ID   PRSA1_STRPQ             Reviewed;         351 AA.
AC   P0DD43; P60751; Q99Z56;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Foldase protein PrsA 1;
DE            EC=5.2.1.8;
DE   Flags: Precursor;
GN   Name=prsA1; OrderedLocusNames=SPs0804;
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; BAC63899.1; -; Genomic_DNA.
DR   RefSeq; WP_002984003.1; NC_004606.1.
DR   AlphaFoldDB; P0DD43; -.
DR   SMR; P0DD43; -.
DR   KEGG; sps:SPs0804; -.
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_0000411461"
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;  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