ID   PRSA1_STRP8             Reviewed;         351 AA.
AC   Q8P0E5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Foldase protein PrsA 1;
DE            EC=5.2.1.8;
DE   Flags: Precursor;
GN   Name=prsA1; OrderedLocusNames=spyM18_1400;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA   Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA   Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18 group
RT   A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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; AE009949; AAL97991.1; -; Genomic_DNA.
DR   RefSeq; WP_011017938.1; NC_003485.1.
DR   AlphaFoldDB; Q8P0E5; -.
DR   SMR; Q8P0E5; -.
DR   KEGG; spm:spyM18_1400; -.
DR   HOGENOM; CLU_034646_6_0_9; -.
DR   OMA; TMKGSTI; -.
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; Rotamase;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..351
FT                   /note="Foldase protein PrsA 1"
FT                   /id="PRO_0000029335"
FT   DOMAIN          145..240
FT                   /note="PpiC"
FT   REGION          303..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   351 AA;  38533 MW;  5DB0499B1FAB1BC9 CRC64;
     MKNSNKLIAS VVTLASVMAL AACQSTNDNT KVISMKGDTI SVSDFYNETK NTEVSQKAML
     NLVISRVFEA QYGDKVSKKE VEKAYHKTAE QYGASFSAAL AQSSLTPETF KRQIRSSKLV
     EYAVKEAAKK ELTTQEYKKA YESYTPTMAV EMITLDNDET AKSVLEELKA EGADFTAIAK
     EKTTTPEKKV TYKFDSGAIN VPTDVVKAAS SLNEGGISDV ISVLDPTSYQ KKFYIVKVTK
     KAEKKSDWQE YKKRLKAIII AEKSKDMNFQ NKVIANALDK ANVKIKDKAF ANILAQYANL
     GQKTKAASES STTSESSKAA EENPSESEQT QTSSAEEPTE TEAQTQEPAA Q