NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|324974707|gb|ADY53691|]
View 

efflux transporter, RND family, MFP subunit [Pseudopedobacter saltans DSM 12145]

Protein Classification

efflux RND transporter periplasmic adaptor subunit( domain architecture ID 11436533)

efflux RND (resistance-nodulation-division) transporter periplasmic adaptor subunit, similar to Bacillus subtilis YknX, which is part of an unusual four-component transporter with a role in protection against sporulation-delaying-protein-induced killing

CATH:  2.40.50.100|2.40.420.20|2.40.30.170|1.10.287.470
Gene Ontology:  GO:0016020|GO:0055085|GO:0022857|GO:0042802
PubMed:  32073314
TCDB:  2.A.6

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 43-370 4.43e-93

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


:

Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 281.45  E-value: 4.43e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  43 VTQEEVSGSENYPAVIVPINETELRAEVSGYITNIFVTDGASVAKGDRLYEIDGTRYAAAVDQAKANLKIAEANLDKVKR 122
Cdd:COG0845    3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 123 DVQRYRKLAEQDAIAKQTLDYAETDLNNQEAQVLAAKANLTTAATNLNRSVIRAPFSGTIGISQVRNGALVSAGTTLLnT 202
Cdd:COG0845   83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLF-T 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 203 ISTVNPITAEFQVPERNIAHFvslqKSGNQSALKLRLSDGQLFDgaGQIITIDRAVDEGTNTIKVRAKFNNPGNQLRAGM 282
Cdd:COG0845  162 IADLDPLEVEFDVPESDLARL----KVGQPVTVTLDAGPGKTFE--GKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGM 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 283 NATITVIEKSSTPELVIPYKAVQEQLGTYNVFVIGDSSKVQQRNISIGLKFEDKVVVKDGLKVGDKVVTEGVMNLKEGVK 362
Cdd:COG0845  236 FVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAK 315


                 ....*...
gi 324974707 363 VTEKSAGN 370
Cdd:COG0845  316 VRVVEAAA 323
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 43-370 4.43e-93

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 281.45  E-value: 4.43e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  43 VTQEEVSGSENYPAVIVPINETELRAEVSGYITNIFVTDGASVAKGDRLYEIDGTRYAAAVDQAKANLKIAEANLDKVKR 122
Cdd:COG0845    3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 123 DVQRYRKLAEQDAIAKQTLDYAETDLNNQEAQVLAAKANLTTAATNLNRSVIRAPFSGTIGISQVRNGALVSAGTTLLnT 202
Cdd:COG0845   83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLF-T 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 203 ISTVNPITAEFQVPERNIAHFvslqKSGNQSALKLRLSDGQLFDgaGQIITIDRAVDEGTNTIKVRAKFNNPGNQLRAGM 282
Cdd:COG0845  162 IADLDPLEVEFDVPESDLARL----KVGQPVTVTLDAGPGKTFE--GKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGM 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 283 NATITVIEKSSTPELVIPYKAVQEQLGTYNVFVIGDSSKVQQRNISIGLKFEDKVVVKDGLKVGDKVVTEGVMNLKEGVK 362
Cdd:COG0845  236 FVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAK 315


                 ....*...
gi 324974707 363 VTEKSAGN 370
Cdd:COG0845  316 VRVVEAAA 323
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 38-365 3.49e-80

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 248.38  E-value: 3.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707   38 VSAVEVTQEEVSGSENYPAVIVPINETELRAEVSGYITNIFVTDGASVAKGDRLYEIDGTRYAAAVDQAKANLKIAEANL 117
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  118 DKVKRDVQRYRKLAEQDAIAKQTLDYAETDLNNQEAQVLAAKANLTTAATNLNRSVIRAPFSGTIGISQVRNGALVSAGT 197
Cdd:TIGR01730  81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  198 TLLnTISTVNPITAEFQVPERniahFVSLQKSGNQSALKLRLSDGQLFDgaGQIITIDRAVDEGTNTIKVRAKFNNPGNQ 277
Cdd:TIGR01730 161 TLA-TIVDLDPLEADFSVPER----DLPQLRRGQTLTVELDALPGEEFK--GKLRFIDPRVDSGTGTVRVRATFPNPDGR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  278 LRAGMNATITVIEKSSTPELVIPYKAVQEQLGTYNVFVIGDSSKVQQRNISIGLKFEDKVVVKDGLKVGDKVVTEGVMNL 357
Cdd:TIGR01730 234 LLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKL 313


