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Conserved domains on  [gi|704416921|ref|WP_033469113|]
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type IV pilus twitching motility protein PilT [Bordetella bronchiseptica]

Protein Classification

type IV pilus twitching motility protein PilT( domain architecture ID 10006640)

type IV pilus twitching motility protein PilT is a hexameric ATPase that drives pilus retraction, which provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility

CATH:  3.30.450.90
Gene Ontology:  GO:0005524|GO:0043107
PubMed:  12142488
SCOP:  4004005

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PilT COG2805
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ...
1-339 0e+00

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


:

Pssm-ID: 442056  Cd Length: 342  Bit Score: 585.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   1 MTIDELLALTVARGASDLHLSAGLPPMLRINGDVVRQDVAALTPDALRAMIHQLMQPAQREEYETRQELDFSIDVEGLAR 80
Cdd:COG2805    3 MDLDELLKLAVEQGASDLHLTVGSPPMLRIDGELVPLDDPPLTPEDLEALLKEILTEEQRERLEEEGELDFSYSLPGLGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  81 FRVNAFNQQRGPAAVLRTIPSAIRTLDELGCPASFKELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNREGEHHILTIED 160
Cdd:COG2805   83 FRVNIFRQRGGVAAVLRLIPSEIPTLEELGLPPVLKELAELPRGLVLVTGPTGSGKSTTLAAMIDYINETRAKHIITIED 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 161 PIEFVHPSRRSLVNQREVGRDTHSFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVDRI 240
Cdd:COG2805  163 PIEFVHKHKKSLINQREVGRDTPSFANALRAALREDPDVILVGEMRDLETIEAALTAAETGHLVFATLHTNSAAQTIDRI 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 241 IDVFPAGEKSMIRSMLSESLRAVIAQVLL-KQEGGGRCAAWEIMVGTPAIRNLIREDKIAQMVSSIQTGQAHSMQTLDQA 319
Cdd:COG2805  243 IDVFPPEEQAQIRSQLAESLRGVISQRLLpRADGGGRVAAREILVNTPAVRNLIREGKTHQIPSLIQTGKKLGMQTMDQS 322
                        330       340
                 ....*....|....*....|
gi 704416921 320 LQDLLRKKLISAEQALAYAR 339
Cdd:COG2805  323 LAELVKEGLITEETALAYAS 342
 
Name Accession Description Interval E-value
PilT COG2805
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ...
1-339 0e+00

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


Pssm-ID: 442056  Cd Length: 342  Bit Score: 585.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   1 MTIDELLALTVARGASDLHLSAGLPPMLRINGDVVRQDVAALTPDALRAMIHQLMQPAQREEYETRQELDFSIDVEGLAR 80
Cdd:COG2805    3 MDLDELLKLAVEQGASDLHLTVGSPPMLRIDGELVPLDDPPLTPEDLEALLKEILTEEQRERLEEEGELDFSYSLPGLGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  81 FRVNAFNQQRGPAAVLRTIPSAIRTLDELGCPASFKELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNREGEHHILTIED 160
Cdd:COG2805   83 FRVNIFRQRGGVAAVLRLIPSEIPTLEELGLPPVLKELAELPRGLVLVTGPTGSGKSTTLAAMIDYINETRAKHIITIED 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 161 PIEFVHPSRRSLVNQREVGRDTHSFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVDRI 240
Cdd:COG2805  163 PIEFVHKHKKSLINQREVGRDTPSFANALRAALREDPDVILVGEMRDLETIEAALTAAETGHLVFATLHTNSAAQTIDRI 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 241 IDVFPAGEKSMIRSMLSESLRAVIAQVLL-KQEGGGRCAAWEIMVGTPAIRNLIREDKIAQMVSSIQTGQAHSMQTLDQA 319
Cdd:COG2805  243 IDVFPPEEQAQIRSQLAESLRGVISQRLLpRADGGGRVAAREILVNTPAVRNLIREGKTHQIPSLIQTGKKLGMQTMDQS 322
                        330       340
                 ....*....|....*....|
gi 704416921 320 LQDLLRKKLISAEQALAYAR 339
Cdd:COG2805  323 LAELVKEGLITEETALAYAS 342
pilT_fam TIGR01420
pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to ...
2-341 0e+00

pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to GspE, a protein involved in type II secretion (also called the General Secretion Pathway). PilT is an apparent cytosolic ATPase associated with type IV pilus systems. It is not required for pilin biogenesis, but is required for twitching motility and social gliding behaviors, shown in some species, powered by pilus retraction. Members of this family may be found in some species that type IV pili but have related structures for DNA uptake and natural transformation. [Cell envelope, Surface structures, Cellular processes, Chemotaxis and motility]


Pssm-ID: 273613  Cd Length: 343  Bit Score: 519.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921    2 TIDELLALTVARGASDLHLSAGLPPMLRINGDVVRQDVAALTPDALRAMIHQLMQPAQREEYETRQELDFSIDVEGLARF 81
Cdd:TIGR01420   1 SLEEILREAVKLGASDIHLTAGAPPAMRIDGDLVRIEFEPLTPEDTQKLAREILSEKQREEFEENGELDFSFSLPGVGRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   82 RVNAFNQQRGPAAVLRTIPSAIRTLDELGCPASFKELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNREGEHHILTIEDP 161
Cdd:TIGR01420  81 RVNAFYQRGGVALVLRLIPSKIPTFEELGLPPVLRELAERPRGLILVTGPTGSGKSTTLASMIDYINKNKAYHIITIEDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  162 IEFVHPSRRSLVNQREVGRDTHSFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVDRII 241
Cdd:TIGR01420 161 IEYVHTNKRSLINQREVGEDTLSFANALRAALREDPDVILIGEMRDLETVELALTAAETGHLVFGTLHTNSAAQTIERII 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  242 DVFPAGEKSMIRSMLSESLRAVIAQVLL-KQEGGGRCAAWEIMVGTPAIRNLIREDKIAQMVSSIQTGQAHSMQTLDQAL 320
Cdd:TIGR01420 241 DVFPAEEQEQIRTQLAESLVAIISQRLLpKADGGGRVLAVEILINTPAVRNLIREGKTHQIKSLIQTGQQLGMQTFDQHL 320
                         330       340
                  ....*....|....*....|.
gi 704416921  321 QDLLRKKLISAEQALAYARDR 341
Cdd:TIGR01420 321 AQLYKKGLITLEDALEAAPSP 341
PilT cd01131
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ...
103-323 2.61e-136

Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility.


