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Database: UniProt
Entry: P60811
LinkDB: P60811
Original site: P60811 
ID   PRSA1_STRP1             Reviewed;         351 AA.
AC   P60811; Q48Y24; Q99Z56;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, 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; OrderedLocusNames=SPy_1390, M5005_Spy1133;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J.,
RA   Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J.,
RA   Hoe N.P., Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of
RT   serotype M1 group A Streptococcus involved multiple horizontal gene
RT   transfer events.";
RL   J. Infect. Dis. 192:771-782(2005).
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; AE004092; AAK34209.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ51751.1; -; Genomic_DNA.
DR   RefSeq; NP_269488.1; NC_002737.1.
DR   RefSeq; YP_282496.1; NC_007297.1.
DR   ProteinModelPortal; P60811; -.
DR   STRING; 160490.SPy_1390; -.
DR   PaxDb; P60811; -.
DR   EnsemblBacteria; AAK34209; AAK34209; SPy_1390.
DR   EnsemblBacteria; AAZ51751; AAZ51751; M5005_Spy1133.
DR   GeneID; 3571757; -.
DR   GeneID; 901457; -.
DR   KEGG; spy:SPy_1390; -.
DR   KEGG; spz:M5005_Spy_1133; -.
DR   PATRIC; 19716296; VBIStrPyo79812_1212.
DR   eggNOG; COG0760; -.
DR   HOGENOM; HOG000014032; -.
DR   KO; K07533; -.
DR   OMA; LYEMMAQ; -.
DR   OrthoDB; EOG66XBH5; -.
DR   BioCyc; SPYO160490:GJ81-1144-MONOMER; -.
DR   BioCyc; SPYO293653:GHFC-1192-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   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; Reference proteome; Rotamase; Signal.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23    351       Foldase protein PrsA 1.
FT                                /FTId=PRO_0000029329.
FT   DOMAIN      145    240       PpiC.
FT   LIPID        23     23       N-palmitoyl cysteine. {ECO:0000255}.
FT   LIPID        23     23       S-diacylglycerol cysteine. {ECO:0000255}.
SQ   SEQUENCE   351 AA;  38535 MW;  EE3A620A26EEF3A8 CRC64;
     MKNSNKLIAS VVTLASVMAL AACQSTNDNT KVISMKGDTI SVSDFYNETK NTEVSQKAML
     NLVISRVFEA QYGDKVSKKE VEKAYHKTAE QYGASFSAAL AQSSLTPETF KRQIRSSKLV
     EYAVKEAAKK ELTTQEYKKA YESYTPTMAV EMITLDNEET AKSVLEELKA EGADFTAIAK
     EKTTTPEKKV TYKFDSGATN VPTDVVKAAS SLNEGGISDV ISVLDPTSYQ KKFYIVKVTK
     KAEKKSDWQE YKKRLKAIII AEKSKDMNFQ NKVIANALDK ANVKIKDKAF ANILAQYANL
     GQKTKAASES STTSESSKAA EENPSESEQT QTSSAEEPTE TEAQTQEPAA Q
//
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