                  ....*...
gi 324974707  358 KEGVKVTE 365
Cdd:TIGR01730 314 RDGAKVKV 321
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
19-363 1.55e-48

MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 169.20  E-value: 1.55e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  19 QSCQNKGAQQ-GQQGEVAVPVSAVEVTQEEVSGSENYPAVIVPINETELRAEVSGYITNIFVTDGASVAKGDRLYEIDGT 97
Cdd:PRK11556  42 QAQQSPAGGRrGMRSGPLAPVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPR 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  98 RYAAAVDQAKANLKIAEANLDKVKRDVQRYRKLAEQDAIAKQTLDYAETDLNNQEAQVLAAKANLTTAATNLNRSVIRAP 177
Cdd:PRK11556 122 PFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAP 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 178 FSGTIGISQVRNGALVSAG-TTLLNTISTVNPITAEFQVPERNIAHFVSLQKSGNQSAL-------KLRLSDGQLFdgag 249
Cdd:PRK11556 202 ISGRVGLKQVDVGNQISSGdTTGIVVITQTHPIDLVFTLPESDIATVVQAQKAGKPLVVeawdrtnSKKLSEGTLL---- 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 250 qiiTIDRAVDEGTNTIKVRAKFNNPG-----NQLragMNATITVieksSTPE--LVIPYKAVQEQLGTYNVFVIGDSSKV 322
Cdd:PRK11556 278 ---SLDNQIDATTGTIKLKARFNNQDdalfpNQF---VNARMLV----DTLQnaVVIPTAALQMGNEGHFVWVLNDENKV 347

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 324974707 323 QQRNISIGLKFEDKVVVKDGLKVGDKVVTEGVMNLKEGVKV 363
Cdd:PRK11556 348 SKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKV 388
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 57-351 7.76e-30

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 116.75  E-value: 7.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707   57 VIVPINETELRAEVSGYITNIFVTDGASVAKGDRLYEIDGTRYAAAVDQAKANLKIAEANLDKVKRDVQRYRKLAEQDAI 136
Cdd:pfam00529  14 VVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  137 AKQTLDYAETDLNNQEAQVLAAKANLTTAATNLNRSVIRAPFSGTIGISQVRNGALVSAG-TTLLNTISTVNPITAEFQV 215
Cdd:pfam00529  94 SRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAqANLLATVAQLDQIYVQITQ 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  216 PERNIAHFVSLQKSG-------NQSALKLRLSDGQ------LFDGAGQIITIdrAVDEGTNTIKVRAKFNNPGNQL-RAG 281
Cdd:pfam00529 174 SAAENQAEVRSELSGaqlqiaeAEAELKLAKLDLErteiraPVDGTVAFLSV--TVDGGTVSAGLRLMFVVPEDNLlVPG 251

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 324974707  282 MNATiTVIEKSSTP-ELVIPYKAVQEQL-GTYNVFVIGDSSKVQQRNISIGLKFEDKVVVKDGLKVGDKVVT 351
Cdd:pfam00529 252 MFVE-TQLDQVRVGqPVLIPFDAFPQTKtGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 63-94 5.44e-04

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 37.78  E-value: 5.44e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 324974707  63 ETELRAEVSGYITNIFVTDGASVAKGDRLYEI 94
Cdd:cd06850   36 ENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 43-370 4.43e-93

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 281.45  E-value: 4.43e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  43 VTQEEVSGSENYPAVIVPINETELRAEVSGYITNIFVTDGASVAKGDRLYEIDGTRYAAAVDQAKANLKIAEANLDKVKR 122
Cdd:COG0845    3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 123 DVQRYRKLAEQDAIAKQTLDYAETDLNNQEAQVLAAKANLTTAATNLNRSVIRAPFSGTIGISQVRNGALVSAGTTLLnT 202
Cdd:COG0845   83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLF-T 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 203 ISTVNPITAEFQVPERNIAHFvslqKSGNQSALKLRLSDGQLFDgaGQIITIDRAVDEGTNTIKVRAKFNNPGNQLRAGM 282
Cdd:COG0845  162 IADLDPLEVEFDVPESDLARL----KVGQPVTVTLDAGPGKTFE--GKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGM 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 283 NATITVIEKSSTPELVIPYKAVQEQLGTYNVFVIGDSSKVQQRNISIGLKFEDKVVVKDGLKVGDKVVTEGVMNLKEGVK 362
Cdd:COG0845  236 FVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAK 315


