Summary: Type IV pilus assembly protein PilM;
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Type IV pilus assembly protein PilM; Provide feedback
The type IV pilus assembly protein PilM is required for competency and pilus biogenesis [1-2]. It binds to PilN and ATP .
Roine E, Nunn DN, Paulin L, Romantschuk M;, J Bacteriol. 1996;178:410-417.: Characterization of genes required for pilus expression in Pseudomonas syringae pathovar phaseolicola. PUBMED:8550460 EPMC:8550460
Rumszauer J, Schwarzenlander C, Averhoff B;, FEBS J. 2006;273:3261-3272.: Identification, subcellular localization and functional interactions of PilMNOWQ and PilA4 involved in transformation competency and pilus biogenesis in the thermophilic bacterium Thermus thermophilus HB27. PUBMED:16857013 EPMC:16857013
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005883
The opportunistic pathogen Pseudomonas aeruginosa produces type 4 fimbriae which promote adhesion to epithelial cells and are associated with a form of surface translocation called twitching motility [PUBMED:7565110]. Four genes, pilM-P, encode the necessary proteins with predicted sizes of 37.9, 22.2, 22.8 and 19.0 kDa, respectively and appear to form an operon. This protein is required for the assembly of the type IV fimbria in P. aeruginosa 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.
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The actin-like ATPase domain forms an alpha/beta canonical fold. The domain can be subdivided into 1A, 1B, 2A and 2B subdomains. Subdomains 1A and 1B share the same RNAseH-like fold (a five-stranded beta-sheet decorated by a number of alpha-helices). Domains 1A and 2A are conserved in all members of this superfamily, whereas domain 1B and 2B have a variable structure and are even missing from some homologues . Within the actin-like ATPase domain the ATP-binding site is highly conserved. The phosphate part of the ATP is bound in a cleft between subdomains 1A and 2A, whereas the adenosine moiety is bound to residues from domains 2A and 2B.
The clan contains the following 29 members:Acetate_kinase Actin BcrAD_BadFG CmcH_NodU DDR DUF1464 DUF1786 EutA FGGY_C FGGY_N FtsA Fumble GDA1_CD39 Glucokinase Hexokinase_1 Hexokinase_2 HSP70 Hydant_A_N Hydantoinase_A MreB_Mbl MutL Pan_kinase Peptidase_M22 PilM_2 Ppx-GppA ROK StbA T2SL UPF0075
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Curation and family details
|Author:||Pollington J, Finn RD, Eberhardt R|
|Number in seed:||37|
|Number in full:||952|
|Average length of the domain:||315.90 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||86.32 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||3|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PilM_2 domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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