQEAANIIEARVEEILEIVSEELR------SMGITDlpGGFVLTGGQAAMPGVMSLAQDVLQN 344
Cdd:pfam06723 222 IRGRDLvtglpkTIEISSEEVREALKEPVSAIVEAVKEVLEktppelAADIVD--RGIVLTGGGALLRGLDKLLSDETGL 299


                  ....*
gi 1036600687 345 NVRVA 349
Cdd:pfam06723 300 PVHIA 304
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
 169-348 1.45e-08

nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466811 [Multi-domain]  Cd Length: 329  Bit Score: 55.96  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 169 LLRCVERAGIEITDICLQ----PLAAGSAAL------SKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRV--------I 230
Cdd:cd10170    93 LREAARAAGFGSDSDNVRlvsePEAAALYALedkgdlLPLKPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevapgggA 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 231 PLGGENIT-------------------KDISIGLRTSTEEAERVKKQFGHAYYDEASEDEVFEVTVIGTNQKQ---TFTQ 288
Cdd:cd10170   173 LLGGTDIDeafekllreklgdkgkdlgRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLPELGLEKgtlLLTE 252

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 289 QEAANIIEARVEEILEIVSEELRSMGITDlPGGFVLTGGQAAMPGVMSLAQDVLQNNVRV 348
Cdd:cd10170   253 EEIRDLFDPVIDKILELIEEQLEAKSGTP-PDAVVLVGGFSRSPYLRERLRERFGSAGII 311
FtsA pfam14450
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
 10-176 2.40e-07

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.


Pssm-ID: 464177 [Multi-domain]  Cd Length: 167  Bit Score: 50.41  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  10 LDIGTSNTKVIVGEmtDDSL---NIIGVGnvpSEGLKKGsivdideTVHSIRKAFDQAERMVGFPLRKAIVGVNGNYINI 86
Cdd:pfam14450   3 IDIGGGTTDIAVFE--DGALrhtRVIPVG---GNGITKD-------IAIGLRTAVEEAERLKIKYGSALASLADEDEVPG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687  87 QDTNGVVAVSSEN-KEIQVEDVRRVMEAAQvvsvpheqlivdvipkqFIVDGRDEITDPKKMLGVrlEVEGTLITGSKTI 165
Cdd:pfam14450  71 VGGREPREISRKElAEIIEARVEEILELVR-----------------AELEDREVLPGEYVRLEV--DVHGIVLTGGGSA 131

                         170
                  ....*....|.
gi 1036600687 166 LHNLLRCVERA 176
Cdd:pfam14450 132 LPGLVELAERA 142
PRK13927 PRK13927
rod shape-determining protein MreB; Provisional
 203-329 2.41e-07

rod shape-determining protein MreB; Provisional


Pssm-ID: 237562 [Multi-domain]  Cd Length: 334  Bit Score: 52.40  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 203 GVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDIS----------IGLRTsteeAERVKKQFGHAYydeaSEDEV 272
Cdd:PRK13927  149 GSMVVDIGGGTTEVAVISLGGIVYSKSVRVGGDKFDEAIInyvrrnynllIGERT----AERIKIEIGSAY----PGDEV 220

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036600687 273 FEVTVIGTNQ------KQTFTQQEAA--------NIIEArVEEILEIVSEELrSMGITDLpgGFVLTGGQA 329
Cdd:PRK13927  221 LEMEVRGRDLvtglpkTITISSNEIRealqeplsAIVEA-VKVALEQTPPEL-AADIVDR--GIVLTGGGA 287
PRK13928 PRK13928
rod shape-determining protein Mbl; Provisional
 186-349 2.60e-07

rod shape-determining protein Mbl; Provisional


Pssm-ID: 237563 [Multi-domain]  Cd Length: 336  Bit Score: 52.21  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 186 QPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDIS----------IGLRTsteeAERV 255
Cdd:PRK13928  131 EPLAAAIGAGLDISQPSGNMVVDIGGGTTDIAVLSLGGIVTSSSIKVAGDKFDEAIIryirkkykllIGERT----AEEI 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 256 KKQFGHAYYDeaSEDEVFEVT----VIGTNQKQTFTQQEAANIIEARVEEILEIVSEELR------SMGITDlpGGFVLT 325
Cdd:PRK13928  207 KIKIGTAFPG--AREEEMEIRgrdlVTGLPKTITVTSEEIREALKEPVSAIVQAVKSVLErtppelSADIID--RGIIMT 282

