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GSPI_PSEAE
ID   GSPI_PSEAE              Reviewed;         129 AA.
AC   Q00516;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Type II secretion system protein I;
DE            Short=T2SS minor pseudopilin I;
DE   AltName: Full=General secretion pathway protein I;
DE   AltName: Full=PilD-dependent protein PddC;
DE   Flags: Precursor;
GN   Name=xcpV; Synonyms=pddC; OrderedLocusNames=PA3099;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=1588814; DOI=10.1111/j.1365-2958.1992.tb01550.x;
RA   Bally M., Filloux A., Akrim M., Ball G., Lazdunski A., Tommassen J.;
RT   "Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp
RT   genes and processing of secretory apparatus components by prepilin
RT   peptidase.";
RL   Mol. Microbiol. 6:1121-1131(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1309616; DOI=10.1073/pnas.89.1.47;
RA   Nunn D.N., Lory S.;
RT   "Components of the protein-excretion apparatus of Pseudomonas aeruginosa
RT   are processed by the type IV prepilin peptidase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:47-51(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [4]
RP   SUBCELLULAR LOCATION, CLEAVAGE, AND METHYLATION AT PHE-7.
RC   STRAIN=PAK;
RX   PubMed=8331069; DOI=10.1128/jb.175.14.4375-4382.1993;
RA   Nunn D.N., Lory S.;
RT   "Cleavage, methylation, and localization of the Pseudomonas aeruginosa
RT   export proteins XcpT, -U, -V, and -W.";
RL   J. Bacteriol. 175:4375-4382(1993).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH XCPT.
RX   PubMed=9282737; DOI=10.1046/j.1365-2958.1997.4561818.x;
RA   Lu H.M., Motley S.T., Lory S.;
RT   "Interactions of the components of the general secretion pathway: role of
RT   Pseudomonas aeruginosa type IV pilin subunits in complex formation and
RT   extracellular protein secretion.";
RL   Mol. Microbiol. 25:247-259(1997).
RN   [6]
RP   FUNCTION.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=12700254; DOI=10.1128/jb.185.9.2749-2758.2003;
RA   Durand E., Bernadac A., Ball G., Lazdunski A., Sturgis J.N., Filloux A.;
RT   "Type II protein secretion in Pseudomonas aeruginosa: the pseudopilus is a
RT   multifibrillar and adhesive structure.";
RL   J. Bacteriol. 185:2749-2758(2003).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH XCPU; XCPW AND XCPX.
RX   PubMed=19828448; DOI=10.1074/jbc.m109.042366;
RA   Douzi B., Durand E., Bernard C., Alphonse S., Cambillau C., Filloux A.,
RA   Tegoni M., Voulhoux R.;
RT   "The XcpV/GspI pseudopilin has a central role in the assembly of a
RT   quaternary complex within the T2SS pseudopilus.";
RL   J. Biol. Chem. 284:34580-34589(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 33-129, FUNCTION, INTERACTION
RP   WITH XCPW, AND DISRUPTION PHENOTYPE.
RX   PubMed=30346996; DOI=10.1371/journal.ppat.1007343;
RA   Zhang Y., Faucher F., Zhang W., Wang S., Neville N., Poole K., Zheng J.,
RA   Jia Z.;
RT   "Structure-guided disruption of the pseudopilus tip complex inhibits the
RT   Type II secretion in Pseudomonas aeruginosa.";
RL   PLoS Pathog. 14:E1007343-E1007343(2018).
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 (PubMed:9282737). Part of the pseudopilus
CC       tip complex that is critical for the recognition and binding of
CC       secretion substrates (PubMed:19828448). Type II pseudopilus confers
CC       increased bacterial adhesive capabilities (PubMed:12700254).
CC       {ECO:0000269|PubMed:12700254, ECO:0000269|PubMed:19828448,
CC       ECO:0000269|PubMed:9282737}.
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. Forms the tip
CC       of the type II pseudopilus by interacting with XcpU, XcpW and XcpX
CC       (PubMed:19828448, PubMed:30346996). Interacts with core component XcpT
CC       (PubMed:9282737). {ECO:0000269|PubMed:19828448,
CC       ECO:0000269|PubMed:30346996, ECO:0000269|PubMed:9282737}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8331069};
CC       Single-pass membrane protein {ECO:0000255}.
CC   -!- PTM: Cleaved by prepilin peptidase. {ECO:0000269|PubMed:8331069}.
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:0000269|PubMed:8331069}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant results in a non-functional T2SS
CC       system. {ECO:0000269|PubMed:30346996}.
CC   -!- SIMILARITY: Belongs to the GSP I family. {ECO:0000305}.
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DR   EMBL; X62666; CAA44537.1; -; Genomic_DNA.
DR   EMBL; M80792; AAA25948.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG06487.1; -; Genomic_DNA.
DR   PIR; S25388; SKPSXV.
DR   RefSeq; NP_251789.1; NC_002516.2.
DR   RefSeq; WP_003103528.1; NZ_QZGE01000009.1.
DR   PDB; 5BW0; X-ray; 2.00 A; B/D/F/H=33-126.
DR   PDB; 5VTM; X-ray; 2.04 A; V=38-129.
DR   PDB; 6UTU; X-ray; 2.85 A; A/D/G=38-129.
DR   PDBsum; 5BW0; -.
DR   PDBsum; 5VTM; -.
DR   PDBsum; 6UTU; -.
DR   AlphaFoldDB; Q00516; -.
DR   SMR; Q00516; -.
DR   STRING; 287.DR97_4834; -.
DR   PaxDb; Q00516; -.
DR   PRIDE; Q00516; -.
DR   DNASU; 882777; -.
DR   EnsemblBacteria; AAG06487; AAG06487; PA3099.
DR   GeneID; 882777; -.
DR   KEGG; pae:PA3099; -.
DR   PATRIC; fig|208964.12.peg.3251; -.
DR   PseudoCAP; PA3099; -.
DR   HOGENOM; CLU_121289_5_0_6; -.
DR   InParanoid; Q00516; -.
DR   OMA; RTWYWQQ; -.
DR   PhylomeDB; Q00516; -.
DR   BioCyc; PAER208964:G1FZ6-3155-MON; -.
DR   Proteomes; UP000002438; 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; IDA:PseudoCAP.
DR   GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
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   1: Evidence at protein level;
KW   3D-structure; 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                   ECO:0000269|PubMed:8331069"
FT                   /id="PRO_0000024240"
FT   CHAIN           7..129
FT                   /note="Type II secretion system protein I"
FT                   /id="PRO_0000024241"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         7
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT   HELIX           37..59
FT                   /evidence="ECO:0007829|PDB:5BW0"
FT   STRAND          66..75
FT                   /evidence="ECO:0007829|PDB:5BW0"
FT   STRAND          78..88
FT                   /evidence="ECO:0007829|PDB:5BW0"
FT   STRAND          95..103
FT                   /evidence="ECO:0007829|PDB:5BW0"
FT   HELIX           113..116
FT                   /evidence="ECO:0007829|PDB:5BW0"
FT   STRAND          118..125
FT                   /evidence="ECO:0007829|PDB:5BW0"
SQ   SEQUENCE   129 AA;  14380 MW;  1111903A96393545 CRC64;
     MKRARGFTLL EVLVALAIFA MVAASVLSAS ARSLQNASRL EDKTLAMWIA DNRLNELQLE
     QTPPSSGRNQ GELEFAGRRW EWRTQVDSTA EQDMRRVIVW VAAKPLGRER GSIEERAAAR
     LVGFLGSQP
 
 
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