NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1278198227|gb|PIX61700|]
View 

MAG: hypothetical protein COZ47_00545 [Lysobacterales bacterium CG_4_10_14_3_um_filter_64_11]

Protein Classification

PBP2_phosphate_like_1 and OmpA_C-like domain-containing protein( domain architecture ID 10194588)

PBP2_phosphate_like_1 and OmpA_C-like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 18-292 4.80e-71

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


:

Pssm-ID: 270371 [Multi-domain]  Cd Length: 240  Bit Score: 224.76  E-value: 4.80e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  18 AADLRIHGSNTIgERLAPALvsdwlqAEGYheiaseqtafeetliraARDGQSISIEIHAHGSGTSARDLIAGTADIGMS 97
Cdd:cd13653     1 SGTITISGSTTV-APLAEAL------AEAF-----------------MEKHPGVRIEVQGGGSGTGIKALIEGTADIGMA 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  98 SRPIKADEAGAANAAglgqldmpaHELVLALDGLSVVVHPDSPLAHIEKGTIRRIFSGQFSDWSQLGLPRGRIALHARDD 177
Cdd:cd13653    57 SRPLKAEEKAAASGL---------VEHVIALDGIAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 178 KSGTWDSFRAMVLGDAPLSPRAKRYESTAKLAAAVASDPLAIGFVGMSEV--KGVKALAVsDGapaVTPDTFHVAVEDYP 255
Cdd:cd13653   128 GSGTRETFEELVLGKKDFAKNAVVVPSNGAVVQAVAKNPNAIGYVSLGYVddSKVKALSV-DG---VAPTPENIKSGKYP 203

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1278198227 256 LARRLYFYLPAKSSDLAQRFVAFSLSDRAQQIVERIG 292
Cdd:cd13653   204 LSRPLYLYTKGEPSGLVKAFIDFALSPEGQAIVEKLG 240
OmpA_C-like cd07185
Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; ...
 324-430 1.59e-18

Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.


:

Pssm-ID: 143586 [Multi-domain]  Cd Length: 106  Bit Score: 80.68  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 324 SLNFRFGSGSSFLDSKAMRDVDRLAQFVRKpeNADKELRLVGFvaADEVLPYSA-WSLSNDRADFIAEQLGAREVPVAR- 401
Cdd:cd07185     1 LITIYFDFGSAELTPEAKPLLDKLAEVLKK--NPDAKIRIEGH--TDSRGSDAYnQELSERRAEAVADYLVSKGVDASRi 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1278198227 402 -VRGMGGAVPVAANDSDIGRNRNRRVEVWL 430
Cdd:cd07185    77 tAVGYGESRPIASNDTEEGRAKNRRVEIVI 106
 
Name Accession Description Interval E-value
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 18-292 4.80e-71

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270371 [Multi-domain]  Cd Length: 240  Bit Score: 224.76  E-value: 4.80e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  18 AADLRIHGSNTIgERLAPALvsdwlqAEGYheiaseqtafeetliraARDGQSISIEIHAHGSGTSARDLIAGTADIGMS 97
Cdd:cd13653     1 SGTITISGSTTV-APLAEAL------AEAF-----------------MEKHPGVRIEVQGGGSGTGIKALIEGTADIGMA 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  98 SRPIKADEAGAANAAglgqldmpaHELVLALDGLSVVVHPDSPLAHIEKGTIRRIFSGQFSDWSQLGLPRGRIALHARDD 177
Cdd:cd13653    57 SRPLKAEEKAAASGL---------VEHVIALDGIAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 178 KSGTWDSFRAMVLGDAPLSPRAKRYESTAKLAAAVASDPLAIGFVGMSEV--KGVKALAVsDGapaVTPDTFHVAVEDYP 255
Cdd:cd13653   128 GSGTRETFEELVLGKKDFAKNAVVVPSNGAVVQAVAKNPNAIGYVSLGYVddSKVKALSV-DG---VAPTPENIKSGKYP 203

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1278198227 256 LARRLYFYLPAKSSDLAQRFVAFSLSDRAQQIVERIG 292
Cdd:cd13653   204 LSRPLYLYTKGEPSGLVKAFIDFALSPEGQAIVEKLG 240
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 17-309 6.61e-57

ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 189.32  E-value: 6.61e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  17 HAADLRIHGSNTigerLAPaLVSDWlqAEGYHEIASEqtafeetliraardgqsISIEIHAHGSGTSARDLIAGTADIGM 96
Cdd:COG0226     2 ASGTITIAGSST----VYP-LAEAW--AEAFQKANPG-----------------VTINVQSGGSGGGIKQFIAGTVDIGN 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  97 SSRPIKADEAGAANAAGLgqldmPAHELVLALDGLSVVVHPDSPLAHIEKGTIRRIFSGQFSDWSQLG--LPRGRIALHA 174
Cdd:COG0226    58 SSRPLKDEELEAAKENGV-----ELVEIPVAIDGIAVVVNPDNPVKNLTGEQLADIFSGKITNWNDIGgkLPDEPITVVG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 175 RDDKSGTWDSFRAMVLG-DAPLSPRAKRYESTAKLAAAVASDPLAIGFVGMSEVK--GVKALAVSDGA-PAVTPDTFHVA 250
Cdd:COG0226   133 RSDGSGTTDYFTEYLLGvGAEVREGVEGAEGNEGVVQAVAQTPGAIGYVGLSYAEqnKLKALAIDNKAgKFVEPTAENIA 212