Pssm-ID: 410875 [Multi-domain]  Cd Length: 223  Bit Score: 386.51  E-value: 2.61e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 103 IRTLDELGCPASFKELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNREGEHHILTIEDPIEFVHPSRRSLVNQREVGRDT 182
Cdd:cd01131    1 IPTFEELGLPPVLKDLALKPRGLVLVTGPTGSGKSTTLAAMIDYINETRSKHIITIEDPIEFVHKHKKSLINQREVGRDT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 183 HSFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVDRIIDVFPAGEKSMIRSMLSESLRA 262
Cdd:cd01131   81 ESFAAALRAALREDPDVILVGEMRDLETIELALTAAETGHLVFSTLHTNSAAQTIDRIIDVFPPEQQEQVRIQLASSLRG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 704416921 263 VIAQVLL-KQEGGGRCAAWEIMVGTPAIRNLIREDKIAQMVSSIQTGQAHSMQTLDQALQDL 323
Cdd:cd01131  161 VISQRLLpKKDGGGRVAAFEILINTPAIRNLIREGKTHQIPSLIQTGARDGMQTMDQSLYEL 222
T2SSE pfam00437
Type II/IV secretion system protein; This family contains components of both the Type II ...
11-268 3.17e-52

Type II/IV secretion system protein; This family contains components of both the Type II protein secretion system (T2SS), including Type 4 pilus (T4P), and Type IV protein secretion system (T4SS) from Gram-negative bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection. The cytoplasmic T2S E ATPase is a Zn-containing protein thought to provide the mechanical force for the secretion process. T2S-E contains Walker A and B motifs, that are essential for secretion and ATPase activity. ATPase PulE and XcpR from Klebsiella oxytoca and Pseudomonas aeruginosa respectively are required for protein secretion via the T2SS. ATPase PilB is required for T4P extension.


Pssm-ID: 425681 [Multi-domain]  Cd Length: 269  Bit Score: 173.62  E-value: 3.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   11 VARGASDLHLSA-GLPPMLRINGDVVRQDVAALTPDALRAMIHQLMQPAQREEYETRQELDFSIDV---EGLARFRVNAF 86
Cdd:pfam00437   8 LDEGASDIHVEPpERIVWIRFRVDGVLREIPFPDADALARLISRIKVMARLDISERRPPQDGRLPLrigGKGVRVRVSTL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   87 NQQRGPAAVLRTIPSAIR--TLDELGCPASFK----ELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNREGEHhILTIED 160
Cdd:pfam00437  88 PTAGGEKLVIRLLDPSNValSLDELGMTGAQDeallEFLRQPRGNILVTGPTGSGKTTTLYAALGELNTRDEN-IVTVED 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  161 PIEFV--HPSRRSLVNQREVgrdthSFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVD 238
Cdd:pfam00437 167 PVEIQleGINQVQLNARAGV-----TFADLLRAILRQDPDRIMVGEIRDLETAEIALQAANTGHLVLSTLHTNSAAGALT 241
                         250       260       270
                  ....*....|....*....|....*....|
gi 704416921  239 RIIDVfpagekSMIRSMLSESLRAVIAQVL 268
Cdd:pfam00437 242 RLQDM------GVPPFELASSLLLVIAQRL 265
PRK10436 PRK10436
hypothetical protein; Provisional
3-268 1.92e-45

hypothetical protein; Provisional


Pssm-ID: 236694  Cd Length: 462  Bit Score: 161.25  E-value: 1.92e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   3 IDELLALTVARGASDLHL---SAGLPPMLRINGdvVRQDVAALTPDALRAMIHQLMQPAQREEYETRQELD--FSIDVEG 77
Cdd:PRK10436  88 INQTLQSALQKRASDIHFepaQNHYRIRLRIDG--VLHPLPDPSPELGAALTARLKVLGNLDIAERRLPQDgqFTVELAG 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  78 LA-RFRVNAFNQQRGPAAVLR---TIPSAIrTLDELGCPAS----FKELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNR 149
Cdd:PRK10436 166 NAySFRIATLPCRGGEKVVLRllqQVQQAL-DLETLGMTPAqlaqFRQALQQPQGLILVTGPTGSGKTVTLYSALQTLNT 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 150 EgEHHILTIEDPIEFVHPSrrslVNQREVGRDTH-SFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATL 228
Cdd:PRK10436 245 A-QINICSVEDPVEIPLAG----INQTQIHPKAGlTFQRVLRALLRQDPDVIMVGEIRDGETAEIAIKAAQTGHLVLSTL 319
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 704416921 229 HTNSAAKTVDRIidvfpaGEKSMIRSMLSESLRAVIAQVL 268
Cdd:PRK10436 320 HTNSTSETLVRL------QQMGIARWMLASALKLVIAQRL 353
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
116-269 5.04e-39

