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Conserved domains on  [gi|695750489|ref|WP_032676746|]
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MULTISPECIES: pilus assembly protein PilM [Enterobacter cloacae complex]

Protein Classification

type IV pilus biogenesis protein PilM( domain architecture ID 1004113)

type IV pilus biogenesis protein PilM binds to PilB, PilT, and possibly PilC and that binding of PilN may modulate the interaction of PilM with PilB, PilT, and/or PilC

Gene Ontology:  GO:0043683|GO:0046872|GO:0005524
PubMed:  28496159

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
9-173 2.95e-16

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd24049:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 339  Bit Score: 76.93  E-value: 2.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489   9 GVHIQQDKVIAVALTRERAGWRLRRWWAVPLSDGVIGEGKILKPEQLVNALRG-WRKTLPHSHRVFLSFPATRVLQRALP 87
Cdd:cd24049    2 GIDIGSSSIKAVELKRSGGGLVLVAFAIIPLPEGAIVDGEIADPEALAEALKKlLKENKIKGKKVVVALPGSDVIVRTIK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489  88 RPSVNLRD-SEQLTWvgaALARELEMPPDTLCFDY---AQDTFSNTFQ---VTAAQNREVDTLLSLAEALRLRLAAIVPD 160
Cdd:cd24049   82 LPKMPEKElEEAIRF---EAEQYLPFPLEEVVLDYqilGEVEEGGEKLevlVVAAPKEIVESYLELLKEAGLKPVAIDVE 158
                        170
                 ....*....|...
gi 695750489 161 AGALANLLSAVAP 173
Cdd:cd24049  159 SFALARALEYLLP 171
 
Name Accession Description Interval E-value
ASKHA_NBD_PilM cd24049
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ...
9-173 2.95e-16

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


Pssm-ID: 466899 [Multi-domain]  Cd Length: 339  Bit Score: 76.93  E-value: 2.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489   9 GVHIQQDKVIAVALTRERAGWRLRRWWAVPLSDGVIGEGKILKPEQLVNALRG-WRKTLPHSHRVFLSFPATRVLQRALP 87
Cdd:cd24049    2 GIDIGSSSIKAVELKRSGGGLVLVAFAIIPLPEGAIVDGEIADPEALAEALKKlLKENKIKGKKVVVALPGSDVIVRTIK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489  88 RPSVNLRD-SEQLTWvgaALARELEMPPDTLCFDY---AQDTFSNTFQ---VTAAQNREVDTLLSLAEALRLRLAAIVPD 160
Cdd:cd24049   82 LPKMPEKElEEAIRF---EAEQYLPFPLEEVVLDYqilGEVEEGGEKLevlVVAAPKEIVESYLELLKEAGLKPVAIDVE 158
                        170
                 ....*....|...
gi 695750489 161 AGALANLLSAVAP 173
Cdd:cd24049  159 SFALARALEYLLP 171
PilM COG4972
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];
8-173 6.15e-14

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


Pssm-ID: 443997 [Multi-domain]  Cd Length: 294  Bit Score: 69.88  E-value: 6.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489   8 TGVHIQQDKVIAVALTRERAGWRLRRWWAVPLSDGVIGEGKILKPEQLVNALRGWRKTLP-HSHRVFLSFPATRVLQRAL 86
Cdd:COG4972    5 VGIDIGSSSIKLVELSKSGGGYRLERYAEEPLPEGAVVDGNIVDPEAVAEALKELLKRLKiKTKRVAIAVPGSSVITRKI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489  87 PRPSVNLRD-SEQLTWvgaalarELE----MPPDTLCFDY------AQDTFSNTFQVTAAQNREVDTLLSLAEALRLRLA 155
Cdd:COG4972   85 TLPALSEKElEEAIEF-------EAEqyipFPLEEVVLDFqvlgpsEEGPEKVEVLLVAARKEVVEDYVELLEAAGLKPV 157
                        170
                 ....*....|....*...
gi 695750489 156 AIVPDAGALANLLSAVAP 173
Cdd:COG4972  158 VVDVEPFALLRALELLPP 175
PilM_2 pfam11104
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for ...
9-97 2.65e-06

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


Pssm-ID: 431656 [Multi-domain]  Cd Length: 340  Bit Score: 47.67  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489    9 GVHIQQDKVIAVALTRERAGWRLRRWWAVPLSDGVIGEGKILKPEQLVNAL-RGWRKTLPHSHRVFLSFPATRVLQRALP 87
Cdd:pfam11104   1 GIDISSSAIKLVELSKKKGGYRLERYAIEPLPKGAVVDGNIENIDAVSEALrRAVKKSGTRLKNVAIAVPGSAVITKKII 80
                          90
                  ....*....|
gi 695750489   88 RPSvNLRDSE 97
Cdd:pfam11104  81 LPA-GLSEEE 89
pilM TIGR01175
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV ...
8-165 6.01e-06

