GSPI_ECOLX
ID GSPI_ECOLX Reviewed; 123 AA.
AC Q8VPC3;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Type II secretion system protein I;
DE Short=T2SS minor pseudopilin I;
DE AltName: Full=Putative general secretion pathway protein I;
DE Flags: Precursor;
GN Name=gspI;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H10407;
RX PubMed=12011463; DOI=10.1073/pnas.092152899;
RA Tauschek M., Gorrell R.J., Strugnell R.A., Robins-Browne R.M.;
RT "Identification of a protein secretory pathway for the secretion of heat-
RT labile enterotoxin by an enterotoxigenic strain of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7066-7071(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 33-118, AND INTERACTION WITH GSPK
RP AND GSPJ.
RX PubMed=18438417; DOI=10.1038/nsmb.1426;
RA Korotkov K.V., Hol W.G.;
RT "Structure of the GspK-GspI-GspJ complex from the enterotoxigenic
RT Escherichia coli type 2 secretion system.";
RL Nat. Struct. Mol. Biol. 15:462-468(2008).
CC -!- FUNCTION: Component of the type II secretion system required for the
CC energy-dependent secretion of extracellular factors such as proteases
CC and toxins from the periplasm. Part of the pseudopilus tip complex that
CC is critical for the recognition and binding of secretion substrates.
CC {ECO:0000250|UniProtKB:Q00516}.
CC -!- SUBUNIT: Type II secretion is composed of four main components: the
CC outer membrane complex, the inner membrane complex, the cytoplasmic
CC secretion ATPase and the periplasm-spanning pseudopilus. Interacts with
CC core component GspG (By similarity). Interacts with pseudopilins GspJ
CC and GspK (PubMed:18438417). {ECO:0000250|UniProtKB:Q00516,
CC ECO:0000269|PubMed:18438417}.
CC -!- INTERACTION:
CC Q8VPC3; Q8VRM4: gspJ; NbExp=3; IntAct=EBI-9009622, EBI-15699424;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q00516}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Cleaved by prepilin peptidase. {ECO:0000250|UniProtKB:Q00516}.
CC -!- PTM: Methylated by prepilin peptidase at the amino group of the N-
CC terminal phenylalanine once the leader sequence is cleaved by prepilin
CC peptidase. {ECO:0000250|UniProtKB:Q00516}.
CC -!- SIMILARITY: Belongs to the GSP I family. {ECO:0000305}.
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DR EMBL; AY056599; AAL10698.1; -; Genomic_DNA.
DR RefSeq; WP_000820137.1; NZ_NKEH01000021.1.
DR PDB; 3CI0; X-ray; 2.20 A; I=33-118.
DR PDBsum; 3CI0; -.
DR AlphaFoldDB; Q8VPC3; -.
DR SMR; Q8VPC3; -.
DR DIP; DIP-46384N; -.
DR IntAct; Q8VPC3; 2.
DR PATRIC; fig|562.7244.peg.3592; -.
DR EvolutionaryTrace; Q8VPC3; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR003413; T2SS_GspI_C.
DR InterPro; IPR010052; T2SS_protein-GspI.
DR PANTHER; PTHR38779; PTHR38779; 1.
DR Pfam; PF07963; N_methyl; 1.
DR Pfam; PF02501; T2SSI; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR01707; gspI; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; Methylation;
KW Transmembrane; Transmembrane helix.
FT PROPEP 1..4
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000449545"
FT CHAIN 5..123
FT /note="Type II secretion system protein I"
FT /id="PRO_0000449546"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 5
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT HELIX 36..57
FT /evidence="ECO:0007829|PDB:3CI0"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:3CI0"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:3CI0"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:3CI0"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:3CI0"
FT STRAND 107..116
FT /evidence="ECO:0007829|PDB:3CI0"
SQ SEQUENCE 123 AA; 13511 MW; EEF8E239BE64E876 CRC64;
MKRGFTLLEV MLALAIFALS ATAVLQIASG ALSNQHVLEE KTVAGWVAEN QTALLYLMTR
GQRAVRQQGE SDMAGSRWYW RTTPLSTGNA LLQAVDIEVS LHEDFSSVIQ SRRAWFSAVG
GQQ
