ID   PRSA_CLOPE              Reviewed;         342 AA.
AC   Q8XHK0;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=CPE2483;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(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; BA000016; BAB82189.1; -; Genomic_DNA.
DR   RefSeq; WP_011010923.1; NC_003366.1.
DR   AlphaFoldDB; Q8XHK0; -.
DR   SMR; Q8XHK0; -.
DR   STRING; 195102.gene:10491817; -.
DR   PRIDE; Q8XHK0; -.
DR   EnsemblBacteria; BAB82189; BAB82189; BAB82189.
DR   KEGG; cpe:CPE2483; -.
DR   HOGENOM; CLU_034646_5_2_9; -.
DR   OMA; QKAKNQY; -.
DR   Proteomes; UP000000818; 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;
KW   Reference proteome; Rotamase; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   CHAIN           23..342
FT                   /note="Foldase protein PrsA"
FT                   /id="PRO_0000029301"
FT   DOMAIN          189..284
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
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   342 AA;  38422 MW;  43C97AAAD4994AC9 CRC64;
     MVSVKKIVAS ALVGVLMFSA VGCNMVEKTQ AAIDKTTVAT VNGEKITLGE VDSHLKGVFA
     QMKSQYGDKY MDDPQVAQQI LQQRQSVVQG LVTDKVLGIE ADKLGIKPSE EEIKKKVDEQ
     FENIKKGMGD NFDKALEAEG YTEDTFKDVI KNQVINQAVQ DYIIKDVKVT DEDAQKYYDE
     NKQQFVAKDS GVLTKHLLFE NEEEAQKAYD EIQSGKTTFN DLFTKYQNNK SENKKPIAEN
     LGVVPAENSG LVQEFVDGLK PLKEGEISKP IKTQFGYHII QAGATYEKGA QLPFDEVKSQ
     IIQILKQQKD SEKFKADMDQ WKKDLNVKVY DDKLQEGLKI SK