GSPI_XANCP
ID GSPI_XANCP Reviewed; 138 AA.
AC P31738;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Type II secretion system protein I;
DE Short=T2SS minor pseudopilin I;
DE AltName: Full=General secretion pathway protein I;
DE Flags: Precursor;
GN Name=xpsI; Synonyms=pefI; OrderedLocusNames=XCC0664;
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 (NOV-2004) 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).
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:Q00516}.
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. Interacts with
CC core component XpsG. {ECO:0000250|UniProtKB:Q00516}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q00516}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Cleaved by prepilin peptidase. {ECO:0000250|UniProtKB:Q00516}.
CC -!- PTM: Methylated by prepilin peptidase at the amino group of the N-
CC terminal tyrosine once the leader sequence is cleaved by prepilin
CC peptidase. {ECO:0000250|UniProtKB:Q00516}.
CC -!- SIMILARITY: Belongs to the GSP I family. {ECO:0000305}.
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DR EMBL; X59079; CAA41807.1; -; Genomic_DNA.
DR EMBL; L02630; AAC27379.2; -; Genomic_DNA.
DR EMBL; AE008922; AAM39980.1; -; Genomic_DNA.
DR PIR; S17941; S17941.
DR RefSeq; NP_636056.1; NC_003902.1.
DR RefSeq; WP_011035904.1; NC_003902.1.
DR AlphaFoldDB; P31738; -.
DR SMR; P31738; -.
DR STRING; 340.xcc-b100_3691; -.
DR EnsemblBacteria; AAM39980; AAM39980; XCC0664.
DR KEGG; xcc:XCC0664; -.
DR PATRIC; fig|190485.4.peg.729; -.
DR eggNOG; COG2165; Bacteria.
DR HOGENOM; CLU_130289_0_0_6; -.
DR OMA; WRTTILP; -.
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; IBA:GO_Central.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IBA:GO_Central.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR010052; T2SS_protein-GspI.
DR PANTHER; PTHR38779; PTHR38779; 1.
DR Pfam; PF07963; N_methyl; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Methylation;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT PROPEP 1..6
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000024244"
FT CHAIN 7..138
FT /note="Type II secretion system protein I"
FT /id="PRO_0000024245"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 7
FT /note="N-methyltyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT CONFLICT 22
FT /note="A -> V (in Ref. 2; AAC27379)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="D -> E (in Ref. 2; AAC27379)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="N -> S (in Ref. 2; AAC27379)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 138 AA; 15125 MW; 01784CF20C74F941 CRC64;
MKHQRGYSLI EVIVAFALLA LALTLLLGSL SGAARQVRGA DDSTRATLHA QSLLAVQGME
QPLVPGQQQG SLEDGHFRWS LDVRPYDEPR RNAQAPVDPS APTLLQLTLV VRWGEQPNQR
LLWRTLRLVT ATAQGNPA
