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 01-MAY-2013, entry version 61.
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 (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; 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 ProtClustDB; PRK01326; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:HAMAP.
DR GO; GO:0006457; P:protein folding; IEA:HAMAP.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
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; Trigger_fac_C_bac; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; FALSE_NEG.
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 23 351 Foldase protein PrsA 1.
FT /FTId=PRO_0000029329.
FT DOMAIN 145 240 PpiC.
FT LIPID 23 23 N-palmitoyl cysteine (Potential).
FT LIPID 23 23 S-diacylglycerol cysteine (Potential).
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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