                 ....*...
gi 324974707 363 VTEKSAGN 370
Cdd:COG0845  316 VRVVEAAA 323
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 38-365 3.49e-80

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 248.38  E-value: 3.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707   38 VSAVEVTQEEVSGSENYPAVIVPINETELRAEVSGYITNIFVTDGASVAKGDRLYEIDGTRYAAAVDQAKANLKIAEANL 117
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  118 DKVKRDVQRYRKLAEQDAIAKQTLDYAETDLNNQEAQVLAAKANLTTAATNLNRSVIRAPFSGTIGISQVRNGALVSAGT 197
Cdd:TIGR01730  81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  198 TLLnTISTVNPITAEFQVPERniahFVSLQKSGNQSALKLRLSDGQLFDgaGQIITIDRAVDEGTNTIKVRAKFNNPGNQ 277
Cdd:TIGR01730 161 TLA-TIVDLDPLEADFSVPER----DLPQLRRGQTLTVELDALPGEEFK--GKLRFIDPRVDSGTGTVRVRATFPNPDGR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  278 LRAGMNATITVIEKSSTPELVIPYKAVQEQLGTYNVFVIGDSSKVQQRNISIGLKFEDKVVVKDGLKVGDKVVTEGVMNL 357
Cdd:TIGR01730 234 LLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKL 313


                  ....*...
gi 324974707  358 KEGVKVTE 365
Cdd:TIGR01730 314 RDGAKVKV 321
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
19-363 1.55e-48

MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 169.20  E-value: 1.55e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  19 QSCQNKGAQQ-GQQGEVAVPVSAVEVTQEEVSGSENYPAVIVPINETELRAEVSGYITNIFVTDGASVAKGDRLYEIDGT 97
Cdd:PRK11556  42 QAQQSPAGGRrGMRSGPLAPVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPR 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  98 RYAAAVDQAKANLKIAEANLDKVKRDVQRYRKLAEQDAIAKQTLDYAETDLNNQEAQVLAAKANLTTAATNLNRSVIRAP 177
Cdd:PRK11556 122 PFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAP 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 178 FSGTIGISQVRNGALVSAG-TTLLNTISTVNPITAEFQVPERNIAHFVSLQKSGNQSAL-------KLRLSDGQLFdgag 249
Cdd:PRK11556 202 ISGRVGLKQVDVGNQISSGdTTGIVVITQTHPIDLVFTLPESDIATVVQAQKAGKPLVVeawdrtnSKKLSEGTLL---- 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 250 qiiTIDRAVDEGTNTIKVRAKFNNPG-----NQLragMNATITVieksSTPE--LVIPYKAVQEQLGTYNVFVIGDSSKV 322
Cdd:PRK11556 278 ---SLDNQIDATTGTIKLKARFNNQDdalfpNQF---VNARMLV----DTLQnaVVIPTAALQMGNEGHFVWVLNDENKV 347

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 324974707 323 QQRNISIGLKFEDKVVVKDGLKVGDKVVTEGVMNLKEGVKV 363
Cdd:PRK11556 348 SKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKV 388
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
1-370 3.42e-46

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 162.58  E-value: 3.42e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707   1 MNKIQ-LTALALV---GTGLFFQSCQNKGAQQGQQGEVAVPVsaVEVTQEEVSGSENYPAVIVPINETELRAEVSGYITN 76
Cdd:PRK15030   1 MNKNRgFTPLAVVlmlSGSLALTGCDDKQAQQGGQQMPAVGV--VTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  77 IFVTDGASVAKGDRLYEIDGTRYAAAVDQAKANLKIAEANLDKVKRDVQRYRKLAEQDAIAKQTLDYAETDLNNQEAQVL 156
Cdd:PRK15030  79 RNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 157 AAKANLTTAATNLNRSVIRAPFSGTIGISQVRNGALVSAG-TTLLNTISTVNPI-------TAEFQVPERNIAHFvSLQK 228
Cdd:PRK15030 159 AAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGqATALATVQQLDPIyvdvtqsSNDFLRLKQELANG-TLKQ 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 229 SGNQSALKLRLSDGQLFDGAGQIITIDRAVDEGTNTIKVRAKFNNPGNQLRAGMNATITVIEKSSTPELVIPYKAV-QEQ 307
Cdd:PRK15030 238 ENGKAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVtRTP 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 324974707 308 LGTYNVFVIGDSSKVQQRNISIGLKFEDKVVVKDGLKVGDKVVTEGVMNLKEG--VKVTEKSAGN 370
Cdd:PRK15030 318 RGDATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGvqVKAQEVTADN 382
PRK09859 PRK09859
multidrug transporter subunit MdtE;
1-368 5.90e-42