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278198227 251 VEDYPLARRLYFYL---PAKSSDLAQRFVAFSLSDRAQQIVERIGFVsqyikPYPAVVRSDA 309
Cdd:COG0226   213 AGSYPLSRPLYIYVkkePDAKAPAVKAFLDFVLSDGGQKIVEKLGYV-----PLPDAVVEKV 269
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
 20-294 2.54e-39

phosphate binding protein; Members of this family are phosphate-binding proteins. Most are found in phosphate ABC-transporter operons, but some are found in phosphate regulatory operons. This model separates members of the current family from the phosphate ABC transporter phosphate binding protein described by TIGRFAMs model TIGR00975. [Transport and binding proteins, Anions]


Pssm-ID: 273991 [Multi-domain]  Cd Length: 287  Bit Score: 143.35  E-value: 2.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  20 DLRIHGSNTigerLAPaLVSDWlqAEGYHEIASeqtafeetliraardgqSISIEIHAHGSGTSARDLIAGTADIGMSSR 99
Cdd:TIGR02136  37 TITIDGSTT----VAP-LAEAA--AEEFQKIHP-----------------GVSVTVQGAGSGTGIKALINGTVDIGNSSR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 100 PIKADEAGAANAAGLGQLdmpahELVLALDGLSVVVHP-DSPLAHIEKGTIRRIFSGQFSDWSQLG--LPRGRIALHARD 176
Cdd:TIGR02136  93 PIKDEELQKDKQKGIKLI-----EHKVAVDGLAVVVNKkNVPVDDLTVEQLKKIYSGEITNWKEVGgdLPNKPIVVVGRN 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 177 DKSGTWDSFRAMVLGDAPLSPRAKRYESTAKLAAAVASDPLAIGFVGMSEV-KGVKALAVsdgaPAVTPDTFHVAVEDYP 255
Cdd:TIGR02136 168 AGSGTRDTFEEEVMGKAKIKPGKNEQESNGAVVSIVSSNPGAIGYLGLGYVdDSVKTLKV----NGVEPSKENIANGSYP 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1278198227 256 LARRLYFYLPAKSSD--LAQRFVAFSLSDRAQQ-IVERIGFV 294
Cdd:TIGR02136 244 LSRPLFMYVNGKPKKpeLVAEFIDFVLSDDGGErIVEELGYV 285
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 52-283 5.71e-26

PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 106.09  E-value: 5.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  52 SEQTAFEETLIRAARDGQSISIEIHAHGSGTSARDLIAGTADIGMSSRPIKADEAGAANAAGLGqldmPAHELVLALDGL 131
Cdd:pfam12849  19 TQAPGLLDLAEAFEKKYPGAKVKVTSVGSGEGIKALLNGDVDVALVSRPLTEEEFEAFGANGAG----GLVEVPVAYDGI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 132 SVVVHPDSPLAHIEKGTIRRIFSGQFSDWSQlGLPRGRIALHARDDKSGTWDSFRAMvLGDAPLSPRAKRYESTAKLAAA 211
Cdd:pfam12849  95 AIVVNKDNPANILTVEALKKIFSGKITNWND-GGPDGPIKFVSRGDNSGTTELFSTH-LKEKGPWGAAGIGAAGSPGVAS 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 212 VASDPLAIGFVGMSE--------------------VKGVKALAVSDGAPAVTPDTFHVAVEDYPLARRLYFYL---PAKS 268
Cdd:pfam12849 173 VVAGPGAIGYVEVSYalanlgytladvaggtylsfAKALKVAKINPGAGLVIPLEEAIADGDYPLSRPYYVIVknpPKGP 252

                         250
                  ....*....|....*
gi 1278198227 269 SDLAQRFVAFSLSDR 283
Cdd:pfam12849 253 APLAKAFLDFLLSDE 267
OmpA_C-like cd07185
Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; ...
 324-430 1.59e-18

Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.


Pssm-ID: 143586 [Multi-domain]  Cd Length: 106  Bit Score: 80.68  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 324 SLNFRFGSGSSFLDSKAMRDVDRLAQFVRKpeNADKELRLVGFvaADEVLPYSA-WSLSNDRADFIAEQLGAREVPVAR- 401
Cdd:cd07185     1 LITIYFDFGSAELTPEAKPLLDKLAEVLKK--NPDAKIRIEGH--TDSRGSDAYnQELSERRAEAVADYLVSKGVDASRi 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1278198227 402 -VRGMGGAVPVAANDSDIGRNRNRRVEVWL 430
Cdd:cd07185    77 tAVGYGESRPIASNDTEEGRAKNRRVEIVI 106
MotB COG1360
Flagellar motor protein MotB [Cell motility];
329-437 8.62e-12

Flagellar motor protein MotB [Cell motility];


Pssm-ID: 440971 [Multi-domain]  Cd Length: 174  Bit Score: 63.32  E-value: 8.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 329 FGSGSSFLDSKAMRDVDRLAQFVRKPENadkELRLVGFVAADEV---LPYSAWSLSNDRADFIAEQLGAREVPVARVR-- 403
Cdd:COG1360    63 FDSGSAELTPEGRELLDKIAAVLAEVPN---RIRVEGHTDNVPIstaRFPSNWELSAARAAAVVRYLIEGGVPPERLSav 139

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1278198227 404 GMGGAVPVAANDSDIGRNRNRRVEVWLANRHTQD 437
Cdd:COG1360   140 GYGDTRPLAPNDTPEGRARNRRVEIVILRRAAEE 173
OmpA pfam00691
OmpA family; The Pfam entry also includes MotB and related proteins which are not included in ...
 329-423 6.80e-11

OmpA family; The Pfam entry also includes MotB and related proteins which are not included in the Prosite family.


