GSPG_KLEOK
ID GSPG_KLEOK Reviewed; 142 AA.
AC A0A0H3HDD6;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 31.
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 Flags: Precursor;
GN OrderedLocusNames=KOX_13580;
OS Klebsiella oxytoca (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 /
OS NRRL B-199 / KCTC 1686 / BUCSAV 143 / CCM 1901).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1006551;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC
RC 1686 / BUCSAV 143 / CCM 1901;
RX PubMed=22493189; DOI=10.1128/jb.00026-12;
RA Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA Yang K.S.;
RT "Complete genome sequence of Klebsiella oxytoca KCTC 1686, used in
RT production of 2,3-butanediol.";
RL J. Bacteriol. 194:2371-2372(2012).
RN [2]
RP SUBUNIT, AND FUNCTION.
RX PubMed=8809775; DOI=10.1111/j.1365-2958.1996.tb02643.x;
RA Pugsley A.P.;
RT "Multimers of the precursor of a type IV pilin-like component of the
RT general secretory pathway are unrelated to pili.";
RL Mol. Microbiol. 20:1235-1245(1996).
RN [3]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15491357; DOI=10.1111/j.1365-2958.2004.04307.x;
RA Koehler R., Schaefer K., Mueller S., Vignon G., Diederichs K.,
RA Philippsen A., Ringler P., Pugsley A.P., Engel A., Welte W.;
RT "Structure and assembly of the pseudopilin PulG.";
RL Mol. Microbiol. 54:647-664(2004).
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 (PubMed:8809775). Pseudopilin
CC (pilin-like) protein that polymerizes to form the pseudopilus. Further
CC polymerization triggers pseudopilus growth (PubMed:15491357).
CC {ECO:0000269|PubMed:15491357, ECO:0000269|PubMed:8809775}.
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:0000269|PubMed:15491357,
CC ECO:0000269|PubMed:8809775}.
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; CP003218; AEX04440.1; -; Genomic_DNA.
DR RefSeq; WP_014228298.1; NC_016612.1.
DR AlphaFoldDB; A0A0H3HDD6; -.
DR SMR; A0A0H3HDD6; -.
DR EnsemblBacteria; AEX04440; AEX04440; KOX_13580.
DR KEGG; kox:KOX_13580; -.
DR HOGENOM; CLU_091705_2_1_6; -.
DR OMA; PWRNDYL; -.
DR Proteomes; UP000007843; Chromosome.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Methylation; Transmembrane;
KW Transmembrane helix.
FT PROPEP 1..8
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000449511"
FT CHAIN 9..142
FT /note="Type II secretion system core protein G"
FT /id="PRO_0000449512"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 122..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ SEQUENCE 142 AA; 15792 MW; 2E97AC64D304407B CRC64;
MRRQSQRGFT LLEIMVVIVI MGILASLVVP NLMGNKDKAD RQKVVSDIVA LESALDMYKL
DNSRYPTTEQ GLQALITKPS VPPEARYYPQ DGYIRRLPQD PWGGDYQLVS PGQHGQIDIF
SSGQDGVPGT DDDIGNWTLS KK
