ID   PRSA2_STRPQ             Reviewed;         309 AA.
AC   P0DD45; Q8K5P3;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Foldase protein PrsA 2;
DE            EC=5.2.1.8;
DE   Flags: Precursor;
GN   Name=prsA2; OrderedLocusNames=SPs1736;
OS   Streptococcus pyogenes serotype M3 (strain SSI-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=193567;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSI-1;
RX   PubMed=12799345; DOI=10.1101/gr.1096703;
RA   Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA   Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA   Hattori M., Hamada S.;
RT   "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT   scale genomic rearrangement in invasive strains and new insights into phage
RT   evolution.";
RL   Genome Res. 13:1042-1055(2003).
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; BA000034; BAC64831.1; -; Genomic_DNA.
DR   RefSeq; WP_002993567.1; NC_004606.1.
DR   AlphaFoldDB; P0DD45; -.
DR   SMR; P0DD45; -.
DR   KEGG; sps:SPs1736; -.
DR   HOGENOM; CLU_034646_6_0_9; -.
DR   OMA; SEFGPGM; -.
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..309
FT                   /note="Foldase protein PrsA 2"
FT                   /id="PRO_0000411462"
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;  34361 MW;  38DA7FFB2B1A02E8 CRC64;
     MKQMNKLITG VVTLATVVTL SACQSSHNNT KLVSMKGDTI TVSDFYNETK NTELAQKAML
     SLVISRVFET QYANKVSDKE VEKAYKQTAD QYGTSFKTVL AQSGLTPETY KKQIRLTKLV
     EYAVKEQAKN ETISKKDYRQ AYDAYTPTMT AEIMQFEKEE DAKAALEAVK AEGADFAAIA
     KEKTIAADKK TTYTFDSGET TLPAEVVRAA SGLKEGNRSE IITALDPATS KRTYHIIKVT
     KKATKKADWK AYQKRLKDII VTGKLKDPDF QNKVIAKALD KANVKIKDKA FANILAQFAK
     PNQKQPAQK