Pssm-ID: 425825 [Multi-domain]  Cd Length: 95  Bit Score: 58.53  E-value: 6.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 329 FGSGSSFLDSKAMRDVDRLAQFVRKPENaDKELRLVGFvAADEVLPYSAWSLSNDRADFIAEQLGAREVPVAR--VRGMG 406
Cdd:pfam00691   1 FDPGSSQLTPKAKATLDEIADLLKFPEL-KNTITIEGH-TDTVGSAAYNWELSQRRAEAVRRYLVNFGVPPSRisVVGYG 78

                          90
                  ....*....|....*..
gi 1278198227 407 GAVPVAANDSDIGRNRN 423
Cdd:pfam00691  79 ATKPITDNKTPEGRARN 95
PRK07033 PRK07033
DotU family type VI secretion system protein;
376-430 2.68e-08

DotU family type VI secretion system protein;


Pssm-ID: 180801 [Multi-domain]  Cd Length: 427  Bit Score: 55.83  E-value: 2.68e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1278198227 376 SAWSLSNDRADFIAEQLGAREVPVARVR--GMGGAVPVAANDSDIGRNRNRRVEVWL 430
Cdd:PRK07033  365 SNWELSQARAQAVRALLAARLGQPERVTaeGRGDSDPVAPNDSAENRARNRRVEITL 421
type_VI_ompA TIGR03350
type VI secretion system peptidoglycan-associated domain; The flagellar motor protein MotB, ...
 376-428 5.45e-07

type VI secretion system peptidoglycan-associated domain; The flagellar motor protein MotB, the Gram-negative bacterial outer membrane protein OmpA (with an N-terminal outer membrane beta barrel domain) share a C-terminal peptidoglycan-associating homology region. This model describes a domain found fused to type VI secretion system homologs of the type IV system protein DotU (see model TIGR03349), with OmpA/MotB homology. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274533 [Multi-domain]  Cd Length: 137  Bit Score: 48.84  E-value: 5.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1278198227 376 SAWSLSNDRADFIAEQLGAREVPVARVR--GMGGAVPVAANDSDIGRNRNRRVEV 428
Cdd:TIGR03350  81 SNWHLSEARAKAVADVLAQAGGPAGRVRaeGRGDSEPIASNATAAGRARNRRVEI 135
 
Name Accession Description Interval E-value
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 18-292 4.80e-71

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270371 [Multi-domain]  Cd Length: 240  Bit Score: 224.76  E-value: 4.80e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  18 AADLRIHGSNTIgERLAPALvsdwlqAEGYheiaseqtafeetliraARDGQSISIEIHAHGSGTSARDLIAGTADIGMS 97
Cdd:cd13653     1 SGTITISGSTTV-APLAEAL------AEAF-----------------MEKHPGVRIEVQGGGSGTGIKALIEGTADIGMA 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  98 SRPIKADEAGAANAAglgqldmpaHELVLALDGLSVVVHPDSPLAHIEKGTIRRIFSGQFSDWSQLGLPRGRIALHARDD 177
Cdd:cd13653    57 SRPLKAEEKAAASGL---------VEHVIALDGIAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 178 KSGTWDSFRAMVLGDAPLSPRAKRYESTAKLAAAVASDPLAIGFVGMSEV--KGVKALAVsDGapaVTPDTFHVAVEDYP 255
Cdd:cd13653   128 GSGTRETFEELVLGKKDFAKNAVVVPSNGAVVQAVAKNPNAIGYVSLGYVddSKVKALSV-DG---VAPTPENIKSGKYP 203

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1278198227 256 LARRLYFYLPAKSSDLAQRFVAFSLSDRAQQIVERIG 292
Cdd:cd13653   204 LSRPLYLYTKGEPSGLVKAFIDFALSPEGQAIVEKLG 240
PBP2_phosphate cd13566
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 18-292 5.58e-69

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270284 [Multi-domain]  Cd Length: 245  Bit Score: 219.38  E-value: 5.58e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  18 AADLRIHGSNTIgERLAPALvsdwlqAEGYheiaseqtafeetliraARDGQSISIEIHAHGSGTSARDLIAGTADIGMS 97
Cdd:cd13566     1 SGTITIAGSSTV-APLAEAL------AEEF-----------------MKKHPGVRVTVQGGGSGAGIKALIAGTADIAMA 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  98 SRPIKADEAGAANAAGLGqldmpAHELVLALDGLSVVVHPDSPLAHIEKGTIRRIFSGQFSDWSQLGLPRGRIALHARDD 177
Cdd:cd13566    57 SRPLKDEEKAAAEANGIE-----LVEFVIAYDGIAVIVNPDNPVASLTLEQLRDIFTGKITNWSEVGGPDEPIVVYGRDE 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 178 KSGTWDSFRAMVLGDAPLSPRAKRYESTAKLAAAVASDPLAIGFVGMSEV---KGVKALAVSDGAPAVTpdtfHVAVEDY 254
Cdd:cd13566   132 GSGTRDYFEELVLGKGEFIRNAVVAPSNGALVQAVAGDPNAIGYVGLGYVdenKKVKALKVDGVAPTVE----NIKSGKY 207