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 139.12  E-value: 5.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 116 KELVRQPQGLILVTGPTGSGKSTTLAAMIDhlNREGEHHILTIEDPIEFVHPSrrslVNQREVGRDTH-SFSAALRSALR 194
Cdd:NF041000 121 KQLLQRRSGLILFSGPTGSGKTTTMYSLAR--KLALNKQVITIEDPVEIKEPN----FLQLQVNEKAGmTYDTLLKAALR 194
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 704416921 195 EDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVDRIIDVfpaGEKsmiRSMLSESLRAVIAQVLL 269
Cdd:NF041000 195 HRPDILIIGEIRDAETAKAAIRAALTGHLVLSTVHAKSAAGVIYRLLEL---GIS---KEELEQTLIGISYQRLI 263
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
122-205 2.14e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 41.20  E-value: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   122 PQGLILVTGPTGSGKSTTLAAMIDHLNREGEHHILTIEDPIEFVHPSRRSLVNQREVGRDTHSFSA---ALRSALREDPD 198
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRlrlALALARKLKPD 80

                   ....*..
gi 704416921   199 IILVGEL 205
Cdd:smart00382  81 VLILDEI 87
 
Name Accession Description Interval E-value
PilT COG2805
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ...
1-339 0e+00

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


Pssm-ID: 442056  Cd Length: 342  Bit Score: 585.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   1 MTIDELLALTVARGASDLHLSAGLPPMLRINGDVVRQDVAALTPDALRAMIHQLMQPAQREEYETRQELDFSIDVEGLAR 80
Cdd:COG2805    3 MDLDELLKLAVEQGASDLHLTVGSPPMLRIDGELVPLDDPPLTPEDLEALLKEILTEEQRERLEEEGELDFSYSLPGLGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  81 FRVNAFNQQRGPAAVLRTIPSAIRTLDELGCPASFKELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNREGEHHILTIED 160
Cdd:COG2805   83 FRVNIFRQRGGVAAVLRLIPSEIPTLEELGLPPVLKELAELPRGLVLVTGPTGSGKSTTLAAMIDYINETRAKHIITIED 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 161 PIEFVHPSRRSLVNQREVGRDTHSFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVDRI 240
Cdd:COG2805  163 PIEFVHKHKKSLINQREVGRDTPSFANALRAALREDPDVILVGEMRDLETIEAALTAAETGHLVFATLHTNSAAQTIDRI 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 241 IDVFPAGEKSMIRSMLSESLRAVIAQVLL-KQEGGGRCAAWEIMVGTPAIRNLIREDKIAQMVSSIQTGQAHSMQTLDQA 319
Cdd:COG2805  243 IDVFPPEEQAQIRSQLAESLRGVISQRLLpRADGGGRVAAREILVNTPAVRNLIREGKTHQIPSLIQTGKKLGMQTMDQS 322
                        330       340
                 ....*....|....*....|
gi 704416921 320 LQDLLRKKLISAEQALAYAR 339
Cdd:COG2805  323 LAELVKEGLITEETALAYAS 342
pilT_fam TIGR01420
pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to ...
2-341 0e+00

pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to GspE, a protein involved in type II secretion (also called the General Secretion Pathway). PilT is an apparent cytosolic ATPase associated with type IV pilus systems. It is not required for pilin biogenesis, but is required for twitching motility and social gliding behaviors, shown in some species, powered by pilus retraction. Members of this family may be found in some species that type IV pili but have related structures for DNA uptake and natural transformation. [Cell envelope, Surface structures, Cellular processes, Chemotaxis and motility]


Pssm-ID: 273613  Cd Length: 343  Bit Score: 519.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921    2 TIDELLALTVARGASDLHLSAGLPPMLRINGDVVRQDVAALTPDALRAMIHQLMQPAQREEYETRQELDFSIDVEGLARF 81
Cdd:TIGR01420   1 SLEEILREAVKLGASDIHLTAGAPPAMRIDGDLVRIEFEPLTPEDTQKLAREILSEKQREEFEENGELDFSFSLPGVGRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   82 RVNAFNQQRGPAAVLRTIPSAIRTLDELGCPASFKELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNREGEHHILTIEDP 161
Cdd:TIGR01420  81 RVNAFYQRGGVALVLRLIPSKIPTFEELGLPPVLRELAERPRGLILVTGPTGSGKSTTLASMIDYINKNKAYHIITIEDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  162 IEFVHPSRRSLVNQREVGRDTHSFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVDRII 241
Cdd:TIGR01420 161 IEYVHTNKRSLINQREVGEDTLSFANALRAALREDPDVILIGEMRDLETVELALTAAETGHLVFGTLHTNSAAQTIERII 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  242 DVFPAGEKSMIRSMLSESLRAVIAQVLL-KQEGGGRCAAWEIMVGTPAIRNLIREDKIAQMVSSIQTGQAHSMQTLDQAL 320
Cdd:TIGR01420 241 DVFPAEEQEQIRTQLAESLVAIISQRLLpKADGGGRVLAVEILINTPAVRNLIREGKTHQIKSLIQTGQQLGMQTFDQHL 320
                         330       340
                  ....*....|....*....|.
gi 704416921  321 QDLLRKKLISAEQALAYARDR 341
Cdd:TIGR01420 321 AQLYKKGLITLEDALEAAPSP 341
PilU COG5008
Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures];
1-338 7.02e-153

