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Database: UniProt
Entry: C0M9L5
LinkDB: C0M9L5
Original site: C0M9L5 
ID   PRSA_STRE4              Reviewed;         333 AA.
AC   C0M9L5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   14-MAY-2014, entry version 35.
DE   RecName: Full=Foldase protein PrsA;
DE            EC=5.2.1.8;
DE   Flags: Precursor;
GN   Name=prsA; OrderedLocusNames=SEQ_0694;
OS   Streptococcus equi subsp. equi (strain 4047).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4047;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K.,
RA   Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K.,
RA   Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K.,
RA   Aanensen D.M., Spratt B.G., Jolley K.A., Maiden M.C.J., Kehoe M.,
RA   Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J.,
RA   Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
CC   -!- FUNCTION: Plays a major role in protein secretion by helping the
CC       post-translocational extracellular folding of several secreted
CC       proteins (By similarity).
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor (Potential).
CC   -!- SIMILARITY: Belongs to the PrsA family.
CC   -!- SIMILARITY: Contains 1 PpiC domain.
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DR   EMBL; FM204883; CAW93050.1; -; Genomic_DNA.
DR   RefSeq; YP_002746044.1; NC_012471.1.
DR   STRING; 553482.SEQ_0694; -.
DR   EnsemblBacteria; CAW93050; CAW93050; SEQ_0694.
DR   GeneID; 7696128; -.
DR   KEGG; seu:SEQ_0694; -.
DR   PATRIC; 19646170; VBIStrEqu13040_0708.
DR   eggNOG; COG0760; -.
DR   HOGENOM; HOG000014032; -.
DR   KO; K07533; -.
DR   OMA; MLVEYAV; -.
DR   OrthoDB; EOG66XBH5; -.
DR   BioCyc; SEQU553482:GJOY-706-MONOMER; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Pfam; PF13145; Rotamase_2; 1.
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; Rotamase; Signal.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    333       Foldase protein PrsA.
FT                                /FTId=PRO_5000453274.
FT   DOMAIN      145    240       PpiC.
FT   LIPID        23     23       N-palmitoyl cysteine (Potential).
FT   LIPID        23     23       S-diacylglycerol cysteine (Potential).
SQ   SEQUENCE   333 AA;  36562 MW;  400FA76118B30A1D CRC64;
     MKKSTKLLAG IVTLASAMTL AACQSTNDNT SVITMKGDTI SVSDFYNETK NTEISQRAML
     NLVVSRVFED QYGKKVSKKR TEEAYNKSAE QYGASFSAAL AQSGLTTDTY KRQIRSAMLV
     EYAVKEAAKK ELTDADYKKA YESYTPEMTT QVTTLDNEET AKAVLGEVKA EGADFAAIAK
     EKTTAADKKV DYKFDSGDTK LPADVIKAAS GLKEGDISEV VSVLDPATYQ NKFYIVKVTK
     KAEKASDWKK YKKRLKEIVL AEKTQNIDFQ NKVIAKALDK ANVKIKDQAF ANILAQYANT
     DKKASKANTS KSDQKSSSDS SKDSQSSKSK SEK
//
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