                         170       180
                  ....*....|....*....|....
gi 1036600687 326 GGQAAMPGVMSLAQDVLQNNVRVA 349
Cdd:PRK13928  283 GGGALLHGLDKLLAEETKVPVYIA 306
PRK13929 PRK13929
rod-share determining protein MreBH; Provisional
 169-348 3.89e-06

rod-share determining protein MreBH; Provisional


Pssm-ID: 184403 [Multi-domain]  Cd Length: 335  Bit Score: 48.75  E-value: 3.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 169 LLRCVERAGIEITDICLQPLAAG-SAALSKDEKNLGVaLIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDIS----- 242
Cdd:PRK13929  117 ISDAVKNCGAKNVHLIEEPVAAAiGADLPVDEPVANV-VVDIGGGTTEVAIISFGGVVSCHSIRIGGDQLDEDIVsfvrk 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 243 -----IGLRTsteeAERVKKQFGHAYYDEasEDEVFEVT----VIGTNQKQTFTQQEAANIIEARVEEILEIVSEELR-- 311
Cdd:PRK13929  196 kynllIGERT----AEQVKMEIGYALIEH--EPETMEVRgrdlVTGLPKTITLESKEIQGAMRESLLHILEAIRATLEdc 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1036600687 312 ----SMGITDLpgGFVLTGGQAAMPGVmslaQDVLQNNVRV 348
Cdd:PRK13929  270 ppelSGDIVDR--GVILTGGGALLNGI----KEWLSEEIVV 304
eutA PRK10719
ethanolamine ammonia-lyase reactivating factor EutA;
190-234 1.16e-05

ethanolamine ammonia-lyase reactivating factor EutA;


Pssm-ID: 236743 [Multi-domain]  Cd Length: 475  Bit Score: 47.56  E-value: 1.16e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1036600687 190 AGSAALSKdEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGG 234
Cdd:PRK10719  135 AGAQTLSE-ERNTRVLNIDIGGGTANYALFDAGKVIDTACLNVGG 178
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 174-334 1.36e-05

Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 47.12  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 174 ERAGIEITDICLQPLAA----GSAALSKDEKnlgVALIDIGGGSTTIAV--FQNGH---LTSTRVIPLGGENIT------ 238
Cdd:COG0443   135 RIAGLEVLRLLNEPTAAalayGLDKGKEEET---ILVYDLGGGTFDVSIlrLGDGVfevLATGGDTHLGGDDFDqalady 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 239 ------KDISIGLRTS-------TEEAERVKKQFghayydeaSEDEVFEVTV---IGTNQKQTFTQQEAANIIEARVEEI 302
Cdd:COG0443   212 vapefgKEEGIDLRLDpaalqrlREAAEKAKIEL--------SSADEAEINLpfsGGKHLDVELTRAEFEELIAPLVERT 283

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1036600687 303 LEIVSEELRSMGIT-DLPGGFVLTGGQAAMPGV 334
Cdd:COG0443   284 LDPVRQALADAGLSpSDIDAVLLVGGSTRMPAV 316
EutA pfam06277
Ethanolamine utilization protein EutA; This family consists of several bacterial EutA ...
 190-234 2.11e-05

Ethanolamine utilization protein EutA; This family consists of several bacterial EutA ethanolamine utilization proteins. The EutA protein is thought to protect the lyase (EutBC) from inhibition by CNB12.