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


Pssm-ID: 273484 [Multi-domain]  Cd Length: 348  Bit Score: 46.70  E-value: 6.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489    8 TGVHIQQDKVIAVALTRERAGWRLRRWWAVPLSDGVIGEGKILKPEQLVNALRGWRKTLP-HSHRVFLSFPATRVLQRAL 86
Cdd:TIGR01175   6 VGIDIGSTSVKVAQLKRSGDRYKLEHYAVEPLPAGIFTEGHIVEYQAVAEALKELLSELGiNTKKAATAVPGSAVITKVI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489   87 PRPSvNLRDSEQLTWVGAALARELEMPPDTLCFDY-AQDTFSN------TFQVTAAQNREVDTLLslaEALRLR-LAAIV 158
Cdd:TIGR01175  86 PVPA-GLDERELEFAVYIEASHYIPYPIEEVSLDFeKLGLKANnpestvQVLLAATRKEVVDSRL---HALKLAgLEPKV 161

                  ....*..
gi 695750489  159 PDAGALA 165
Cdd:TIGR01175 162 VDVESFA 168
 
Name Accession Description Interval E-value
ASKHA_NBD_PilM cd24049
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ...
9-173 2.95e-16

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


Pssm-ID: 466899 [Multi-domain]  Cd Length: 339  Bit Score: 76.93  E-value: 2.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489   9 GVHIQQDKVIAVALTRERAGWRLRRWWAVPLSDGVIGEGKILKPEQLVNALRG-WRKTLPHSHRVFLSFPATRVLQRALP 87
Cdd:cd24049    2 GIDIGSSSIKAVELKRSGGGLVLVAFAIIPLPEGAIVDGEIADPEALAEALKKlLKENKIKGKKVVVALPGSDVIVRTIK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489  88 RPSVNLRD-SEQLTWvgaALARELEMPPDTLCFDY---AQDTFSNTFQ---VTAAQNREVDTLLSLAEALRLRLAAIVPD 160
Cdd:cd24049   82 LPKMPEKElEEAIRF---EAEQYLPFPLEEVVLDYqilGEVEEGGEKLevlVVAAPKEIVESYLELLKEAGLKPVAIDVE 158
                        170
                 ....*....|...
gi 695750489 161 AGALANLLSAVAP 173
Cdd:cd24049  159 SFALARALEYLLP 171
PilM COG4972
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];
8-173 6.15e-14

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


Pssm-ID: 443997 [Multi-domain]  Cd Length: 294  Bit Score: 69.88  E-value: 6.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489   8 TGVHIQQDKVIAVALTRERAGWRLRRWWAVPLSDGVIGEGKILKPEQLVNALRGWRKTLP-HSHRVFLSFPATRVLQRAL 86
Cdd:COG4972    5 VGIDIGSSSIKLVELSKSGGGYRLERYAEEPLPEGAVVDGNIVDPEAVAEALKELLKRLKiKTKRVAIAVPGSSVITRKI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489  87 PRPSVNLRD-SEQLTWvgaalarELE----MPPDTLCFDY------AQDTFSNTFQVTAAQNREVDTLLSLAEALRLRLA 155
Cdd:COG4972   85 TLPALSEKElEEAIEF-------EAEqyipFPLEEVVLDFqvlgpsEEGPEKVEVLLVAARKEVVEDYVELLEAAGLKPV 157
                        170
                 ....*....|....*...
gi 695750489 156 AIVPDAGALANLLSAVAP 173
Cdd:COG4972  158 VVDVEPFALLRALELLPP 175
PilM_2 pfam11104
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for ...
9-97 2.65e-06

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


Pssm-ID: 431656 [Multi-domain]  Cd Length: 340  Bit Score: 47.67  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489    9 GVHIQQDKVIAVALTRERAGWRLRRWWAVPLSDGVIGEGKILKPEQLVNAL-RGWRKTLPHSHRVFLSFPATRVLQRALP 87
Cdd:pfam11104   1 GIDISSSAIKLVELSKKKGGYRLERYAIEPLPKGAVVDGNIENIDAVSEALrRAVKKSGTRLKNVAIAVPGSAVITKKII 80
                          90
                  ....*....|
gi 695750489   88 RPSvNLRDSE 97
Cdd:pfam11104  81 LPA-GLSEEE 89
pilM TIGR01175
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV ...
8-165 6.01e-06

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


Pssm-ID: 273484 [Multi-domain]  Cd Length: 348  Bit Score: 46.70  E-value: 6.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489    8 TGVHIQQDKVIAVALTRERAGWRLRRWWAVPLSDGVIGEGKILKPEQLVNALRGWRKTLP-HSHRVFLSFPATRVLQRAL 86
Cdd:TIGR01175   6 VGIDIGSTSVKVAQLKRSGDRYKLEHYAVEPLPAGIFTEGHIVEYQAVAEALKELLSELGiNTKKAATAVPGSAVITKVI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695750489   87 PRPSvNLRDSEQLTWVGAALARELEMPPDTLCFDY-AQDTFSN------TFQVTAAQNREVDTLLslaEALRLR-LAAIV 158
Cdd:TIGR01175  86 PVPA-GLDERELEFAVYIEASHYIPYPIEEVSLDFeKLGLKANnpestvQVLLAATRKEVVDSRL---HALKLAgLEPKV 161

                  ....*..
gi 695750489  159 PDAGALA 165
Cdd:TIGR01175 162 VDVESFA 168
 
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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