ID   PRSA_STRS7              Reviewed;         333 AA.
AC   C0MCT3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Foldase protein PrsA {ECO:0000255|HAMAP-Rule:MF_01145};
DE            EC=5.2.1.8 {ECO:0000255|HAMAP-Rule:MF_01145};
DE   Flags: Precursor;
GN   Name=prsA {ECO:0000255|HAMAP-Rule:MF_01145}; OrderedLocusNames=SZO_13310;
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
CC   -!- FUNCTION: Plays a major role in protein secretion by helping the post-
CC       translocational extracellular folding of several secreted proteins.
CC       {ECO:0000255|HAMAP-Rule:MF_01145}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01145};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01145};
CC       Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01145}.
CC   -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01145}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FM204884; CAW99882.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MCT3; -.
DR   SMR; C0MCT3; -.
DR   EnsemblBacteria; CAW99882; CAW99882; SZO_13310.
DR   KEGG; seq:SZO_13310; -.
DR   PATRIC; fig|40041.11.peg.1413; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_6_0_9; -.
DR   OMA; TMKGSTI; -.
DR   Proteomes; UP000001368; 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; Rotamase;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   CHAIN           23..333
FT                   /note="Foldase protein PrsA"
FT                   /id="PRO_5000453429"
FT   DOMAIN          145..240
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   REGION          301..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
SQ   SEQUENCE   333 AA;  36560 MW;  4EC1BB274295E6E3 CRC64;
     MKKSTKLLAG IVTLASAMTL AACQSTNDNT SVITMKGDTI SVSDFYNETK NTEVSQRAML
     NLVVSRVFED QYGKKVSKKK TEEAYNKSAE QYGASFSAAL AQSGLTTDTY KRQIRSAMLV
     EYAVKEAAKK ELTDADYKKA YESYTPEMTT QVITLDNEET AKAILGEVKA EGADFAAIAK
     EKTTAADKKV DYKFDSGDTK LPADVIKAAS GLKEGDISEV VSVLDPATYQ NKFYIVKVTK
     KAEKASDWKK YKKRLKEIVL AEKTQNIDFQ NKVIAKALDK ANVKIKDQAF ANILAQYANT
     DKKASKANTS KSDQKTSSDS SKDSQSSKSK SEK