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


Pssm-ID: 444032  Cd Length: 370  Bit Score: 434.14  E-value: 7.02e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   1 MTIDELLALTVARGASDLHLSAGLPPMLRINGDVVRQDVAALTPDALRAMIHQLMQPAQREEYETRQELDFSIDVEGLAR 80
Cdd:COG5008    1 MDLEDLLKLMVEKKASDLFITAGAPPSIKIDGKLTPLSQQPLTPEQVRELAYSIMNEEQREEFERTKECNFAISLPGVGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  81 FRVNAFNQQRGPAAVLRTIPSAIRTLDELGCPASFKELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNREGEHHILTIED 160
Cdd:COG5008   81 FRVNAFRQRGSVGMVLRRIETEIPTLDELGLPPVLKDLIMEKRGLVLFVGATGSGKSTTLAAMIDHRNENSSGHILTIED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 161 PIEFVHPSRRSLVNQREVGRDTHSFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVDRI 240
Cdd:COG5008  161 PIEFVHKHKKSIVTQREVGVDTESYEVALKNALRQAPDVILIGEIRDRETMEHAIAFAETGHLCLATLHANNANQALDRI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 241 IDVFPAGEKSMIRSMLSESLRAVIAQVLLKQEGGGRCAAWEIMVGTPAIRNLIREDKIAQMVSSIQTGQAHSMQTLDQAL 320
Cdd:COG5008  241 INFFPEERRPQLLMDLSLNLRAIVSQRLVPTKDGGRVAAVEVLLNTPLIADLIRKGEIHEIKEAMEKSRELGMQTFDQAL 320
                        330
                 ....*....|....*...
gi 704416921 321 QDLLRKKLISAEQALAYA 338
Cdd:COG5008  321 FRLYEAGKISYEEALRNA 338
PilT cd01131
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ...
103-323 2.61e-136

Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility.


Pssm-ID: 410875 [Multi-domain]  Cd Length: 223  Bit Score: 386.51  E-value: 2.61e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 103 IRTLDELGCPASFKELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNREGEHHILTIEDPIEFVHPSRRSLVNQREVGRDT 182
Cdd:cd01131    1 IPTFEELGLPPVLKDLALKPRGLVLVTGPTGSGKSTTLAAMIDYINETRSKHIITIEDPIEFVHKHKKSLINQREVGRDT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 183 HSFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVDRIIDVFPAGEKSMIRSMLSESLRA 262
Cdd:cd01131   81 ESFAAALRAALREDPDVILVGEMRDLETIELALTAAETGHLVFSTLHTNSAAQTIDRIIDVFPPEQQEQVRIQLASSLRG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 704416921 263 VIAQVLL-KQEGGGRCAAWEIMVGTPAIRNLIREDKIAQMVSSIQTGQAHSMQTLDQALQDL 323
Cdd:cd01131  161 VISQRLLpKKDGGGRVAAFEILINTPAIRNLIREGKTHQIPSLIQTGARDGMQTMDQSLYEL 222
PulE-GspE-like cd01129
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ...
113-286 1.05e-62

PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.


Pssm-ID: 410873 [Multi-domain]  Cd Length: 159  Bit Score: 196.94  E-value: 1.05e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 113 ASFKELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNREgEHHILTIEDPIEFVHPSrrslVNQREVGRDTH-SFSAALRS 191
Cdd:cd01129    1 ARLRRLIKRPHGLILVTGPTGSGKTTTLYAMLRELNGP-ERNIITIEDPVEYQIPG----INQSQVNEKIGlTFADALRA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 192 ALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVDRIIDVFpageksMIRSMLSESLRAVIAQVLLkq 271
Cdd:cd01129   76 ILRQDPDIIMVGEIRDAETAEIAIRAALTGHLVLSTLHTNDALGAITRLLDMG------IEPFLLASALRGVIAQRLV-- 147
                        170
                 ....*....|....*
gi 704416921 272 eggGRCAAWEIMVGT 286
Cdd:cd01129  148 ---GRTAIAEVLVLD 159
PulE COG2804
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ...
3-335 7.12e-62

Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442055 [Multi-domain]  Cd Length: 561  Bit Score: 206.97  E-value: 7.12e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   3 IDELLALTVARGASDLHLSaglpPM-------LRINGdvVRQDVAALTPDALRAMIHQL--MqpAQREEYETRQELD--F 71
Cdd:COG2804  183 VNAILEDAIKEGASDIHIE----PYekrlrvrFRIDG--VLREVLRLPKSLAPALVSRIkiM--ANLDIAERRLPQDgrI 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  72 SIDVEGLA-RFRVNAFNQQRGPAAVLRTIP--SAIRTLDELGCP----ASFKELVRQPQGLILVTGPTGSGKSTTLAAMI 144
Cdd:COG2804  255 KLRLGGREiDLRVSTLPTVYGEKVVLRILDksAALLDLEQLGFSpdqlERLRRLIRRPHGIILVTGPTGSGKTTTLYAAL 334
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 145 DHLNREgEHHILTIEDPIEFVHPsrrsLVNQ----REVGRDthsFSAALRSALREDPDIILVGELRDLETMRLAMTAAET 220
Cdd:COG2804  335 NELNTP-ERNIITVEDPVEYQLP----GINQvqvnPKIGLT---FASALRSILRQDPDVIMVGEIRDLETAEIAVQAALT 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 221 GHLVFATLHTNSAAKTVDRIIDvfpageksMI--RSMLSESLRAVIAQVLL-------KQE------------------- 272
Cdd:COG2804  407 GHLVLSTLHTNDAPSAITRLLD--------MGvePFLLASSLLGVLAQRLVrrlcphcKEPyepdpeelerlglppeela 478
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 273 -------GG----------GRCAAWEIMVGTPAIRNLIREDK-IAQMvssIQTGQAHSMQTLDQALQDLLRKKLISAEQA 334
Cdd:COG2804  479 pltfyrgVGcehcngtgykGRTGIYELLVIDDELRELIAEGAsAAEL---REAARKEGMRTLREDGLEKVLQGITTLEEV 555

                 .
gi 704416921 335 L 335
Cdd:COG2804  556 L 556
DotB_TraJ cd19516
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ...
117-284 8.21e-54

dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.


