GSPG_XANCP
ID GSPG_XANCP Reviewed; 143 AA.
AC P31734;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 113.
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 Name=xpsG; Synonyms=pefG; OrderedLocusNames=XCC0662;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=8000 NCPPB 1145;
RX PubMed=1944223; DOI=10.1007/bf00267456;
RA Dums F., Dow J.M., Daniels M.J.;
RT "Structural characterization of protein secretion genes of the bacterial
RT phytopathogen Xanthomonas campestris pathovar campestris: relatedness to
RT secretion systems of other Gram-negative bacteria.";
RL Mol. Gen. Genet. 229:357-364(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Xc1701;
RA Hu N.-T.T., Hung M.-N., Wang K.C.;
RL Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11931643; DOI=10.1042/bj20020194;
RA Hu N.T., Leu W.M., Lee M.S., Chen A., Chen S.C., Song Y.L., Chen L.Y.;
RT "XpsG, the major pseudopilin in Xanthomonas campestris pv. campestris,
RT forms a pilus-like structure between cytoplasmic and outer membranes.";
RL Biochem. J. 365:205-211(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH XPSN AND XPSD.
RX PubMed=15590656; DOI=10.1074/jbc.m409362200;
RA Lee M.S., Chen L.Y., Leu W.M., Shiau R.J., Hu N.T.;
RT "Associations of the major pseudopilin XpsG with XpsN (GspC) and secretin
RT XpsD of Xanthomonas campestris pv. campestris type II secretion apparatus
RT revealed by cross-linking analysis.";
RL J. Biol. Chem. 280:4585-4591(2005).
RN [6]
RP FUNCTION, AND INTERACTION WITH XPSI; XPSJ AND XPSH.
RX PubMed=16078004; DOI=10.1007/s11373-005-7372-3;
RA Kuo W.W., Kuo H.W., Cheng C.C., Lai H.L., Chen L.Y.;
RT "Roles of the minor pseudopilins, XpsH, XpsI and XpsJ, in the formation of
RT XpsG-containing pseudopilus in Xanthomonas campestris pv. campestris.";
RL J. Biomed. Sci. 12:587-599(2005).
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:15590656,
CC PubMed:16078004). Pseudopilin (pilin-like) protein that polymerizes to
CC form the pseudopilus (PubMed:11931643). Further polymerization triggers
CC pseudopilus growth (PubMed:11931643). {ECO:0000269|PubMed:11931643,
CC ECO:0000269|PubMed:15590656, ECO:0000269|PubMed:16078004}.
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 (By similarity). Interacts with pseudopilin tip complex
CC component XpsJ as well as XpsI and XcpH (PubMed:16078004). Interacts
CC with XpsN and secretin XpsD (PubMed:15590656).
CC {ECO:0000250|UniProtKB:Q00514, ECO:0000269|PubMed:15590656,
CC ECO:0000269|PubMed:16078004}.
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 methionine once the leader sequence is cleaved.
CC {ECO:0000250|UniProtKB:Q00514}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants can no longer assemble into the
CC pillar-like structure. {ECO:0000269|PubMed:11931643}.
CC -!- SIMILARITY: Belongs to the GSP G family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59079; CAA41805.1; -; Genomic_DNA.
DR EMBL; L02630; AAC27377.1; -; Genomic_DNA.
DR EMBL; AE008922; AAM39978.1; -; Genomic_DNA.
DR PIR; S17939; S17939.
DR RefSeq; NP_636054.1; NC_003902.1.
DR RefSeq; WP_011035902.1; NC_003902.1.
DR AlphaFoldDB; P31734; -.
DR SMR; P31734; -.
DR STRING; 340.xcc-b100_3693; -.
DR EnsemblBacteria; AAM39978; AAM39978; XCC0662.
DR GeneID; 58014778; -.
DR KEGG; xcc:XCC0662; -.
DR PATRIC; fig|190485.4.peg.727; -.
DR eggNOG; COG2165; Bacteria.
DR HOGENOM; CLU_091705_2_0_6; -.
DR OMA; VAPKYFS; -.
DR Proteomes; UP000001010; 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; 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;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT PROPEP 1..17
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000449510"
FT CHAIN 18..143
FT /note="Type II secretion system core protein G"
FT /id="PRO_0000024213"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 18
FT /note="N-methylmethionine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ SEQUENCE 143 AA; 15148 MW; 41E4416A16D23401 CRC64;
MIKRSITRSP SRAGQAGMSL LEIIIVIVLI GAVLTLVGSR VLGGADRGKA NLAKSQIQTL
AGKIENFQLD TGKLPSKLDD LVTQPGGSSG WLGPYAKPVE LNDPWGHTIE YRVPGDGQAF
DLISLGKDGR PGGSSYDSDI KYQ