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 151.02  E-value: 5.90e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707   1 MNKIQLTALALVGTGLFFQSCQNKGAQQGQqgeVAVP-VSAVEVTQEEVSGSENYPAVIVPINETELRAEVSGYITNIFV 79
Cdd:PRK09859   1 MNRRRKLLIPLLFCGAMLTACDDKSAENAA---AMTPeVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  80 TDGASVAKGDRLYEIDGTRYAAAVDQAKANLKIAEANLDKVKRDVQRYRKLAEQDAIAKQTLDYAETDLNNQEAQVLAAK 159
Cdd:PRK09859  78 IEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 160 ANLTTAATNLNRSVIRAPFSGTIGISQVRNGALVSAGTT-LLNTISTVNPITAEFQvpeRNIAHFVSL---------QKS 229
Cdd:PRK09859 158 AAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQAdSLVTVQRLDPIYVDLT---QSVQDFLRMkeevasgqiKQV 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 230 GNQSALKLRLSDGQLFDGAGQIITIDRAVDEGTNTIKVRAKFNNPGNQLRAGMNATITVIEKSSTPELVIPYKAVQEQL- 308
Cdd:PRK09859 235 QGSTPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAq 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 309 GTYNVFVIGDSSKVQQRNISIGLKFEDKVVVKDGLKVGDKVVTEGVMNLKEGVKVTEKSA 368
Cdd:PRK09859 315 GKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISS 374
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
59-291 1.20e-36

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 135.18  E-value: 1.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  59 VPINETELRAEVSGYITNIFVTDGASVAKGDRLYEIDGTRYAAAVDQAKANLKIAEA----------------------- 115
Cdd:COG1566   41 VEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAqlarleaelgaeaeiaaaeaqla 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 116 ----NLDKVKRDVQRYRKLAEQDAIAKQTLDYAETDLNN---------------------------QEAQVLAAKANLTT 164
Cdd:COG1566  121 aaqaQLDLAQRELERYQALYKKGAVSQQELDEARAALDAaqaqleaaqaqlaqaqaglreeeelaaAQAQVAQAEAALAQ 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 165 AATNLNRSVIRAPFSGTIGISQVRNGALVSAGTTLLnTISTVNPITAEFQVPERNIAHFvslqKSGNQSALKLRLSDGQL 244
Cdd:COG1566  201 AELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLL-TIVPLDDLWVEAYVPETDLGRV----KPGQPVEVRVDAYPDRV 275

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 324974707 245 FDG--------AGQIITIDRAVDEGTNTIKVRAKFNNP-GNQLRAGMNATITVIEK 291
Cdd:COG1566  276 FEGkvtsispgAGFTSPPKNATGNVVQRYPVRIRLDNPdPEPLRPGMSATVEIDTE 331
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
6-370 1.75e-32

MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 125.29  E-value: 1.75e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707   6 LTALALVGtgLFFQSCQNKGaQQGQQGEVAVPVSAVEVTQEEVSGSENYPAVIVPINETELRAEVSGYITNIFVTDGASV 85
Cdd:PRK09578   9 LLLAALVA--LFVLAGCGKG-DSDAAAAAPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  86 AKGDRLYEIDGTRYAAAVDQAKANLKIAEANLDKVKRDVQRYRKLAEQDAIAKQTLDYAETDLNNQEAQVLAAKANLTTA 165
Cdd:PRK09578  86 KQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELARA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 166 ATNLNRSVIRAPFSGTIGISQVRNGALVSAGT-TLLNTISTVNPITAEFQVPERNIAHFVSLQKSG-------NQSALKL 237
Cdd:PRK09578 166 QLQLDYATVTAPIDGRARRALVTEGALVGQDQaTPLTTVEQLDPIYVNFSQPAADVEALRRAVKSGratgiaqQDVAVTL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 238 RLSDGQLFDGAGQIITIDRAVDEGTNTIKVRAKFNNPGNQLRAGMNATITVIEKSSTPELVIPYKAVQEQLGTYNVFVIG 317
Cdd:PRK09578 246 VRADGSEYPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVKVVG 325