Pssm-ID: 410924 [Multi-domain]  Cd Length: 179  Bit Score: 174.87  E-value: 8.21e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 117 ELVRQ--PQ-GLILVTGPTGSGKSTTLAAMIDHL--NREGEHHILTIEDPIEFVH---PSRRSLVNQREVGRDTHSFSAA 188
Cdd:cd19516    2 DLVEAlfPReGLVYVAGATGSGKSTLLAAIYRYIleNDPPDRKIITYEDPIEFVYdgiKSKHSIIVQSQIPRHFKSFAKA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 189 LRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVDRIIDVFPAGEKSMIRSMLSESLRAVIAQVL 268
Cdd:cd19516   82 VREALRRKPSLIGVGELRDQETISAAVEASLTGHPVYSTVHTKSVAETIRRLISLFPPEERDAAAYDLLSTLRFIIVQRL 161
                        170
                 ....*....|....*.
gi 704416921 269 LKQEGGGRCAAWEIMV 284
Cdd:cd19516  162 VRTTDGKRVAVREYLV 177
T2SSE pfam00437
Type II/IV secretion system protein; This family contains components of both the Type II ...
11-268 3.17e-52

Type II/IV secretion system protein; This family contains components of both the Type II protein secretion system (T2SS), including Type 4 pilus (T4P), and Type IV protein secretion system (T4SS) from Gram-negative bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection. The cytoplasmic T2S E ATPase is a Zn-containing protein thought to provide the mechanical force for the secretion process. T2S-E contains Walker A and B motifs, that are essential for secretion and ATPase activity. ATPase PulE and XcpR from Klebsiella oxytoca and Pseudomonas aeruginosa respectively are required for protein secretion via the T2SS. ATPase PilB is required for T4P extension.


Pssm-ID: 425681 [Multi-domain]  Cd Length: 269  Bit Score: 173.62  E-value: 3.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   11 VARGASDLHLSA-GLPPMLRINGDVVRQDVAALTPDALRAMIHQLMQPAQREEYETRQELDFSIDV---EGLARFRVNAF 86
Cdd:pfam00437   8 LDEGASDIHVEPpERIVWIRFRVDGVLREIPFPDADALARLISRIKVMARLDISERRPPQDGRLPLrigGKGVRVRVSTL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   87 NQQRGPAAVLRTIPSAIR--TLDELGCPASFK----ELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNREGEHhILTIED 160
Cdd:pfam00437  88 PTAGGEKLVIRLLDPSNValSLDELGMTGAQDeallEFLRQPRGNILVTGPTGSGKTTTLYAALGELNTRDEN-IVTVED 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  161 PIEFV--HPSRRSLVNQREVgrdthSFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVD 238
Cdd:pfam00437 167 PVEIQleGINQVQLNARAGV-----TFADLLRAILRQDPDRIMVGEIRDLETAEIALQAANTGHLVLSTLHTNSAAGALT 241
                         250       260       270
                  ....*....|....*....|....*....|
gi 704416921  239 RIIDVfpagekSMIRSMLSESLRAVIAQVL 268
Cdd:pfam00437 242 RLQDM------GVPPFELASSLLLVIAQRL 265
type_II_gspE TIGR02533
type II secretion system protein E; This family describes GspE, the E protein of the type II ...
3-271 1.83e-45

type II secretion system protein E; This family describes GspE, the E protein of the type II secretion system, also called the main terminal branch of the general secretion pathway. This model separates GspE from the PilB protein of type IV pilin biosynthesis. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 131585 [Multi-domain]  Cd Length: 486  Bit Score: 161.78  E-value: 1.83e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921    3 IDELLALTVARGASDLHLSA---GLPPMLRINGdvVRQDVAALTPDALRAMIHQLMQPAQREEYETR--QELDFSIDVEG 77
Cdd:TIGR02533 112 VNSLLSRAVKERASDIHIEPfekALVVRFRVDG--VLRDVLSPPKKLHAALVSRVKIMAKLNIAEKRlpQDGRISLRVGG 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   78 LA-RFRVNAFNQQRGPAAVLRTI--PSAIRTLDELGCP----ASFKELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNRE 150
Cdd:TIGR02533 190 RDiDIRVSTVPTSHGERVVMRLLdkTAVRLDLETLGMSpellSRFERLIRRPHGIILVTGPTGSGKTTTLYAALSRLNTP 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  151 gEHHILTIEDPIEF-VHPSRRSLVNQReVGRDthsFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLH 229
Cdd:TIGR02533 270 -ERNILTVEDPVEYqIEGIGQIQVNPK-IGLT---FAAGLRAILRQDPDIIMVGEIRDLETAQIAIQASLTGHLVLSTLH 344
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 704416921  230 TNSAAKTVDRIID--VFPAgeksmirsMLSESLRAVIAQVLLKQ 271
Cdd:TIGR02533 345 TNDAAGAVTRLIDmgVEPF--------LLASSLLGVLAQRLVRR 380
PRK10436 PRK10436
hypothetical protein; Provisional
3-268 1.92e-45

hypothetical protein; Provisional


Pssm-ID: 236694  Cd Length: 462  Bit Score: 161.25  E-value: 1.92e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   3 IDELLALTVARGASDLHL---SAGLPPMLRINGdvVRQDVAALTPDALRAMIHQLMQPAQREEYETRQELD--FSIDVEG 77
Cdd:PRK10436  88 INQTLQSALQKRASDIHFepaQNHYRIRLRIDG--VLHPLPDPSPELGAALTARLKVLGNLDIAERRLPQDgqFTVELAG 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  78 LA-RFRVNAFNQQRGPAAVLR---TIPSAIrTLDELGCPAS----FKELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNR 149
Cdd:PRK10436 166 NAySFRIATLPCRGGEKVVLRllqQVQQAL-DLETLGMTPAqlaqFRQALQQPQGLILVTGPTGSGKTVTLYSALQTLNT 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 150 EgEHHILTIEDPIEFVHPSrrslVNQREVGRDTH-SFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATL 228
Cdd:PRK10436 245 A-QINICSVEDPVEIPLAG----INQTQIHPKAGlTFQRVLRALLRQDPDVIMVGEIRDGETAEIAIKAAQTGHLVLSTL 319
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 704416921 229 HTNSAAKTVDRIidvfpaGEKSMIRSMLSESLRAVIAQVL 268
Cdd:PRK10436 320 HTNSTSETLVRL------QQMGIARWMLASALKLVIAQRL 353
plasmid_TraJ TIGR02525
plasmid transfer ATPase TraJ; Members of this protein family are predicted ATPases associated ...
15-291 7.42e-45

