ID   GSPI_AERHY              Reviewed;         119 AA.
AC   P31737;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Type II secretion system protein I;
DE            Short=T2SS minor pseudopilin I;
DE   AltName: Full=General secretion pathway protein I;
DE   Flags: Precursor;
GN   Name=exeI;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ah65;
RX   PubMed=8407845; DOI=10.1128/jb.175.20.6695-6703.1993;
RA   Howard S.P., Critch J., Bedi A.;
RT   "Isolation and analysis of eight exe genes and their involvement in
RT   extracellular protein secretion and outer membrane assembly in Aeromonas
RT   hydrophila.";
RL   J. Bacteriol. 175:6695-6703(1993).
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 ExeG. {ECO:0000250|UniProtKB:Q00516}.
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 methionine 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; X66504; CAA47130.1; -; Genomic_DNA.
DR   PIR; B49905; B49905.
DR   AlphaFoldDB; P31737; -.
DR   SMR; P31737; -.
DR   STRING; 1448139.AI20_16505; -.
DR   eggNOG; COG2165; Bacteria.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Methylation;
KW   Protein transport; Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..5
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024230"
FT   CHAIN           6..119
FT                   /note="Type II secretion system protein I"
FT                   /id="PRO_0000024231"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         6
FT                   /note="N-methylmethionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ   SEQUENCE   119 AA;  13339 MW;  826ECB33A26BD873 CRC64;
     MNARGMTLLE VMVALAVFAI AGLAVMKTAS EHLSALNYLE EKTLATWVVE NQLVQQKLEA
     KWPGDSWVEG GEQMAGQTWY WRYRGVATAD NNFKALDMEV RTAPKAESPV AFIRTYISR