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 324974707 318 DSSKVQQRNI-SIGLKFEDKVVVKdGLKVGDKVVTEGVMNLKEG--VKVTEKSAGN 370
Cdd:PRK09578 326 QNGKVRDVEVeADQMSGRDWIVTR-GLAGGERVIVDNAAQFAPGtaVKAVERAPAA 380
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 57-351 7.76e-30

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 116.75  E-value: 7.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707   57 VIVPINETELRAEVSGYITNIFVTDGASVAKGDRLYEIDGTRYAAAVDQAKANLKIAEANLDKVKRDVQRYRKLAEQDAI 136
Cdd:pfam00529  14 VVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  137 AKQTLDYAETDLNNQEAQVLAAKANLTTAATNLNRSVIRAPFSGTIGISQVRNGALVSAG-TTLLNTISTVNPITAEFQV 215
Cdd:pfam00529  94 SRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAqANLLATVAQLDQIYVQITQ 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  216 PERNIAHFVSLQKSG-------NQSALKLRLSDGQ------LFDGAGQIITIdrAVDEGTNTIKVRAKFNNPGNQL-RAG 281
Cdd:pfam00529 174 SAAENQAEVRSELSGaqlqiaeAEAELKLAKLDLErteiraPVDGTVAFLSV--TVDGGTVSAGLRLMFVVPEDNLlVPG 251

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 324974707  282 MNATiTVIEKSSTP-ELVIPYKAVQEQL-GTYNVFVIGDSSKVQQRNISIGLKFEDKVVVKDGLKVGDKVVT 351
Cdd:pfam00529 252 MFVE-TQLDQVRVGqPVLIPFDAFPQTKtGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 59-284 8.83e-18

Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.


Pssm-ID: 435440 [Multi-domain]  Cd Length: 214  Bit Score: 81.01  E-value: 8.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707   59 VPINETELR---AEVSGYITNIFV-TDGASVAKGDRLYEIdgtrYAAAVDQAKANLKIAEANLDKVKRDVQRYRklaeqd 134
Cdd:pfam16576  12 VAYDERRLAhvhARVEGWIEKLYVnATGDPVKKGQPLAEL----YSPELVAAQQEYLLALRSGDALSKSELLRA------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  135 aiAKQTLDYaetdLNNQEAQVlaakANLTTAATNLNRSVIRAPFSGTIGISQVRNGALVSAGTTLLnTISTVNPITAEFQ 214
Cdd:pfam16576  82 --ARQRLRL----LGMPEAQI----AELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLF-TIADLSTVWVEAD 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  215 VPERNIAhfvsLQKSGNQSALKLRLSDGQLFdgAGQIITIDRAVDEGTNTIKVRAKFNNPGNQLRAGMNA 284
Cdd:pfam16576 151 VPEQDLA----LVKVGQPAEVTLPALPGKTF--EGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
PRK10476 PRK10476
multidrug transporter subunit MdtN;
68-205 2.95e-16

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 78.92  E-value: 2.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  68 AEVSGYITNIFVTDGASVAKGDRLYEIDGTRYAAAVDQAKANLKIAEA----------------------------NLDK 119
Cdd:PRK10476  53 SEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAqimttqrsvdaersnaasaneqveraraNAKL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 120 VKRDVQRYRKLAEQDAIAKQTLDYAET------------------------DLNNQEAQVLAAKANLTTAATNLNRSVIR 175
Cdd:PRK10476 133 ATRTLERLEPLLAKGYVSAQQVDQARTaqrdaevslnqallqaqaaaaavgGVDALVAQRAAREAALAIAELHLEDTTVR 212

                        170       180       190
                 ....*....|....*....|....*....|
gi 324974707 176 APFSGTIGISQVRNGALVSAGTTLLNTIST 205
Cdd:PRK10476 213 APFDGRVVGLKVSVGEFAAPMQPIFTLIDT 242
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
69-198 3.64e-16