plasmid transfer ATPase TraJ; Members of this protein family are predicted ATPases associated with plasmid transfer loci in bacteria. This family is most similar to the DotB ATPase of a type-IV secretion-like system of obligate intracellular pathogens Legionella pneumophila and Coxiella burnetii (TIGR02524). [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 131577 [Multi-domain]  Cd Length: 372  Bit Score: 157.66  E-value: 7.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   15 ASDLHLSAGLPPMLRINGDVVRQDVAALTPDALRAMIHQLMQPAQREEYETRQELDFSIDVEGLA------------RFR 82
Cdd:TIGR02525  24 VSDIHLQGGSPIVVERHGRQVPASSFPLDNLELERLVDEVFGPEIKPTVKSGAPVDRAIQLRGDEngryglgrgervRFR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   83 VN-----AFNQQRGPAAVLRTIPSAIRTLDELGC-PASFKELVRQpQGLILVTGPTGSGKSTTLAAMIDH-LNREGEHHI 155
Cdd:TIGR02525 104 CNfiqatIGKLETAISLTLRVIPSDIPDLKQMGIePDLFNSLLPA-AGLGLICGETGSGKSTLAASIYQHcGETYPDRKI 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  156 LTIEDPIEFVHPSRRSLV--NQREVGRDTHSFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSA 233
Cdd:TIGR02525 183 VTYEDPIEYILGSPDDLLppAQSQIGRDVDSFANGIRLALRRAPKIIGVGEIRDLETFQAAVLAGQSGHFCLGTLHVKSP 262
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 704416921  234 AKTVDRIIDVFPAGEKSMIRSMLSESLRAVIAQVLLKQEGGGRCAAWEIMVGTPAIRN 291
Cdd:TIGR02525 263 GEAISRCLQMYPPEMREAAAFDLLSILQYIIVQRLLRTTDGKRQAVREYIVFDDSLRR 320
type_IV_pilB TIGR02538
type IV-A pilus assembly ATPase PilB; This model describes a protein of type IV pilus ...
81-242 2.69e-44

type IV-A pilus assembly ATPase PilB; This model describes a protein of type IV pilus biogenesis designated PilB in Pseudomonas aeruginosa but PilF in Neisseria gonorrhoeae; the more common usage, reflected here, is PilB. This protein is an ATPase involved in protein export for pilin assembly and is closely related to GspE (TIGR02533) of type II secretion, also called the main terminal branch of the general secretion pathway. Note that type IV pilus systems are often divided into type IV-A and IV-B, with the latter group including bundle-forming pilus, mannose-sensitive hemagglutinin, etc. Members of this family are found in type IV-A systems. [Cell envelope, Surface structures, Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274186 [Multi-domain]  Cd Length: 564  Bit Score: 159.80  E-value: 2.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   81 FRVNAFNQQRGPAAVLRTI-PSAIR-TLDELGCP----ASFKELVRQPQGLILVTGPTGSGKSTTLAAMIDHLNREgEHH 154
Cdd:TIGR02538 268 FRVSTLPTLFGEKVVLRILdSSAAQlDIDKLGFEpdqkALFLEAIHKPQGMVLVTGPTGSGKTVSLYTALNILNTE-EVN 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  155 ILTIEDPIEFVHPSrrslVNQREVGRDTH-SFSAALRSALREDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSA 233
Cdd:TIGR02538 347 ISTAEDPVEINLPG----INQVNVNPKIGlTFAAALRSFLRQDPDIIMVGEIRDLETAEIAIKAAQTGHLVLSTLHTNDA 422

                  ....*....
gi 704416921  234 AKTVDRIID 242
Cdd:TIGR02538 423 PETLARLVN 431
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
116-269 5.04e-39

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 139.12  E-value: 5.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 116 KELVRQPQGLILVTGPTGSGKSTTLAAMIDhlNREGEHHILTIEDPIEFVHPSrrslVNQREVGRDTH-SFSAALRSALR 194
Cdd:NF041000 121 KQLLQRRSGLILFSGPTGSGKTTTMYSLAR--KLALNKQVITIEDPVEIKEPN----FLQLQVNEKAGmTYDTLLKAALR 194
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 704416921 195 EDPDIILVGELRDLETMRLAMTAAETGHLVFATLHTNSAAKTVDRIIDVfpaGEKsmiRSMLSESLRAVIAQVLL 269
Cdd:NF041000 195 HRPDILIIGEIRDAETAKAAIRAALTGHLVLSTVHAKSAAGVIYRLLEL---GIS---KEELEQTLIGISYQRLI 263
type_II_IV_secretion_ATPases cd19477
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ...
114-271 2.57e-27

type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410885 [Multi-domain]  Cd Length: 168  Bit Score: 105.55  E-value: 2.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 114 SFKELVRQPqGLILVTGPTGSGKSTTLAAMIDHLNREgeHHILTIEDPIEFVHPSRRSLVNQREVGRDThsFSAALRSAL 193
Cdd:cd19477    2 AIKDGIAIG-KNVIVCGGTGSGKTTYIKSILEFIPKE--ERIISIEDTEEIVFKHHKNYTQLFFGGNIT--SADCLKSCL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 194 REDPDIILVGELRDlETMRLAMTAAETGH-LVFATLHTNSAAKTVDRIIDVFPAGEKSMIRSMLSE------SLRAVIAQ 266
Cdd:cd19477   77 RQRPDRIILGELRS-SEAYDFYNVLCSGHkGTLTTLHAGSSEEAFIRLAN*SSSNSAARNIKFESLiegfkdLIDGIVHI 155

                 ....*
gi 704416921 267 VLLKQ 271
Cdd:cd19477  156 NHHKQ 160
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
113-264 8.70e-20

Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.


