ID   PRSA_STAAW              Reviewed;         320 AA.
AC   P60749; Q99T36;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=MW1782;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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}.
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DR   EMBL; BA000033; BAB95647.1; -; Genomic_DNA.
DR   RefSeq; WP_000782121.1; NC_003923.1.
DR   AlphaFoldDB; P60749; -.
DR   SMR; P60749; -.
DR   EnsemblBacteria; BAB95647; BAB95647; BAB95647.
DR   KEGG; sam:MW1782; -.
DR   HOGENOM; CLU_034646_6_2_9; -.
DR   OMA; TMKGSTI; -.
DR   Proteomes; UP000000418; 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; PF00639; Rotamase; 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..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   CHAIN           21..320
FT                   /note="Foldase protein PrsA"
FT                   /id="PRO_0000029322"
FT   DOMAIN          139..245
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   REGION          159..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
SQ   SEQUENCE   320 AA;  35638 MW;  16A0E692B1A78561 CRC64;
     MKMINKLIVP VTASALLLGA CGASATDSKE NTLISSKAGD VTVADTMKKI GKDQIANASF
     TEMLNKILAD KYKNKVNDKK IDEQIEKMQK QYGGKDKFEK ALQQQGLTAD KYKENLRTAA
     YHKELLSDKI KISDSEIKED SKKASHILIK VKSKKSDKEG LDDKEAKQKA EEIQKEVSKD
     PSKFGEIAKK ESMDTGSAKK DGELGYVLKG QTDKDFEKAL FKLKDGEVSE VVKSSFGYHI
     IKADKPTDFN SEKQSLKEKL VDQKVQKNPK LLTDAYKDLL KEYDVDFKDR DIKSVVEDKI
     LNPEKLKQGG AQGGQSGMSQ