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Database: UniProt
Entry: P0C2B5
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Original site: P0C2B5 
ID   PRSA_LACLC              Reviewed;         299 AA.
AC   P0C2B5; P14308; P15294; Q53962; Q9AIQ3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   16-APR-2014, entry version 35.
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   Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OG   Plasmid pLP763, Plasmid pWV05, and Plasmid pHP003.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Wg2;
RX   PubMed=2708318;
RA   Haandrikman A.J., Kok J., Laan H., Soemitro S., Ledeboer A.M.,
RA   Konings W.N., Venema G.;
RT   "Identification of a gene required for maturation of an extracellular
RT   lactococcal serine proteinase.";
RL   J. Bacteriol. 171:2789-2794(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCDO 763 / ML3; PLASMID=pLP763;
RX   PubMed=2501630; DOI=10.1111/j.1365-2958.1989.tb00181.x;
RA   Kiwaki M., Ikemura H., Shimizu-Kadota M., Hirashima A.;
RT   "Molecular characterization of a cell wall-associated proteinase gene
RT   from Streptococcus lactis NCDO763.";
RL   Mol. Microbiol. 3:359-369(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19257 / DSM 20069 / LMG 6897 / NCDO 607 / NCIMB 8662;
RC   PLASMID=pHP003;
RX   PubMed=11473599; DOI=10.1046/j.1365-2672.2001.01390.x;
RA   Christensson C., Pillidge C.J., Ward L.J., O'Toole P.W.;
RT   "Nucleotide sequence and characterization of the cell envelope
RT   proteinase plasmid in Lactococcus lactis subsp. cremoris HP.";
RL   J. Appl. Microbiol. 91:334-343(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-295.
RC   STRAIN=Wg2; PLASMID=pWV05;
RX   PubMed=3278687;
RA   Kok J., Leenhouts K.J., Haandrikman A.J., Ledeboer A.M., Venema G.;
RT   "Nucleotide sequence of the cell wall proteinase gene of Streptococcus
RT   cremoris Wg2.";
RL   Appl. Environ. Microbiol. 54:231-238(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-299.
RC   STRAIN=Wg2; PLASMID=pWV05;
RX   PubMed=2166472;
RA   Haandrikman A.J., van Leeuwen C., Kok J., Vos P., de Vos W.M.,
RA   Venema G.;
RT   "Insertion elements on lactococcal proteinase plasmids.";
RL   Appl. Environ. Microbiol. 56:1890-1896(1990).
RN   [6]
RP   CHARACTERIZATION, SUBCELLULAR LOCATION, PALMITOYLATION, AND
RP   MUTAGENESIS OF CYS-24.
RC   STRAIN=Wg2;
RX   PubMed=1906066;
RA   Haandrikman A.J., Kok J., Venema G.;
RT   "Lactococcal proteinase maturation protein PrtM is a lipoprotein.";
RL   J. Bacteriol. 173:4517-4525(1991).
CC   -!- FUNCTION: This protein is essential for production of active forms
CC       of the serine proteinase located in or secreted from the cell
CC       envelope.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor (Probable).
CC   -!- SIMILARITY: Belongs to the PrsA family.
CC   -!- SIMILARITY: Contains 1 PpiC domain.
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DR   EMBL; M26694; AAA60395.1; -; Genomic_DNA.
DR   EMBL; X14130; CAA32349.1; -; Genomic_DNA.
DR   EMBL; AF247159; AAK27980.1; -; Genomic_DNA.
DR   EMBL; M24767; AAA17676.1; -; Unassigned_DNA.
DR   PIR; S08083; S08083.
DR   RefSeq; NP_858118.1; NC_004847.1.
DR   RefSeq; YP_006965817.1; NC_019377.1.
DR   ProteinModelPortal; P0C2B5; -.
DR   GeneID; 1113513; -.
DR   GeneID; 13919691; -.
DR   ProtClustDB; PRK04405; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01145; Foldase_PrsA; 1.
DR   InterPro; IPR023059; Foldase_PrsA.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR023058; PPIase_PpiC_CS.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom.
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   1: Evidence at protein level;
KW   Cell membrane; Isomerase; Lipoprotein; Membrane; Palmitate; Plasmid;
KW   Rotamase; Signal.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    299       Foldase protein PrsA.
FT                                /FTId=PRO_0000029305.
FT   DOMAIN      144    236       PpiC.
FT   LIPID        24     24       N-palmitoyl cysteine (Probable).
FT   LIPID        24     24       S-diacylglycerol cysteine (Probable).
FT   MUTAGEN      24     24       C->A: Leads to very low amounts of
FT                                secreted foldase; it is degraded by PrtP.
FT   CONFLICT     46     46       L -> F (in Ref. 2 and 3).
FT   CONFLICT     83     83       N -> Y (in Ref. 4; AAA17676).
FT   CONFLICT    169    169       A -> S (in Ref. 3; AAK27980).
FT   CONFLICT    249    249       A -> V (in Ref. 3; AAK27980).
FT   CONFLICT    267    267       R -> P (in Ref. 4; AAA17676).
SQ   SEQUENCE   299 AA;  33133 MW;  3A7D355DE330ED5B CRC64;
     MKKKMRLKVL LASTATALLL LSGCQSNQTD QTVATYSGGK VTESSLYKEL 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
//
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