ID   PRSA_LACLS              Reviewed;         299 AA.
AC   Q02VE3; P14308;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
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; OrderedLocusNames=LACR_C43;
OS   Lactococcus lactis subsp. cremoris (strain SK11).
OG   Plasmid pSK111, and Plasmid pLACR3.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=272622;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], POSSIBLE SUBCELLULAR LOCATION, AND ROLE
RP   IN PRTP PROTEASE SECRETION.
RC   PLASMID=pSK111;
RX   PubMed=2496115; DOI=10.1128/jb.171.5.2795-2802.1989;
RA   Vos P., van Asseldonk M., van Jeveren F., Siezen R., Simons G.,
RA   de Vos W.M.;
RT   "A maturation protein is essential for production of active forms of
RT   Lactococcus lactis SK11 serine proteinase located in or secreted from the
RT   cell envelope.";
RL   J. Bacteriol. 171:2795-2802(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK11; PLASMID=pLACR3;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-299.
RC   PLASMID=pSK111;
RX   PubMed=2166472; DOI=10.1128/aem.56.6.1890-1896.1990;
RA   Haandrikman A.J., van Leeuwen C., Kok J., Vos P., de Vos W.M., Venema G.;
RT   "Insertion elements on lactococcal proteinase plasmids.";
RL   Appl. Environ. Microbiol. 56:1890-1896(1990).
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       {ECO:0000269|PubMed:2496115}.
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; J04962; AAA03532.1; -; Unassigned_DNA.
DR   EMBL; CP000428; ABJ74079.1; -; Genomic_DNA.
DR   EMBL; M37395; AAA25209.1; -; Genomic_DNA.
DR   PIR; A32314; A32313.
DR   RefSeq; WP_011669080.1; NC_008505.1.
DR   AlphaFoldDB; Q02VE3; -.
DR   SMR; Q02VE3; -.
DR   MEROPS; X15.001; -.
DR   EnsemblBacteria; ABJ74079; ABJ74079; LACR_C43.
DR   KEGG; llc:LACR_C43; -.
DR   HOGENOM; CLU_034646_6_1_9; -.
DR   OMA; SEFGPGM; -.
DR   Proteomes; UP000000240; Plasmid pLACR3.
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; Plasmid;
KW   Rotamase; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..299
FT                   /note="Foldase protein PrsA"
FT                   /id="PRO_0000272037"
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;  33167 MW;  3A7B775DE3324F5B CRC64;
     MKKKMRLKVL LASTATALLL LSGCQSNQTD QTVATYSGGK VTESSFYKEL KQSPTTKTML
     ANMLIYRALN HAYGKSVSTK TVNDAYDSYK QQYGENFDAF LSQNGFSRSS FKESLRTNFL
     SEVALKKLKK VSESQLKAAW KTYQPKVTVQ HILTSDEDTA KQVISDLAAG KDFAMLAKTD
     SIDTATKDNG GKISFELNNK TLDATFKDAA YKLKNGDYTQ TPVKVTDGYE VIKMINHPAK
     GTFTSSKKAL TASVYAKWSR DSSIMQRVIS QVLKNQHVTI KDKDLADALD SYKKLATTN