GSPH_XANCP
ID GSPH_XANCP Reviewed; 169 AA.
AC P31736;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Type II secretion system protein H;
DE Short=T2SS minor pseudopilin H;
DE AltName: Full=General secretion pathway protein H;
DE Flags: Precursor;
GN Name=xpsH; Synonyms=pefH; OrderedLocusNames=XCC0663;
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 INTERACTION WITH XPSG.
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 XPSG; XPSI AND XPSJ.
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: 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:Q00515}.
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 (By
CC similarity). Interacts with core component XpsG (PubMed:16078004).
CC Interacts with minor pseudopilins XpsI and XpsJ (PubMed:16078004).
CC {ECO:0000250|UniProtKB:Q00515, ECO:0000269|PubMed:16078004}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q00515}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Cleaved by prepilin peptidase. {ECO:0000250|UniProtKB:Q00515}.
CC -!- PTM: Methylated by prepilin peptidase at the amino group of the N-
CC terminal phenylalanine once the leader sequence is cleaved by prepilin
CC peptidase. {ECO:0000250|UniProtKB:Q00515}.
CC -!- SIMILARITY: Belongs to the GSP H family. {ECO:0000305}.
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DR EMBL; X59079; CAA41806.1; -; Genomic_DNA.
DR EMBL; L02630; AAC27378.1; -; Genomic_DNA.
DR EMBL; AE008922; AAM39979.1; -; Genomic_DNA.
DR PIR; S17940; S17940.
DR RefSeq; NP_636055.1; NC_003902.1.
DR RefSeq; WP_011035903.1; NC_003902.1.
DR AlphaFoldDB; P31736; -.
DR SMR; P31736; -.
DR STRING; 340.xcc-b100_3692; -.
DR EnsemblBacteria; AAM39979; AAM39979; XCC0663.
DR KEGG; xcc:XCC0663; -.
DR PATRIC; fig|190485.4.peg.728; -.
DR eggNOG; COG4970; Bacteria.
DR HOGENOM; CLU_123291_0_0_6; -.
DR OMA; RRWRIDI; -.
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; IPR045584; Pilin-like.
DR InterPro; IPR022346; T2SS_GspH.
DR InterPro; IPR002416; T2SS_protein-GspH.
DR Pfam; PF12019; GspH; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR01708; typeII_sec_gspH; 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..29
FT /note="Leader sequence"
FT /evidence="ECO:0000250|UniProtKB:Q00515"
FT /id="PRO_0000024228"
FT CHAIN 30..169
FT /note="Type II secretion system protein H"
FT /id="PRO_0000449530"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 30
FT /note="N-methylmethionine"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="L -> F (in Ref. 2; AAC27378)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="H -> S (in Ref. 2; AAC27378)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 169 AA; 18235 MW; A79455CD86205A87 CRC64;
MRVARLPLLH PHRAAPVVRR QLRGSSLLEM LLVIALIALA GVLAAAALTG GIDGMRLRSA
GKAIAAQLRY TRTQAIATGT PQRFLIDPQQ RRWEAPGGHH GDLPAALEVR FTGARQVQSR
QDQGAIQFFA DGASTGGRID LTIKDARWRV DVGWITGEVR SGPLRTPAP