Pssm-ID: 410874 [Multi-domain]  Cd Length: 177  Bit Score: 85.28  E-value: 8.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 113 ASFKELVRQPQGlILVTGPTGSGKSTTLAAMIDHLNREgeHHILTIEDPIEFV--HPSRRSLVnQREVGRDTHSFSAA-- 188
Cdd:cd01130    3 AFLRLAVRARKN-ILISGGTGSGKTTLLNALLSFIPPD--ERIVTIEDTRELQlpHPNVVHLL-TRPGGGEKGEVTMAdl 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 704416921 189 LRSALREDPDIILVGELRDLETMRLaMTAAETGHL-VFATLHTNSAAKTVDRIIDVFPAGEKSMIRSMLSESLRAVI 264
Cdd:cd01130   79 LKAALRMRPDRIIVGEVRGGEAYDM-LQAMNTGHPgSITTIHANSAEDAIDRLATLVLEAGVNLDEEALRRLIASAI 154
VirB11 COG0630
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ...
126-282 8.69e-16

Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440395 [Multi-domain]  Cd Length: 462  Bit Score: 77.81  E-value: 8.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 126 ILVTGPTGSGKSTTLAA---MIDHLNRegehhILTIED--PIEFVHPsrrslvN-QREVGRDTHSFSAA-------LRSA 192
Cdd:COG0630  293 VLVAGGTASGKTTLLNAllsFIPPDAK-----IVTIEDtrELNLPHE------NwISLVTRESFGGEEGdvtmfdlLKAA 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 193 LREDPDIILVGELRDLEtMRLAMTAAETGHLVFATLHTNSAAKTVDRIIDVfPAG-EKSMIRsmlseSLRAVIAQVLLKQ 271
Cdd:COG0630  362 LRQRPDYIVVGEVRGEE-AYTLFQAMATGHGVLSTFHADSVESAINRLTSP-PINvPRTLLQ-----ALDLVVFQKRVRV 434
                        170
                 ....*....|....
gi 704416921 272 EGGG--RCAA-WEI 282
Cdd:COG0630  435 GGKRvrRVTSiVEI 448
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
31-276 1.34e-13

Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443988 [Multi-domain]  Cd Length: 386  Bit Score: 70.97  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  31 NGDVVRQDVAALTPDALRAMIHQLMQPAQREeyetrqeLDFS---IDveglARF----RVNAFNQ---QRGPAAVLRTIP 100
Cdd:COG4962   84 GGRLERTDVRFDSEEELRRLIERIAARVGRR-------LDESspiVD----ARLpdgsRVNAVIPpvaRDGPSLSIRKFR 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 101 SAIRTLDEL--------GCPASFKELVRQpqGL-ILVTGPTGSGKSTTLAAM---IDHlnregEHHILTIEDPIE--FVH 166
Cdd:COG4962  153 KRPLTLEDLvalgsltpEMAEFLRAAVRA--RLnILVSGGTGSGKTTLLNALsgfIPP-----DERIVTIEDAAElqLQH 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 167 PSRRSLV----NQREVG----RDthsfsaALRSALREDPDIILVGELRDLETmrLAM-TAAETGHL-VFATLHTNSAAKT 236
Cdd:COG4962  226 PHVVRLEtrppNVEGAGevtlRD------LVRNALRMRPDRIIVGEVRGAEA--LDMlQAMNTGHDgSMSTLHANSARDA 297
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 704416921 237 VDRIID-VFPAGEK---SMIRSMLSESLRAVIAQVLLkqEGGGR 276
Cdd:COG4962  298 LARLETlALMAGENlprEAVRRQIASAIDLVVHLERL--RDGRR 339
PRK13894 PRK13894
conjugal transfer ATPase TrbB; Provisional
90-240 6.14e-10

conjugal transfer ATPase TrbB; Provisional


Pssm-ID: 184377  Cd Length: 319  Bit Score: 59.75  E-value: 6.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  90 RGPAAVLRTIPSAIRTLDE--------LGCPASFKELVRQPQGlILVTGPTGSGKSTTLAAMIDHL-NREGEHHILTIED 160
Cdd:PRK13894 108 PAPTFAIRKKAVAIFTLDQyvergimtAAQREAIIAAVRAHRN-ILVIGGTGSGKTTLVNAIINEMvIQDPTERVFIIED 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 161 PIEfVHPSRRSLVNQR---EVgrdthSFSAALRSALREDPDIILVGELRDLETMRLAMtAAETGHL-VFATLHTNSAAKT 236
Cdd:PRK13894 187 TGE-IQCAAENYVQYHtsiDV-----NMTALLKTTLRMRPDRILVGEVRGPEALDLLM-AWNTGHEgGAATLHANNAKAG 259

                 ....
gi 704416921 237 VDRI 240
Cdd:PRK13894 260 LDRL 263
PRK13851 PRK13851
type IV secretion system protein VirB11; Provisional
126-207 3.79e-08

type IV secretion system protein VirB11; Provisional


Pssm-ID: 172375  Cd Length: 344  Bit Score: 54.13  E-value: 3.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 126 ILVTGPTGSGKSTTLAAMIDHLNRegEHHILTIEDPIEFVHPSR---RSLVNQREVGRDTHSFSAALRSALREDPDIILV 202
Cdd:PRK13851 165 MLLCGPTGSGKTTMSKTLISAIPP--QERLITIEDTLELVIPHEnhvRLLYSKNGAGLGAVTAEHLLQASLRMRPDRILL 242

