GenomeNet

Database: UniProt
Entry: Q88X05
LinkDB: Q88X05
Original site: Q88X05 
ID   PRSA1_LACPL             Reviewed;         298 AA.
AC   Q88X05; F9UNJ3;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   29-OCT-2014, entry version 69.
DE   RecName: Full=Foldase protein PrsA 1;
DE            EC=5.2.1.8;
DE   Flags: Precursor;
GN   Name=prsA1; Synonyms=prtM1; OrderedLocusNames=lp_1452;
OS   Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D.,
RA   Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M.,
RA   Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A.,
RA   Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B.,
RA   De Vos W.M., Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
CC   -!- FUNCTION: Plays a major role in protein secretion by helping the
CC       post-translocational extracellular folding of several secreted
CC       proteins. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PpiC domain. {ECO:0000305}.
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DR   EMBL; AL935263; CCC78782.1; -; Genomic_DNA.
DR   RefSeq; YP_004889296.1; NC_004567.2.
DR   ProteinModelPortal; Q88X05; -.
DR   STRING; 220668.lp_1452; -.
DR   EnsemblBacteria; CCC78782; CCC78782; lp_1452.
DR   GeneID; 1062391; -.
DR   KEGG; lpl:lp_1452; -.
DR   PATRIC; 22249145; VBILacPla27411_1215.
DR   eggNOG; COG0760; -.
DR   HOGENOM; HOG000014031; -.
DR   KO; K07533; -.
DR   OMA; YSSHISD; -.
DR   BioCyc; LPLA220668-WGS:GSPK-1243-MONOMER; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01145; Foldase_PrsA; 1.
DR   InterPro; IPR023059; Foldase_PrsA.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Isomerase; Lipoprotein; Membrane;
KW   Palmitate; Reference proteome; Rotamase; Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    298       Foldase protein PrsA 1.
FT                                /FTId=PRO_0000029307.
FT   DOMAIN      136    232       PpiC.
FT   LIPID        20     20       N-palmitoyl cysteine. {ECO:0000255}.
FT   LIPID        20     20       S-diacylglycerol cysteine. {ECO:0000255}.
SQ   SEQUENCE   298 AA;  32619 MW;  342E76C1B8997326 CRC64;
     MKKWLIALAG VLLTFTLAGC GSKTVASTSG GKITESQYYS SMKGTSSGKQ VLQQMILNKV
     LEKDYGSKVS TKQVTKQYNT YKSQYGSSFS TVLSQNGLTT KTFKEQLRSN LLLKEAVKDK
     VKITDKALKK QWKSYEPKVT VQHILVAKSA TADKVLDALK KDSSQANFTK LAKKYSTDTT
     TKNDGGKLSA FDNTNTSYSS KFLTAAFKLK NGEYTTSAVK TSNGYEIIRM IKNPGKGKMS
     DHTADLKKQI WDNDMSDSTV LQNVVSKVLK GGNVSIKDND LKDILSSYLS TSSSSSSN
//
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