Pssm-ID: 377642  Cd Length: 475  Bit Score: 46.47  E-value: 2.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1036600687 190 AGSAALSKdEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGG 234
Cdd:pfam06277 132 AGAAAYSK-EHHTRVLNIDIGGGTSNIALFKAGEVIDTACLDVGG 175
ASKHA_NBD_HpPPX-GppA-like cd24052
nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine ...
 206-257 1.12e-04

nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (HpPPX/GppA) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds a group of proteins similar to Helicobacter pylori PPX/GppA (HpPPX/GppA). HpPPX/GppA is phylogenetically distant from the Escherichia coli homologs. Unlike E. coli that possesses two homologs, EcGppA and EcPPX, H. pylori encodes only one PPX/GppA homolog, HpPPX/GppA. As such, HpPPX/GppA may play important roles in the homeostasis of both (p)ppGpp and PolyP.


Pssm-ID: 466902 [Multi-domain]  Cd Length: 298  Bit Score: 44.01  E-value: 1.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036600687 206 LIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIGLRTSTEEAERVKK 257
Cdd:cd24052   128 VVDIGGGSTELVLFKNGKIKESISLPLGSLRLYERFVSGILPTEKELKKIRK 179
ASKHA_NBD_PPX_GppA cd24006
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ...
 198-313 1.46e-04

nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GppA) domain family; Members of the PPX/GppA family are involved in bacterial survival and metabolism. They may play distinct biochemical roles involved in polyphosphate and (p)ppGpp metabolic pathways. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Some bacteria, such as Escherichia coli, possesses two homologs, EcGppA and EcPPX. Some others, such as Helicobacter pylori and Aquifex aeolicus, encode only one PPX/GppA homolog, which may play important roles in the homeostasis of both (p)ppGpp and PolyP. The PPX/GppA family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466856 [Multi-domain]  Cd Length: 294  Bit Score: 43.29  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 198 DEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIGLRTSTEEAERVKKqFGHAYYDEASEDEVFEVTV 277
Cdd:cd24006   122 PLGDGNALIVDIGGGSTELTLGDNGEILFSESLPLGAVRLTERFLKDDPPSELLEEYLRS-FVRSVLRPLPKRRKIKFDV 200

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1036600687 278 -IGTN------QKQTFTQQEAANIIEARVEEILEIVsEELRSM 313
Cdd:cd24006   201 aIGSGgtilalAAMALARKGKPHGYEISREELKALY-DELLRL 242
ASKHA_NBD_HSP70_DnaK_HscA_HscC cd24029
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ...
 174-344 1.33e-03

nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and similar proteins; Escherichia coli DnaK, also called heat shock 70 kDa protein/HSP70, plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Moreover, DnaK participates actively in the response to hyperosmotic shock. Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. The family also includes Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.


Pssm-ID: 466879 [Multi-domain]  Cd Length: 351  Bit Score: 40.64  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 174 ERAGIEITDICLQPLAA----GSAALSKDEKnlgVALIDIGGGSTTIAVF--QNGHLtstRVIP------LGGENITK-- 239
Cdd:cd24029   134 ELAGLNVLRLINEPTAAalayGLDKEGKDGT---ILVYDLGGGTFDVSILeiENGKF---EVLAtggdnfLGGDDFDEai 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 240 --------DISIGLRTSTE----------EAERVKKQFghAYYDEASEDEVFEvtVIGTNQKQTFTQQEAANIIEARVEE 301
Cdd:cd24029   208 aelilekiGIETGILDDKEderararlreAAEEAKIEL--SSSDSTDILILDD--GKGGELEIEITREEFEELIAPLIER 283

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1036600687 302 ILEIVSEELRSMGIT-DLPGGFVLTGGQAAMPGVMSLAQDVLQN 344
Cdd:cd24029   284 TIDLLEKALKDAKLSpEDIDRVLLVGGSSRIPLVREMLEEYFGR 327
ASKHA_NBD_HSP70_HscA cd10236
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ...
 176-334 2.29e-03

nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar proteins; Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HscA's partner J-domain protein is HscB; it does not appear to require a NEF and has been shown to be induced by cold-shock. The HscA-HscB chaperone/co-chaperone pair is involved in [Fe-S] cluster assembly.