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 78.24  E-value: 3.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  69 EVSGYITNIFVTDGASVAKGDRLYEIDGTRYAAAVDQAKANLKIAEANLDKVKRDVQRYRKLAEQdAIAKQTLDYAETDL 148
Cdd:PRK10559  53 DVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRLGVQ-AMSREEIDQANNVL 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 324974707 149 NNQEAQVLAAKANLTTAATNLNRSVIRAPFSGTIGISQVRNGALVSAGTT 198
Cdd:PRK10559 132 QTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGST 181
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 68-351 4.20e-16

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 78.66  E-value: 4.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  68 AEVSGYITNIFVTDGASVAKGDRLYEIDGTR-------YAAAVDQAKANLKIAEANLDKVKRDVQRYRKLAEQDAIAKQT 140
Cdd:PRK11578  66 AQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQaenqikeVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQD 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 141 LDYAETDL-------NNQEAQVLAAKANLTTAATNLNRSVIRAPFSGTIGISQVRNGALVSAGTTLLN--TISTVNPITA 211
Cdd:PRK11578 146 LDTAATELavkqaqiGTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPNilTLADMSTMLV 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 212 EFQVPERNIAHFvslqKSGNQSALKLRLSDGQLFDgaGQIITIDRAVDEGTNTIKVRAKFN--NPGNQLRAGMNATITVI 289
Cdd:PRK11578 226 KAQVSEADVIHL----KPGQKAWFTVLGDPLTRYE--GVLKDILPTPEKVNDAIFYYARFEvpNPNGLLRLDMTAQVHIQ 299

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 324974707 290 EKSSTPELVIPYKAVQEQLGT--YNVFVIGDsSKVQQRNISIGLKFEDKVVVKDGLKVGDKVVT 351
Cdd:PRK11578 300 LTDVKNVLTIPLSALGDPVGDnrYKVKLLRN-GETREREVTIGARNDTDVEIVKGLEAGDEVII 362
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
 59-219 6.75e-16

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 77.69  E-value: 6.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  59 VPINETELRAEVSGYITNIFVTDGASVAKGDRLYEIDGTRYAAAVDQAKANLKIAEANLDKVK----------------- 121
Cdd:PRK03598  39 VDIRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLDLMLagyrdeeiaqaraavkq 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 122 ---------RDVQRYRKLAEQDAIAKQTLDYAET--------------------------DLNNQEAQVLAAKANLTTAA 166
Cdd:PRK03598 119 aqaaydyaqNFYNRQQGLWKSRTISANDLENARSsrdqaqatlksaqdklsqyregnrpqDIAQAKASLAQAQAALAQAE 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 324974707 167 TNLNRSVIRAPFSGTIgISQVR-NGALVSAGTTLLnTISTVNPITAEFQVPERN 219
Cdd:PRK03598 199 LNLQDTELIAPSDGTI-LTRAVePGTMLNAGSTVF-TLSLTRPVWVRAYVDERN 250
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
 171-354 2.53e-09

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 58.34  E-value: 2.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 171 RSVIRAPFSGTIGISQVRNGALVSAGTTLLNtISTVNPITAEFQVPErNIAHFVslqKSGNQSALKLRLSDGQLFDGAGQ 250
Cdd:PRK09783 209 RFTLKAPIDGVITAFDLRAGMNIAKDNVVAK-IQGMDPVWVTAAIPE-SIAWLV---KDASQFTLTVPARPDKTFTIRKW 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 251 iiTIDRAVDEGTNTIKVRAKFNNPGNQLRAGMNATITvIEKSSTPELVIPYKAVQEQLGTYNVFVIGDSSKVQQRNISIG 330
Cdd:PRK09783 284 --TLLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQ-LNTASEPMLLIPSQALIDTGSEQRVITVDADGRFVPKRVAVF 360

                        170       180
                 ....*....|....*....|....
gi 324974707 331 LKFEDKVVVKDGLKVGDKVVTEGV 354
Cdd:PRK09783 361 QESQGVTAIRSGLAEGEKVVSSGL 384
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 173-281 1.02e-08

HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.