                 ....*
gi 704416921 203 GELRD 207
Cdd:PRK13851 243 GEMRD 247
PRK13900 PRK13900
type IV secretion system ATPase VirB11; Provisional
114-283 3.11e-06

type IV secretion system ATPase VirB11; Provisional


Pssm-ID: 184381  Cd Length: 332  Bit Score: 48.21  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 114 SFKELVRQPQGLILVTGPTGSGKST-TLAAM--IDHLNRegehhILTIEDPIEFV---HPSRRSLVNQR-EVGRDTHSFS 186
Cdd:PRK13900 151 EFLEHAVISKKNIIISGGTSTGKTTfTNAALreIPAIER-----LITVEDAREIVlsnHPNRVHLLASKgGQGRAKVTTQ 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 187 AALRSALREDPDIILVGELRDLETMRLaMTAAETGHL-VFATLHTNSAAKTVDRI-IDVFPAGeKSMIRSMLSESLRAVI 264
Cdd:PRK13900 226 DLIEACLRLRPDRIIVGELRGAEAFSF-LRAINTGHPgSISTLHADSPAMAIEQLkLMVMQAG-LGMPPDQIKKYILNVV 303
                        170       180
                 ....*....|....*....|
gi 704416921 265 AQVL-LKQEGGGRCAAWEIM 283
Cdd:PRK13900 304 DIVVqLKRGSGGKRYVSEIY 323
PRK13833 PRK13833
conjugal transfer protein TrbB; Provisional
126-240 3.68e-06

conjugal transfer protein TrbB; Provisional


Pssm-ID: 172360 [Multi-domain]  Cd Length: 323  Bit Score: 47.87  E-value: 3.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921 126 ILVTGPTGSGKSTTLAAMIDHLNREG-EHHILTIEDPIEFVHPSRRSLVNQREvgrDTHSFSAALRSALREDPDIILVGE 204
Cdd:PRK13833 147 IVISGGTGSGKTTLANAVIAEIVASApEDRLVILEDTAEIQCAAENAVALHTS---DTVDMARLLKSTMRLRPDRIIVGE 223
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 704416921 205 LRDLETMRLaMTAAETGHL-VFATLHTNSAAKTVDRI 240
Cdd:PRK13833 224 VRDGAALTL-LKAWNTGHPgGVTTIHSNTAMSALRRL 259
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
45-141 1.68e-05

flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 45.79  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   45 DALRAMIHQLMQPAQREE--------YETRQELDFSidvEGLARFRVNAFNQQRGPAAVLRTIPSAIRtlDELGCPASFK 116
Cdd:TIGR03499 114 EALRELLERLLAGLAWLQrpperaklYERLLEAGVS---EELARELLEKLPEDADAEDAWRWLREALE--GMLPVKPEED 188
                          90       100
                  ....*....|....*....|....*
gi 704416921  117 ELVRQPQGLILVtGPTGSGKSTTLA 141
Cdd:TIGR03499 189 PILEQGGVIALV-GPTGVGKTTTLA 212
AAA_22 pfam13401
AAA domain;
119-204 2.10e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 40.79  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  119 VRQPQGLILVTGPTGSGKSTTLAAMIDHLNREgEHHILTIE-----DPIEFVHPSRRSLVNQREVGRDTHSFSAALRSAL 193
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLEQLPEV-RDSVVFVDlpsgtSPKDLLRALLRALGLPLSGRLSKEELLAALQQLL 79
                          90
                  ....*....|...
gi 704416921  194 RE--DPDIILVGE 204
Cdd:pfam13401  80 LAlaVAVVLIIDE 92
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
122-205 2.14e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 41.20  E-value: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921   122 PQGLILVTGPTGSGKSTTLAAMIDHLNREGEHHILTIEDPIEFVHPSRRSLVNQREVGRDTHSFSA---ALRSALREDPD 198
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRlrlALALARKLKPD 80

                   ....*..
gi 704416921   199 IILVGEL 205
Cdd:smart00382  81 VLILDEI 87
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
119-161 1.51e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 39.77  E-value: 1.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 704416921 119 VRQPQGLILVTGPTGSGKSTTLAAMIDHLNRegEHHILTIEDP 161
Cdd:COG3267   39 LAQGGGFVVLTGEVGTGKTTLLRRLLERLPD--DVKVAYIPNP 79
AAA_29 pfam13555
P-loop containing region of AAA domain;
122-144 1.76e-03

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 36.42  E-value: 1.76e-03
                          10        20
                  ....*....|....*....|...
gi 704416921  122 PQGLILVTGPTGSGKSTTLAAMI 144
Cdd:pfam13555  21 PRGNTLLTGPSGSGKSTLLDAIQ 43
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
99-165 8.78e-03

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 37.20  E-value: 8.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704416921  99 IPSAIRTLDEL---GCPASFkelvrqpqgLILVTGPTGSGKSTTLAAMIDHLNREGEH-HILTIEDPIEFV 165
Cdd:COG0467    2 VPTGIPGLDELlggGLPRGS---------STLLSGPPGTGKTTLALQFLAEGLRRGEKgLYVSFEESPEQL 63
PRK09302 PRK09302
circadian clock protein KaiC; Reviewed
68-156 9.47e-03

circadian clock protein KaiC; Reviewed


Pssm-ID: 236461 [Multi-domain]  Cd Length: 509  Bit Score: 37.55  E-value: 9.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704416921  68 ELDFSIDVEGLARFRVNAFN-QQRGPAAVlrtIPSAIRTLDELgCPASFkelvrQPQGLILVTGPTGSGKSTTLAAMIDH 146
Cdd:PRK09302 226 EYPFTITEDGISVLPLTAMRlTQRSSNER---ISSGVPDLDEM-LGGGF-----FRGSIILVSGATGTGKTLLASKFAEA 296
                         90
                 ....*....|
gi 704416921 147 LNREGEHHIL 156
Cdd:PRK09302 297 ACRRGERCLL 306
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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