ID   PRSA_LACPA              Reviewed;         299 AA.
AC   Q02473;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Foldase protein PrsA;
DE            EC=5.2.1.8;
DE   AltName: Full=Protease maturation protein PrtM;
DE   Flags: Precursor;
GN   Name=prsA; Synonyms=prtM;
OS   Lacticaseibacillus paracasei (Lactobacillus paracasei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25302 / DSM 5622 / BCRC 12248 / JCM 8130 / KCTC 3510 / LMG
RC   13087 / NBRC 15889 / NCDO 151 / RO94;
RX   PubMed=1512565; DOI=10.1099/00221287-138-7-1353;
RA   Holck A., Naes H.;
RT   "Cloning, sequencing and expression of the gene encoding the cell-envelope-
RT   associated proteinase from Lactobacillus paracasei subsp. paracasei NCDO
RT   151.";
RL   J. Gen. Microbiol. 138:1353-1364(1992).
CC   -!- FUNCTION: This protein is essential for production of active forms of
CC       the serine proteinase located in or secreted from the cell envelope.
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; M83946; AAA25247.1; -; Genomic_DNA.
DR   PIR; A44858; A44858.
DR   RefSeq; WP_003661851.1; NZ_LKFN01000095.1.
DR   AlphaFoldDB; Q02473; -.
DR   SMR; Q02473; -.
DR   MEROPS; X15.001; -.
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; IPR023058; PPIase_PpiC_CS.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   Pfam; PF00639; Rotamase; 1.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..299
FT                   /note="Foldase protein PrsA"
FT                   /id="PRO_0000029306"
FT   DOMAIN          144..236
FT                   /note="PpiC"
FT   LIPID           24
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           24
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   299 AA;  33146 MW;  B9CF1EAB2F8C5867 CRC64;
     MKKKMRLKVL LASTATALLL LSGCQSNQAD QKVATYSGGK VTESNFYKEL KQSPTTKTML
     ANMLIYRALN HAYGKSVSTK TVNDAYDSYK QQYGENFDAF LSQNGFSRSS FKESLRTNFL
     SEVALKKLKK VSESQLKAVW KTYQPKVTVQ HILTSDEDTA KQVISDLAAG KDFATLAKTD
     SIDTATKDNG GKISFESNNK TLDATFKDAA YKLKNGDYTQ TPVKVTNGYE VIKMINHPAK
     GTFTSSKKAL TASVYAKWSR DSSIMQRVIS QVLKNQHVTI KDKDLADALD SYKKPATTN