Summary: Type II secretion system (T2SS), protein G
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Type II secretion system (T2SS), protein G Provide feedback
The Type II secretion system, also called Secretion-dependent pathway (SDP), is responsible for the transport of proteins across the outer membrane first exported to the periplasm by the Sec or Tat translocon in Gram-negative (diderm) bacteria [1,2]. The T2SG family includes proteins such as EpsG (P45773) in Vibrio cholera, XcpT also called PddA (Q00514) in Pseudomonas aeruginosa or PulG (P15746)in Klebsiella pneumoniae. The PulG is thought to be anchored in the inner membrane with its C-terminus directed towards the periplasme . Together with other members of the Type II secretion machinery, it is thought to assemble into a pilus-like structure that may function as a dynamic mechanism to push secreted proteins out of the cell. The polypeptide is organized into a long N-terminal alpha-helix followed by a loop region that separates it from a C-terminal anti-parallel beta-sheet .
Kohler R, Schafer K, Muller S, Vignon G, Diederichs K, Philippsen A, Ringler P, Pugsley AP, Engel A, Welte W; , Mol Microbiol 2004;54:647-664.: Structure and assembly of the pseudopilin PulG. PUBMED:15491357 EPMC:15491357
Bally M, Filloux A, Akrim M, Ball G, Lazdunski A, Tommassen J; , Mol Microbiol 1992;6:1121-1131.: Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase. PUBMED:1588814 EPMC:1588814
Reyss I, Pugsley AP; , Mol Gen Genet 1990;222:176-184.: Five additional genes in the pulC-O operon of the gram-negative bacterium Klebsiella oxytoca UNF5023 which are required for pullulanase secretion. PUBMED:2129543 EPMC:2129543
Peabody CR, Chung YJ, Yen MR, Vidal-Ingigliardi D, Pugsley AP, Saier MH Jr;, Microbiology. 2003;149:3051-3072.: Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella. PUBMED:14600218 EPMC:14600218
Desvaux M, Hebraud M, Talon R, Henderson IR;, Trends Microbiol. 2009;17:139-145.: Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. PUBMED:19299134 EPMC:19299134
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR013545
The general secretion pathway, or type II pullulanase-like machinery, is responsible for the transport of proteins from the periplasm across the outer membrane in Gram-negative bacteria [PUBMED:15491357, PUBMED:1588814]. This entry includes protein G (e.g. SWISSPROT, SWISSPROT) involved in this pathway. The PulG protein (SWISSPROT) is thought to be anchored in the inner membrane with its C terminus directed towards the periplasm [PUBMED:2129543]. Together with other members of the secretion machinery, it is thought to assemble into a pilus-like structure that may function as a dynamic mechanism to push secreted proteins out of the cell. The polypeptide is organised into a long N-terminal alpha-helix followed by a loop region that separates it from a C-terminal anti-parallel beta-sheet [PUBMED:15491357].
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This is a clan contains bacterial pilus subunits and proteins involved in secretion. Pili proteins enable the transfer of plasmid between bacteria. The families in this clan adopt an alpha helical structure which is packed against a beta sheet [2-3].
The clan contains the following 10 members:Bundlin N_methyl N_methyl_2 N_methyl_3 Pilin PilS T2SG T2SI TcpA YadA_anchor
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Curation and family details
|Seed source:||Pfam-B_1144 (release 18.0)|
|Author:||Fenech M, Desvaux M|
|Number in seed:||175|
|Number in full:||1599|
|Average length of the domain:||105.00 aa|
|Average identity of full alignment:||40 %|
|Average coverage of the sequence by the domain:||69.58 %|
|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:||6|
|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 T2SG domain has been found. There are 10 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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