ID   GSPG_DICCH              Reviewed;         153 AA.
AC   P31585;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Type II secretion system core protein G;
DE            Short=T2SS core protein G;
DE   AltName: Full=General secretion pathway protein G;
DE   AltName: Full=Pectic enzymes secretion protein OutG;
DE   Flags: Precursor;
GN   Name=outG;
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=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: Core component of the type II secretion system required for
CC       the energy-dependent secretion of extracellular factors such as
CC       proteases and toxins from the periplasm. Pseudopilin (pilin-like)
CC       protein that polymerizes to form the pseudopilus. Further
CC       polymerization triggers pseudopilus growth.
CC       {ECO:0000250|UniProtKB:Q00514}.
CC   -!- SUBUNIT: Type II secretion system is composed of four main components:
CC       the outer membrane complex, the inner membrane complex, the cytoplasmic
CC       secretion ATPase and the periplasm-spanning pseudopilus. Forms
CC       homomultimers. {ECO:0000250|UniProtKB:Q00514}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:Q00514}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: Cleaved by the prepilin peptidase. {ECO:0000250|UniProtKB:Q00514}.
CC   -!- PTM: Methylated by prepilin peptidase at the amino group of the N-
CC       terminal phenylalanine once the leader sequence is cleaved.
CC       {ECO:0000250|UniProtKB:Q00514}.
CC   -!- SIMILARITY: Belongs to the GSP G family. {ECO:0000305}.
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DR   EMBL; L02214; AAA24834.1; -; Genomic_DNA.
DR   PIR; E47021; E47021.
DR   AlphaFoldDB; P31585; -.
DR   SMR; P31585; -.
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; IPR000983; Bac_GSPG_pilin.
DR   InterPro; IPR012902; N_methyl_site.
DR   InterPro; IPR045584; Pilin-like.
DR   InterPro; IPR013545; T2SS_protein-GspG_C.
DR   InterPro; IPR010054; Type2_sec_GspG.
DR   Pfam; PF07963; N_methyl; 1.
DR   Pfam; PF08334; T2SSG; 1.
DR   PRINTS; PR00813; BCTERIALGSPG.
DR   SUPFAM; SSF54523; SSF54523; 1.
DR   TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR   TIGRFAMs; TIGR01710; typeII_sec_gspG; 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..7
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000449507"
FT   CHAIN           8..153
FT                   /note="Type II secretion system core protein G"
FT                   /id="PRO_0000024205"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          68..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         8
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ   SEQUENCE   153 AA;  16789 MW;  4749B62838FCE341 CRC64;
     MERRQRGFTL LEIMVVIVIL GVLASLVVPN LMGNKEKADK QKAVSDIVAL ESQLDMYKLD
     NSRYPTTEQG LGALVKKPTT PPEPRNYPQD GYIRRLPQDP WGAEYQLVSP GRHGKIDVFS
     YGPDGMPDTD DDIGNWNVGN GAHNNGGNGN GNP