GSPG_PECCC
ID GSPG_PECCC Reviewed; 156 AA.
AC P31586;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 87.
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 Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS carotovora).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=555;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SCRI 193;
RX PubMed=8326859; DOI=10.1111/j.1365-2958.1993.tb01589.x;
RA Reeves P.J., Whitcombe D., Wharam S., Gibson M., Allison G., Bunce N.,
RA Barallon R., Douglas P., Mulholland V., Stevens S., Walker S.,
RA Salmond G.P.C.;
RT "Molecular cloning and characterization of 13 out genes from Erwinia
RT carotovora subspecies carotovora: genes encoding members of a general
RT secretion pathway (GSP) widespread in Gram-negative bacteria.";
RL Mol. Microbiol. 8:443-456(1993).
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; X70049; CAA49648.1; -; Genomic_DNA.
DR PIR; S32861; S32861.
DR RefSeq; WP_048329249.1; NZ_VBUA01000017.1.
DR AlphaFoldDB; P31586; -.
DR SMR; P31586; -.
DR GeneID; 61408869; -.
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..22
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000449506"
FT CHAIN 23..156
FT /note="Type II secretion system core protein G"
FT /id="PRO_0000024203"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 23
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ SEQUENCE 156 AA; 17352 MW; 3DD742743ABE3245 CRC64;
MQQSQRGCGQ NSYGQSGYRQ RGFTLLEIMV VIVILGVLAS LVVPNLMGNK EKADRQKAVS
DIVSLESALD MYKLDNNRYP STEQGLKALV TKPTVQPEPR NYPADGYIRR LPQDPWGTDY
QLLNPGQHGK LDIFSLGPDG MPGTEDDIGN WNLDKK