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GSPI_ECOLI
ID   GSPI_ECOLI              Reviewed;         125 AA.
AC   P45760; Q2M6Z5;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Putative type II secretion system protein I;
DE            Short=T2SS minor pseudopilin I;
DE   AltName: Full=Putative general secretion pathway protein I;
DE   Flags: Precursor;
GN   Name=gspI; Synonyms=yheH; OrderedLocusNames=b3330, JW5706;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   LACK OF EXPRESSION.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=8655552; DOI=10.1128/jb.178.12.3544-3549.1996;
RA   Francetic O., Pugsley A.P.;
RT   "The cryptic general secretory pathway (gsp) operon of Escherichia coli K-
RT   12 encodes functional proteins.";
RL   J. Bacteriol. 178:3544-3549(1996).
RN   [4]
RP   LACK OF EXPRESSION, AND TRANSCRIPTIONAL REGULATION.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=11118204; DOI=10.1093/emboj/19.24.6697;
RA   Francetic O., Belin D., Badaut C., Pugsley A.P.;
RT   "Expression of the endogenous type II secretion pathway in Escherichia coli
RT   leads to chitinase secretion.";
RL   EMBO J. 19:6697-6703(2000).
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 GspG. {ECO:0000250|UniProtKB:Q00516}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:Q00516}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: Silenced by the DNA-binding protein H-NS under standard
CC       growth conditions. {ECO:0000269|PubMed:11118204}.
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 methionine once the leader sequence is cleaved by prepilin
CC       peptidase. {ECO:0000250|UniProtKB:Q00516}.
CC   -!- MISCELLANEOUS: Part of a cryptic operon that encodes proteins involved
CC       in type II secretion machinery in other organisms, but is not expressed
CC       in strain K12.
CC   -!- SIMILARITY: Belongs to the GSP I family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA58127.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U18997; AAA58127.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76355.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77961.1; -; Genomic_DNA.
DR   PIR; E65126; E65126.
DR   RefSeq; NP_417789.4; NC_000913.3.
DR   RefSeq; WP_001041743.1; NZ_STEB01000038.1.
DR   AlphaFoldDB; P45760; -.
DR   SMR; P45760; -.
DR   BioGRID; 4259596; 248.
DR   STRING; 511145.b3330; -.
DR   PaxDb; P45760; -.
DR   PRIDE; P45760; -.
DR   EnsemblBacteria; AAC76355; AAC76355; b3330.
DR   EnsemblBacteria; BAE77961; BAE77961; BAE77961.
DR   GeneID; 947833; -.
DR   KEGG; ecj:JW5706; -.
DR   KEGG; eco:b3330; -.
DR   PATRIC; fig|1411691.4.peg.3401; -.
DR   EchoBASE; EB2729; -.
DR   eggNOG; COG2165; Bacteria.
DR   HOGENOM; CLU_121289_7_0_6; -.
DR   InParanoid; P45760; -.
DR   PhylomeDB; P45760; -.
DR   BioCyc; EcoCyc:G7708-MON; -.
DR   BioCyc; MetaCyc:G7708-MON; -.
DR   PRO; PR:P45760; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; 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; IPR045584; Pilin-like.
DR   InterPro; IPR003413; T2SS_GspI_C.
DR   InterPro; IPR010052; T2SS_protein-GspI.
DR   PANTHER; PTHR38779; PTHR38779; 1.
DR   Pfam; PF07963; N_methyl; 1.
DR   Pfam; PF02501; T2SSI; 1.
DR   SUPFAM; SSF54523; SSF54523; 1.
DR   TIGRFAMs; TIGR01707; gspI; 1.
DR   TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR   PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE   2: Evidence at transcript level;
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_0000024232"
FT   CHAIN           7..125
FT                   /note="Putative type II secretion system protein I"
FT                   /id="PRO_0000024233"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         7
FT                   /note="N-methylmethionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ   SEQUENCE   125 AA;  13901 MW;  7BC1FB9B8192C2A4 CRC64;
     MNKQSGMTLL EVLLAMSIFT AVALTLMSSM QGQRNAIERM RNETLALWIA DNQLQSQDSF
     GEENTSSSGK ELINGEEWNW RSDIHSSKDG TLLERTITVT LPSGQTTSLT RYQSIDNKSG
     QAQDD
 
 
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