ID   PRSA_STAAM              Reviewed;         320 AA.
AC   P60747; Q99T36;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=SAV1841;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB58003.1; -; Genomic_DNA.
DR   RefSeq; WP_000782121.1; NC_002758.2.
DR   PDB; 2JZV; NMR; -; A=140-245.
DR   PDBsum; 2JZV; -.
DR   AlphaFoldDB; P60747; -.
DR   BMRB; P60747; -.
DR   SMR; P60747; -.
DR   World-2DPAGE; 0002:P60747; -.
DR   PaxDb; P60747; -.
DR   EnsemblBacteria; BAB58003; BAB58003; SAV1841.
DR   KEGG; sav:SAV1841; -.
DR   HOGENOM; CLU_034646_6_2_9; -.
DR   OMA; TMKGSTI; -.
DR   PhylomeDB; P60747; -.
DR   BioCyc; SAUR158878:SAV_RS09930-MON; -.
DR   EvolutionaryTrace; P60747; -.
DR   Proteomes; UP000002481; 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   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Isomerase; Lipoprotein; Membrane; Palmitate;
KW   Rotamase; 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_0000029318"
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"
FT   STRAND          140..151
FT                   /evidence="ECO:0007829|PDB:2JZV"
FT   STRAND          158..161
FT                   /evidence="ECO:0007829|PDB:2JZV"
FT   HELIX           163..178
FT                   /evidence="ECO:0007829|PDB:2JZV"
FT   HELIX           184..191
FT                   /evidence="ECO:0007829|PDB:2JZV"
FT   HELIX           195..198
FT                   /evidence="ECO:0007829|PDB:2JZV"
FT   TURN            199..202
FT                   /evidence="ECO:0007829|PDB:2JZV"
FT   STRAND          203..208
FT                   /evidence="ECO:0007829|PDB:2JZV"
FT   HELIX           214..221
FT                   /evidence="ECO:0007829|PDB:2JZV"
FT   STRAND          232..234
FT                   /evidence="ECO:0007829|PDB:2JZV"
FT   STRAND          237..243
FT                   /evidence="ECO:0007829|PDB:2JZV"
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