ID   GSPI_DICCH              Reviewed;         125 AA.
AC   P24688;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Type II secretion system protein I;
DE            Short=T2SS minor pseudopilin I;
DE   AltName: Full=General secretion pathway protein I;
DE   AltName: Full=Pectic enzymes secretion protein OutI;
DE   Flags: Precursor;
GN   Name=outI;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EC16;
RX   PubMed=1992458; DOI=10.1073/pnas.88.3.1079;
RA   He S.Y., Lindeberg M., Chatterjee A.K., Collmer A.;
RT   "Cloned Erwinia chrysanthemi out genes enable Escherichia coli to
RT   selectively secrete a diverse family of heterologous proteins to its
RT   milieu.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:1079-1083(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1429461; DOI=10.1128/jb.174.22.7385-7397.1992;
RA   Lindeberg M., Collmer A.;
RT   "Analysis of eight out genes in a cluster required for pectic enzyme
RT   secretion by Erwinia chrysanthemi: sequence comparison with secretion genes
RT   from other Gram-negative bacteria.";
RL   J. Bacteriol. 174:7385-7397(1992).
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 OutG. {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; M37886; AAA24827.1; -; Genomic_DNA.
DR   EMBL; L02214; AAA24836.1; -; Genomic_DNA.
DR   PIR; G47021; G47021.
DR   RefSeq; WP_012769044.1; NZ_JSYH01000001.1.
DR   AlphaFoldDB; P24688; -.
DR   SMR; P24688; -.
DR   OMA; RTWYWQQ; -.
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_0000024236"
FT   CHAIN           6..125
FT                   /note="Type II secretion system protein I"
FT                   /id="PRO_0000024237"
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   125 AA;  14024 MW;  DA4856256ADF3F3C CRC64;
     MKQQGMTLLE VMVALVIFAL AGLTVLKTTA QQANGLGRLE EKTFALWIAE NQQAAMRLEK
     QWPQSQWVDG EVNFAGSLWF WRIQGIATAD TRVRAIDVEV RHDRDSRAAD AVLRSYLVQP
     GEPAQ