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1278198227 255 PLARRLYFYLPAKSSDLAQRFVAFSLSDRAQQIVERIG 292
Cdd:cd13566   208 PLSRPLFLYTKGEPSPAVKAFIDFALSPEGQKIIEEVG 245
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 17-309 6.61e-57

ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 189.32  E-value: 6.61e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  17 HAADLRIHGSNTigerLAPaLVSDWlqAEGYHEIASEqtafeetliraardgqsISIEIHAHGSGTSARDLIAGTADIGM 96
Cdd:COG0226     2 ASGTITIAGSST----VYP-LAEAW--AEAFQKANPG-----------------VTINVQSGGSGGGIKQFIAGTVDIGN 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  97 SSRPIKADEAGAANAAGLgqldmPAHELVLALDGLSVVVHPDSPLAHIEKGTIRRIFSGQFSDWSQLG--LPRGRIALHA 174
Cdd:COG0226    58 SSRPLKDEELEAAKENGV-----ELVEIPVAIDGIAVVVNPDNPVKNLTGEQLADIFSGKITNWNDIGgkLPDEPITVVG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 175 RDDKSGTWDSFRAMVLG-DAPLSPRAKRYESTAKLAAAVASDPLAIGFVGMSEVK--GVKALAVSDGA-PAVTPDTFHVA 250
Cdd:COG0226   133 RSDGSGTTDYFTEYLLGvGAEVREGVEGAEGNEGVVQAVAQTPGAIGYVGLSYAEqnKLKALAIDNKAgKFVEPTAENIA 212

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278198227 251 VEDYPLARRLYFYL---PAKSSDLAQRFVAFSLSDRAQQIVERIGFVsqyikPYPAVVRSDA 309
Cdd:COG0226   213 AGSYPLSRPLYIYVkkePDAKAPAVKAFLDFVLSDGGQKIVEKLGYV-----PLPDAVVEKV 269
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
 20-294 2.54e-39

phosphate binding protein; Members of this family are phosphate-binding proteins. Most are found in phosphate ABC-transporter operons, but some are found in phosphate regulatory operons. This model separates members of the current family from the phosphate ABC transporter phosphate binding protein described by TIGRFAMs model TIGR00975. [Transport and binding proteins, Anions]


Pssm-ID: 273991 [Multi-domain]  Cd Length: 287  Bit Score: 143.35  E-value: 2.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  20 DLRIHGSNTigerLAPaLVSDWlqAEGYHEIASeqtafeetliraardgqSISIEIHAHGSGTSARDLIAGTADIGMSSR 99
Cdd:TIGR02136  37 TITIDGSTT----VAP-LAEAA--AEEFQKIHP-----------------GVSVTVQGAGSGTGIKALINGTVDIGNSSR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 100 PIKADEAGAANAAGLGQLdmpahELVLALDGLSVVVHP-DSPLAHIEKGTIRRIFSGQFSDWSQLG--LPRGRIALHARD 176
Cdd:TIGR02136  93 PIKDEELQKDKQKGIKLI-----EHKVAVDGLAVVVNKkNVPVDDLTVEQLKKIYSGEITNWKEVGgdLPNKPIVVVGRN 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 177 DKSGTWDSFRAMVLGDAPLSPRAKRYESTAKLAAAVASDPLAIGFVGMSEV-KGVKALAVsdgaPAVTPDTFHVAVEDYP 255
Cdd:TIGR02136 168 AGSGTRDTFEEEVMGKAKIKPGKNEQESNGAVVSIVSSNPGAIGYLGLGYVdDSVKTLKV----NGVEPSKENIANGSYP 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1278198227 256 LARRLYFYLPAKSSD--LAQRFVAFSLSDRAQQ-IVERIGFV 294
Cdd:TIGR02136 244 LSRPLFMYVNGKPKKpeLVAEFIDFVLSDDGGErIVEELGYV 285
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 52-283 5.71e-26

PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 106.09  E-value: 5.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  52 SEQTAFEETLIRAARDGQSISIEIHAHGSGTSARDLIAGTADIGMSSRPIKADEAGAANAAGLGqldmPAHELVLALDGL 131
Cdd:pfam12849  19 TQAPGLLDLAEAFEKKYPGAKVKVTSVGSGEGIKALLNGDVDVALVSRPLTEEEFEAFGANGAG----GLVEVPVAYDGI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 132 SVVVHPDSPLAHIEKGTIRRIFSGQFSDWSQlGLPRGRIALHARDDKSGTWDSFRAMvLGDAPLSPRAKRYESTAKLAAA 211
Cdd:pfam12849  95 AIVVNKDNPANILTVEALKKIFSGKITNWND-GGPDGPIKFVSRGDNSGTTELFSTH-LKEKGPWGAAGIGAAGSPGVAS 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 212 VASDPLAIGFVGMSE--------------------VKGVKALAVSDGAPAVTPDTFHVAVEDYPLARRLYFYL---PAKS 268
Cdd:pfam12849 173 VVAGPGAIGYVEVSYalanlgytladvaggtylsfAKALKVAKINPGAGLVIPLEEAIADGDYPLSRPYYVIVknpPKGP 252