Pssm-ID: 433206 [Multi-domain]  Cd Length: 104  Bit Score: 52.36  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  173 VIRAPFSGTIGISQVRNGALVSAGTTLLnTISTVNPITAEFQVPERNIAHFVSLQKsgnqsaLKLRLSDGQLFDGAGQII 252
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQVVQAGDPLA-TIVPPDRLLVEAFVPAADLGSLKKGQK------VTLKLDPGSDYTLEGKVV 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 324974707  253 TIDRAVDEGTNTIKVRAKFNNPGNQ--LRAG 281
Cdd:pfam13437  74 RISPTVDPDTGVIPVRVSIENPKTPipLLPG 104
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
65-111 8.86e-08

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 48.21  E-value: 8.86e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 324974707   65 ELRAEVSGYITNIFVTDGASVAKGDRLYEIDGTRYAAAVDQAKANLK 111
Cdd:pfam13533   4 KIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
62-207 1.57e-06

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 49.69  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  62 NETELRAEVSGYITNIFVTDGASVAKGDRLYEIDGTRYAAAVDQAK---------------------ANLKIAEANLDKV 120
Cdd:PRK15136  60 NQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKtalansvrqthqlminskqyqANIELQKTALAQA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707 121 KRDVQRYRKLAEQDAIAKQTLDYA--------------------------ETDLNNQEAqVLAAKANLTTAATNLNRSVI 174
Cdd:PRK15136 140 QSDLNRRVPLGNANLIGREELQHArdavasaqaqldvaiqqynanqamilNTPLEDQPA-VQQAATEVRNAWLALQRTKI 218

                        170       180       190
                 ....*....|....*....|....*....|...
gi 324974707 175 RAPFSGTIGISQVRNGALVSAGTTLLNTISTVN 207
Cdd:PRK15136 219 VSPMTGYVSRRSVQVGAQISPTTPLMAVVPATN 251
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
83-175 7.52e-05

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 44.26  E-value: 7.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  83 ASVAKGDRL--YEID-GTRYAAAVDQAKANLKIAEANLDKVKRDVQR--------YRKLAEQDAIAKQTLDYAE------ 145
Cdd:COG1538   30 LRQARAGLLpsQELDlGGKRRARIEAAKAQAEAAEADLRAARLDLAAevaqayfdLLAAQEQLALAEENLALAEellela 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 324974707 146 -----------TDLNNQEAQVLAAKANLTTAATNLNRSVIR 175
Cdd:COG1538  110 raryeaglasrLDVLQAEAQLAQARAQLAQAEAQLAQARNA 150
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
95-175 1.11e-04

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 43.87  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707  95 DGTRYAAAVDQAKANLKIAEANLDKVKRDV--------QRYRKLAEQDAIAKQTLDYAE-----------------TDLN 149
Cdd:COG1538  252 DGGRNRARVRAAKAQLEQAEAQYEQTVLQAlqevedalAALRAAREQLEALEEALEAAEealelararyraglaslLDVL 331

                         90       100
                 ....*....|....*....|....*.
gi 324974707 150 NQEAQVLAAKANLTTAATNLNRSVIR 175
Cdd:COG1538  332 DAQRELLQAQLNLIQARYDYLLALVQ 357
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
105-171 4.27e-04

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 41.95  E-value: 4.27e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 324974707 105 QAKANLKIAEANLDKVKRDVQRYRKLAEQDAIAKQTLDYAETDLNNQEAQVLAAKANLTTAATNLNR 171
Cdd:COG1538   87 AAQEQLALAEENLALAEELLELARARYEAGLASRLDVLQAEAQLAQARAQLAQAEAQLAQARNALAL 153
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 63-94 5.44e-04

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 37.78  E-value: 5.44e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 324974707  63 ETELRAEVSGYITNIFVTDGASVAKGDRLYEI 94
Cdd:cd06850   36 ENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
 72-170 2.07e-03

type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 130902 [Multi-domain]  Cd Length: 423  Bit Score: 39.99  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324974707   72 GYITNIFVTDGASVAKGDRLYEIDGTryaaavdQAKANLKIAEANLDKVKRDVQRYRKLAEQDAIAKQTLDYAETDLNNQ 151
Cdd:TIGR01843  52 GIVREILVREGDRVKAGQVLVELDAT-------DVEADAAELESQVLRLEAEVARLRAEADSQAAIEFPDDLLSAEDPAV 124

                          90
                  ....*....|....*....
gi 324974707  152 EAQVLAAKANLTTAATNLN 170
Cdd:TIGR01843 125 PELIKGQQSLFESRKSTLR 143
 
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