ID   PRSA2_STRP1             Reviewed;         309 AA.
AC   P60812; Q48WC5; Q99XT9;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Foldase protein PrsA 2;
DE            EC=5.2.1.8;
DE   Flags: Precursor;
GN   Name=prsA2; OrderedLocusNames=SPy_2037, M5005_Spy1732;
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., Yuan X.,
RA   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., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
CC   -!- FUNCTION: Plays a major role in protein secretion by helping the post-
CC       translocational extracellular folding of several secreted proteins.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000305}.
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DR   EMBL; AE004092; AAK34705.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ52350.1; -; Genomic_DNA.
DR   RefSeq; NP_269984.1; NC_002737.2.
DR   AlphaFoldDB; P60812; -.
DR   SMR; P60812; -.
DR   STRING; 1314.HKU360_01849; -.
DR   PaxDb; P60812; -.
DR   EnsemblBacteria; AAK34705; AAK34705; SPy_2037.
DR   KEGG; spy:SPy_2037; -.
DR   KEGG; spz:M5005_Spy1732; -.
DR   PATRIC; fig|160490.10.peg.1765; -.
DR   HOGENOM; CLU_034646_6_0_9; -.
DR   OMA; SEFGPGM; -.
DR   Proteomes; UP000000750; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.50.40; -; 1.
DR   HAMAP; MF_01145; Foldase_PrsA; 1.
DR   InterPro; IPR023059; Foldase_PrsA.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
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; Isomerase; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Rotamase; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..309
FT                   /note="Foldase protein PrsA 2"
FT                   /id="PRO_0000029330"
FT   DOMAIN          146..241
FT                   /note="PpiC"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   309 AA;  34349 MW;  38DA6E0B27EA1FE8 CRC64;
     MKQMNKLITG VVTLATVVTL SACQSSHNNT KLVSMKGDTI TVSDFYNETK NTELAQKAML
     SLVISRVFET QYANKVSDKE VEKAYKQTAD QYGTSFKTVL AQSGLTPETY KKQIRLTKLV
     EYAVKEQAKN ETISKKDYRQ AYDAYTPTMT AEIMQFEKEE DAKAALEAVK AEGADFAAIA
     KEKTTAADKK TTYTFDSGET TLPAEVVRAA SGLKEGNRSE IITALDPATS KRTYHIIKVT
     KKATKKADWK AYQKRLKDII VTGKLKDPDF QNKVIAKALD KANVKIKDKA FANILAQFAK
     PNQKQPAQK