                         250
                  ....*....|....*
gi 1278198227 269 SDLAQRFVAFSLSDR 283
Cdd:pfam12849 253 APLAKAFLDFLLSDE 267
PBP2_phosphate_like_2 cd13654
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 65-292 1.71e-25

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270372  Cd Length: 259  Bit Score: 104.64  E-value: 1.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  65 ARDGQSISIEIHAHGSGTSARDLIAGTADIGMSSRPIKadeagAANAAGLGQLDMPAHELVLALDGLSVVVHPDSPLA-- 142
Cdd:cd13654    24 GKSGPGVTVTVGSSGTGGGFKKFCAGETDISNASRPIK-----DSEAELCEANGIEYIELPVAYDGLTVVVNPANDWAkc 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 143 -HIEKGTIRRIFSGQFSDWSQL--GLPRGRIALHARDDKSGTWDSFRAMVLGDAplspRAKRYESTAK-----LAAAVAS 214
Cdd:cd13654    99 lTELELKSIWAAESPITTWSDVrpSWPDEPIELYGPGTDSGTFDYFTEAIVGEG----GSIREDYTASeddnvLVQGVAG 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 215 DPLAIGFVGMS---EVKG-VKALAVSDGAPAVTPDTFHVAV-EDYPLARRLYFYLPAKSSDLA---QRFVAFSLSDrAQQ 286
Cdd:cd13654   175 DKNALGFFGYAyyeENGDkLKAVKIDGGEGTVAPSAETTISgGYYPLSRPLFIYVKKASLAEKpavAAFVKFYLEN-AQE 253


                  ....*.
gi 1278198227 287 IVERIG 292
Cdd:cd13654   254 AAGEVG 259
OmpA_C-like cd07185
Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; ...
 324-430 1.59e-18

Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.


Pssm-ID: 143586 [Multi-domain]  Cd Length: 106  Bit Score: 80.68  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 324 SLNFRFGSGSSFLDSKAMRDVDRLAQFVRKpeNADKELRLVGFvaADEVLPYSA-WSLSNDRADFIAEQLGAREVPVAR- 401
Cdd:cd07185     1 LITIYFDFGSAELTPEAKPLLDKLAEVLKK--NPDAKIRIEGH--TDSRGSDAYnQELSERRAEAVADYLVSKGVDASRi 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1278198227 402 -VRGMGGAVPVAANDSDIGRNRNRRVEVWL 430
Cdd:cd07185    77 tAVGYGESRPIASNDTEEGRAKNRRVEIVI 106
OmpA COG2885
Outer membrane protein OmpA and related peptidoglycan-associated (lipo)proteins [Cell wall ...
 152-430 8.86e-16

Outer membrane protein OmpA and related peptidoglycan-associated (lipo)proteins [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442131 [Multi-domain]  Cd Length: 294  Bit Score: 77.52  E-value: 8.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 152 IFSGQFSDWSQLGLPRGRIALHARDDKSGTWDSFRAMVLGDAPLSPRAKRYESTAKLAAAVASDPLAIGFVGMSEVKGVK 231
Cdd:COG2885    14 DAAGGLLSGAALLLALLGVLGSAGGLLSLADDLAEASAGAAGGAAAGAEAGGLSAGLELLDAGSLSATAAAGAAALLVLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 232 ALAVSDGAPAVTPDTFHVAVEDYPLARRLYFYLPAKSSDLAQRFVAFSLSDRAQQIVERIGFVSQYIKPYPAVVRSDAPA 311
Cdd:COG2885    94 AALGALGAGLAALLLAIAAAASAAAADALALAAGAAAALGALGASAAAAAAALAAAKALGDSAAAALDAAAKAEAAAAAA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 312 DYRSIVQGAQRLSLNFRFGSGSSFLDSKAMRDVDRLAQFVRkpENADKELRLVGFvaADEVLPYSA-WSLSNDRADFIAE 390
Cdd:COG2885   174 ALLPAAVAEVVLLSNVYFDFDSAELTPEAKAALDELAALLK--ENPDLRIEIEGH--TDSRGSDAYnLALSERRAEAVKD 249

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1278198227 391 QLGAREVPVAR--VRGMGGAVPVAANDSDIGRNRNRRVEVWL 430
Cdd:COG2885   250 YLVSKGIPASRitAVGYGESRPVASNDTEEGRAKNRRVEIVV 291
MotB COG1360
Flagellar motor protein MotB [Cell motility];
329-437 8.62e-12

Flagellar motor protein MotB [Cell motility];


Pssm-ID: 440971 [Multi-domain]  Cd Length: 174  Bit Score: 63.32  E-value: 8.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 329 FGSGSSFLDSKAMRDVDRLAQFVRKPENadkELRLVGFVAADEV---LPYSAWSLSNDRADFIAEQLGAREVPVARVR-- 403
Cdd:COG1360    63 FDSGSAELTPEGRELLDKIAAVLAEVPN---RIRVEGHTDNVPIstaRFPSNWELSAARAAAVVRYLIEGGVPPERLSav 139

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1278198227 404 GMGGAVPVAANDSDIGRNRNRRVEVWLANRHTQD 437
Cdd:COG1360   140 GYGDTRPLAPNDTPEGRARNRRVEIVILRRAAEE 173
OmpA pfam00691
OmpA family; The Pfam entry also includes MotB and related proteins which are not included in ...
 329-423 6.80e-11

OmpA family; The Pfam entry also includes MotB and related proteins which are not included in the Prosite family.