Pssm-ID: 466834 [Multi-domain]  Cd Length: 367  Bit Score: 39.89  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 176 AGIEITDICLQPLAAgSAALSKDEKNLGV-ALIDIGGGSTTIA-------VFQ----NGHLTstrvipLGG--------E 235
Cdd:cd10236   159 AGLNVLRLLNEPTAA-ALAYGLDQKKEGTiAVYDLGGGTFDISilrlsdgVFEvlatGGDTA------LGGddfdhllaD 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 236 NITKDISIGLRTSTEE-------AERVKKQFghAYYDEASEdevfEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSE 308
Cdd:cd10236   232 WILKQIGIDARLDPAVqqallqaARRAKEAL--SDADSASI----EVEVEGKDWEREITREEFEELIQPLVKRTLEPCRR 305

                         170       180
                  ....*....|....*....|....*..
gi 1036600687 309 ELRSMGIT-DLPGGFVLTGGQAAMPGV 334
Cdd:cd10236   306 ALKDAGLEpADIDEVVLVGGSTRIPLV 332
ASKHA_NBD_ParM-like cd10227
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ...
 153-239 2.52e-03

nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466825 [Multi-domain]  Cd Length: 263  Bit Score: 39.43  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 153 EVEGTLITGSKTILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLG----VALIDIGGGSTTIAVFQNG--HLTS 226
Cdd:cd10227   110 EEKKELKKKLLKGLHEFTFNGKERRITINDVKVLPEGAGAYLDYLLDDDELedgnVLVIDIGGGTTDILTFENGkpIEES 189

                          90
                  ....*....|...
gi 1036600687 227 TRVIPLGGENITK 239
Cdd:cd10227   190 SDTLPGGEEALEK 202
ASKHA_NBD_ParM_R1-like cd24022
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ...
 168-361 4.54e-03

nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and similar proteins from ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Escherichia coli ParM, also called ParA locus 36 kDa protein, or protein StbA. It is a plasmid-encoded protein involved in the control of plasmid partition and required for accurate segregation of low-copy-number plasmid R1.


Pssm-ID: 466872 [Multi-domain]  Cd Length: 324  Bit Score: 38.79  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 168 NLLRCVERAG----IEITDICLQP--LAAGSAALSKDEKNL--------GVALIDIGGGSTTIAVFQNG----HLTSTrV 229
Cdd:cd24022   126 NLKKPVTLLGgkspATIVSVKVMPegVAAYFDYLLDEDGNGtdeeeeegPVAVIDIGGTTTDIAVVSGGlsidHARSG-T 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036600687 230 IPLGGENITKDIsiglrtsteeAERVKKQFGHAYYDEASEDEVFEVTVIGTNQKQtftQQEAANIIEARVEEILEIVSEE 309
Cdd:cd24022   205 IELGVLDVRDAL----------KDALKKRFGLSSISDAELDRALRTGKFRLNGGK---EVDVSDLVNEAIAEVAERILNE 271

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1036600687 310 L-RSMGITDLPGGFVLTGGQAAmpgvmsLAQDVLQNNVRvasPNYIGVRDPQY 361
Cdd:cd24022   272 IkRRLGDASDLDRVIFVGGGAE------LLEDELKEALG---PNAIIVDEPEF 315
ASKHA_NBD_FGGY_RhaB-like cd07771
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ...
 7-65 9.33e-03

nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.


Pssm-ID: 466791 [Multi-domain]  Cd Length: 460  Bit Score: 38.28  E-value: 9.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036600687   7 YVSLDIGTSNTKVIVGEMTDDSLNIIGVGNVPSEGLKKGSIV--DID----ETVHSIRKAFDQAE 65
Cdd:cd07771     2 YLAVDLGASSGRVILGSLDGGKLELEEIHRFPNRPVEINGHLywDIDrlfdEIKEGLKKAAEQGG 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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