Pssm-ID: 425825 [Multi-domain]  Cd Length: 95  Bit Score: 58.53  E-value: 6.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 329 FGSGSSFLDSKAMRDVDRLAQFVRKPENaDKELRLVGFvAADEVLPYSAWSLSNDRADFIAEQLGAREVPVAR--VRGMG 406
Cdd:pfam00691   1 FDPGSSQLTPKAKATLDEIADLLKFPEL-KNTITIEGH-TDTVGSAAYNWELSQRRAEAVRRYLVNFGVPPSRisVVGYG 78

                          90
                  ....*....|....*..
gi 1278198227 407 GAVPVAANDSDIGRNRN 423
Cdd:pfam00691  79 ATKPITDNKTPEGRARN 95
PBP2_phosphate_binding cd01006
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 75-289 1.21e-09

Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 periplasmic-binding fold superfamily; This phosphate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270227 [Multi-domain]  Cd Length: 253  Bit Score: 58.81  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  75 IHAHGSGTSA--RDLIAGTADIGMSSRPIKADEAGAANAaglgqldmpaHELVLALDGLSVVVHPDSPLAH--IEKGTIR 150
Cdd:cd01006    32 VAVQGVGSTAgiSQLKAGTVDIGASDAYLSESEAANKGL----------HTFTLAIDGLAIVVNQPGPVTNltLNGKQLY 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 151 RIFSGQFSDWSQLG---------LPRGRIALHARDDKSGTWDSFRAMV------------LGDAPLSPRAKRYESTAKLA 209
Cdd:cd01006   102 GIYKGQIKNWDDVGiaalnpgvnLPDQKIAVVTREDGSGTRFSFTSYLgktktekdgkgtTEVSDVAPTALGVNGNSG*K 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 210 AAVASDPLAIGFVGMSEVKGvKALAvsdgapavtpdtfhvAVEDYPLARRLYFYLPAKSSDLA-----QRFVAFSLSD-R 283
Cdd:cd01006   182 TLVNHNPGAVGYISIGSVDQ-SSLK---------------AIQLYPISRPFLILHYSDQKDAAtdeqtKEFIAWAKSEgA 245


                  ....*.
gi 1278198227 284 AQQIVE 289
Cdd:cd01006   246 AKLIVE 251
PRK07033 PRK07033
DotU family type VI secretion system protein;
376-430 2.68e-08

DotU family type VI secretion system protein;


Pssm-ID: 180801 [Multi-domain]  Cd Length: 427  Bit Score: 55.83  E-value: 2.68e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1278198227 376 SAWSLSNDRADFIAEQLGAREVPVARVR--GMGGAVPVAANDSDIGRNRNRRVEVWL 430
Cdd:PRK07033  365 SNWELSQARAQAVRALLAARLGQPERVTaeGRGDSDPVAPNDSAENRARNRRVEITL 421
PRK08126 PRK08126
hypothetical protein; Provisional
 380-431 2.79e-07

hypothetical protein; Provisional


Pssm-ID: 236157 [Multi-domain]  Cd Length: 432  Bit Score: 52.39  E-value: 2.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1278198227 380 LSNDRADFIAEQLGAREVPVARVR--GMGGAVPVAANDSDIGRNRNRRVEVWLA 431
Cdd:PRK08126  378 LSEKRAAQVAQMLQSAGVPASRLEavGKGDAQPVADNRTPQGRAQNRRVEITVA 431
motB PRK06667
flagellar motor protein MotB; Validated
 329-428 3.26e-07

flagellar motor protein MotB; Validated


Pssm-ID: 180652 [Multi-domain]  Cd Length: 252  Bit Score: 51.33  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 329 FGSGSSFLDSKAMRDV-DRLAQFVRKPENADKELRLVGFVAADEVLP----YSAWSLSNDRADFIAEQL---GAREVPVA 400
Cdd:PRK06667  129 FYPGSAEVKLEENRETlQKIASFIGFLDLAGRNFRIEGHTDNVDVNPegpwKSNWELSGARAVNMLEYIlnyGDQSESWF 208

                          90       100
                  ....*....|....*....|....*...
gi 1278198227 401 RVRGMGGAVPVAANDSDIGRNRNRRVEV 428
Cdd:PRK06667  209 QVSGFAGSRPLATEDTPEGRAYNRRIDI 236
type_VI_ompA TIGR03350
type VI secretion system peptidoglycan-associated domain; The flagellar motor protein MotB, ...
 376-428 5.45e-07

type VI secretion system peptidoglycan-associated domain; The flagellar motor protein MotB, the Gram-negative bacterial outer membrane protein OmpA (with an N-terminal outer membrane beta barrel domain) share a C-terminal peptidoglycan-associating homology region. This model describes a domain found fused to type VI secretion system homologs of the type IV system protein DotU (see model TIGR03349), with OmpA/MotB homology. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274533 [Multi-domain]  Cd Length: 137  Bit Score: 48.84  E-value: 5.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1278198227 376 SAWSLSNDRADFIAEQLGAREVPVARVR--GMGGAVPVAANDSDIGRNRNRRVEV 428
Cdd:TIGR03350  81 SNWHLSEARAKAVADVLAQAGGPAGRVRaeGRGDSEPIASNATAAGRARNRRVEI 135
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
 51-293 1.01e-06

ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440489 [Multi-domain]  Cd Length: 253  Bit Score: 49.87  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  51 ASEQTAFEETLIRAARDGQSISIEIHAHGSGTSARDLIAG-TADIGMSSRPikadeaGAANAAGLGQLDMPAHELVLALD 129
Cdd:COG0725    33 ASLKEALEELAAAFEKEHPGVKVELSFGGSGALARQIEQGaPADVFISADE------KYMDKLAKKGLILAGSRVVFATN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 130 GLSVVVHPDSPLahiekgtirrifsgQFSDWSQLGLPRGRIAL-HARDDKSG--TWDSFRAMVLGDApLSPRAKRYESTA 206
Cdd:COG0725   107 RLVLAVPKGNPA--------------DISSLEDLAKPGVRIAIgDPKTVPYGkyAKEALEKAGLWDA-LKPKLVLGENVR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 207 KLAAAVASDPLAIGFVGMSEvkgvkALAVSDGAPAVT-PDTFHVAVEdYPLArrlyfyLP--AKSSDLAQRFVAFSLSDR 283
Cdd:COG0725   172 QVLAYVESGEADAGIVYLSD-----ALAAKGVLVVVElPAELYAPIV-YPAA------VLkgAKNPEAAKAFLDFLLSPE 239

                         250
                  ....*....|
gi 1278198227 284 AQQIVERIGF 293
Cdd:COG0725   240 AQAILEKYGF 249
PRK10510 PRK10510
OmpA family lipoprotein;
380-431 1.27e-06

OmpA family lipoprotein;


Pssm-ID: 182507 [Multi-domain]  Cd Length: 219  Bit Score: 49.10  E-value: 1.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1278198227 380 LSNDRADFIAEQLGAREVPVARVR--GMGGAVPVAANDSDIGRNRNRRVEVWLA 431
Cdd:PRK10510  164 LSQQRADSVASALITQGVDASRIRtqGMGPANPIASNSTAEGKAQNRRVEITLS 217
PBP2_PstS cd13565
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 71-292 2.70e-06

Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 periplasmic-binding fold superfamily; This subfamily contians phosphate binding domain found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270283 [Multi-domain]  Cd Length: 254  Bit Score: 48.77  E-value: 2.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  71 ISIEIHAHGSGTSARDLIAGTADIGMSSRPIKadeagaanAAGLGQLDMPAHELVLALDGLSVVVH-PD-SPLAHIEKGT 148
Cdd:cd13565    30 VKINYQSIGSGAGIKQFIAGTVDFGASDAPLS--------DAELAKAGGGLLQIPTVIGAVVVAYNlPGvKGLLLLSGEV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 149 IRRIFSGQFSDWSQ---------LGLPRGRIALHARDDKSGT---------------WDSFRAmvlGDAPLSPRAKRYES 204
Cdd:cd13565   102 LADIFLGKITKWNDpaiaalnpgVNLPDTPITVVHRSDGSGTtfiftdylsavspewKDKVGA---GKSVAWPVGLGGKG 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 205 TAKLAAAVASDPLAIGFVGMSEVK--GVKALAVsdgapavtpdtfhvavedYPLARRLYFYLPAKSSDLAQ-----RFVA 277
Cdd:cd13565   179 NEGVAAAVKQTPGSIGYVELSYALqnGLPAAAL------------------YPIVGFTYILVKKDYKDAEKakavkKFLK 240

                         250
                  ....*....|....*
gi 1278198227 278 FSLSDrAQQIVERIG 292
Cdd:cd13565   241 WALTE-GQKFAADLG 254
motB PRK08457
flagellar motor protein MotB; Reviewed
 322-430 6.82e-06

flagellar motor protein MotB; Reviewed


Pssm-ID: 181435 [Multi-domain]  Cd Length: 257  Bit Score: 47.40  E-value: 6.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 322 RLSLNFRFGSGSSFLDSKAMRD-VDRLAQFVRK-PENADKELRlvGFVAADEVL---PYSAWSLSNDRADFIAEQLGARE 396
Cdd:PRK08457  119 KLPSKLLFENGSAEIINADMMDyLKRIAKIITKlPKQVKINVR--GYTDNSPLNksrYKDHYELAAARAYNVMKVLIQYG 196

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1278198227 397 VPVARVR--GMGGAVPVAANDSDIGRNRNRRVEVWL 430
Cdd:PRK08457  197 INPNRLSfsSYGSNNPIAPNDSLENRLKNNRVEIFF 232
motB PRK08944
flagellar motor protein MotB; Reviewed
 329-428 7.09e-06

flagellar motor protein MotB; Reviewed


Pssm-ID: 236356 [Multi-domain]  Cd Length: 302  Bit Score: 47.70  E-value: 7.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 329 FGSGSSFLDSKAMRDVDRLAQFVrkpenADKELRLV--GF---VAADEVLPYSAWSLSNDRADFIAEQLGA-REVPVAR- 401
Cdd:PRK08944  183 FPSGSAFLQPKFKPVVRKIGELL-----KDVPGIITvsGHtdnVPISSELYRSNWDLSSARAVAVAHELLKvKGFDPQRl 257

                          90       100
                  ....*....|....*....|....*...
gi 1278198227 402 -VRGMGGAVPVAANDSDIGRNRNRRVEV 428
Cdd:PRK08944  258 kVVGMADTQPLVPNDTAENRARNRRVEI 285
PRK09038 PRK09038
flagellar motor protein MotD; Reviewed
 329-428 1.83e-05

flagellar motor protein MotD; Reviewed


Pssm-ID: 181618 [Multi-domain]  Cd Length: 281  Bit Score: 46.16  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 329 FGSGSSFLDSKAMRDVDRLAQFVRKPENAdkeLRLVGFvaADEV------LPySAWSLSNDRADFIAEQLGAREVPVARV 402
Cdd:PRK09038  137 FGSGDAMLSDQAFAILEKVAEVLKPAPNP---IHVEGF--TDNVpiataqFP-SNWELSAARAASVVRLLADDGVAPSRL 210

                          90       100
                  ....*....|....*....|....*...
gi 1278198227 403 RGMG-GAV-PVAANDSDIGRNRNRRVEV 428
Cdd:PRK09038  211 AAVGyGEFqPVADNDTAEGRARNRRVVL 238
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 158-293 6.01e-04

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 41.10  E-value: 6.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 158 SDWSQLGLPRGRIAL-HARDDKSG--TWDSFRAMVLGDAPLSPRAKRYESTAKLAAAVASDPLAIGFVGMSEVKgvkALA 234
Cdd:pfam13531  93 SGLADLLKPGVRLAVaDPKTAPSGraALELLEKAGLLKALEKKVVVLGENVRQALTAVASGEADAGIVYLSEAL---FPE 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1278198227 235 VSDGAPAVTPDTFHVAVEDYPLARRLYfylpAKSSDLAQRFVAFSLSDRAQQIVERIGF 293
Cdd:pfam13531 170 NGPGLEVVPLPEDLNLPLDYPAAVLKK----AAHPEAARAFLDFLLSPEAQAILRKYGF 224
PRK09040 PRK09040
hypothetical protein; Provisional
 378-428 3.35e-03

hypothetical protein; Provisional


Pssm-ID: 181620 [Multi-domain]  Cd Length: 214  Bit Score: 38.84  E-value: 3.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1278198227 378 WSLSNDRADFIAEQLGAREVPVARV--RGMGGAVPVAANDSDIGRNRNRRVEV 428
Cdd:PRK09040  147 WELSAQRALTVTRALIDAGVPASSVfaAAFGSEQPVASNADDEGRAKNRRVEI 199
PBP2_CysL_like cd08420
C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which ...
 21-278 8.77e-03

C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which activates the transcription of the cysJI operon encoding sulfite reductase, contains the type 2 periplasmic binding fold; CysL, also known as YwfK, is a regular of sulfur metabolism in Bacillus subtilis. Sulfur is required for the synthesis of proteins and essential cofactors in all living organism. Sulfur can be assimilated either from inorganic sources (sulfate and thiosulfate), or from organic sources (sulfate esters, sulfamates, and sulfonates). CysL activates the transcription of the cysJI operon encoding sulfite reductase, which reduces sulfite to sulfide. Both cysL mutant and cysJI mutant are unable to grow using sulfate or sulfite as the sulfur source. Like other LysR-type regulators, CysL also negatively regulates its own transcription. In Escherichia coli, three LysR-type activators are involved in the regulation of sulfur metabolism: CysB, Cbl and MetR. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 176112 [Multi-domain]  Cd Length: 201  Bit Score: 37.47  E-value: 8.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227  21 LRIHGSNTIGERLAPALVSDWLQAegYHEiaseqtafeetliraardgqsISIEIHAHGSGTSARDLIAGTADIGMSSRP 100
Cdd:cd08420     2 LRIGASTTIGEYLLPRLLARFRKR--YPE---------------------VRVSLTIGNTEEIAERVLDGEIDLGLVEGP 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 101 IKADeagaanaaglgqldmpahELV---LALDGLSVVVHPDSPLAHIEKGTIRRIfsgqfsdwsqLGLPrgriaLHARDD 177
Cdd:cd08420    59 VDHP------------------DLIvepFAEDELVLVVPPDHPLAGRKEVTAEEL----------AAEP-----WILREP 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 178 KSGTWDSF-RAMVLGDAPLSPRAKRYE--STAKLAAAVASDpLAIGFVGMSEVKgvKALAvsDGAPAVtpdtfhVAVEDY 254
Cdd:cd08420   106 GSGTREVFeRALAEAGLDGLDLNIVMElgSTEAIKEAVEAG-LGISILSRLAVR--KELE--LGRLVA------LPVEGL 174

                         250       260
                  ....*....|....*....|....*.
gi 1278198227 255 PLARRLYF-YLPAKS-SDLAQRFVAF 278
Cdd:cd08420   175 RLTRPFSLiYHKDKYlSPAAEAFLEF 200
PRK09039 PRK09039
peptidoglycan -binding protein;
329-433 9.29e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.02  E-value: 9.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278198227 329 FGSGSSFLDSKAMRDVDRLAQFVRK-----PENADKELRLVGFvaADEVlPYSA-------WSLSNDRADFIAEQLGARE 396
Cdd:PRK09039  228 FPTGSAELNPEGQAEIAKLAAALIElakeiPPEINWVLRVDGH--TDNV-PLSGtgrfrdnWELSSARAISVVKFLIALG 304

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1278198227 397 VPVARV--RGMGGAVPVAANDSDIGRNRNRRVEVWLANR 433
Cdd:PRK09039  305 VPADRLaaAGFGEFQPLDPGDTPEARARNRRIELKLTER 343
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH