PRSA_LACLC
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 25-MAY-2022, entry version 73.
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; DOI=10.1128/jb.171.5.2789-2794.1989;
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 from
RT Streptococcus lactis NCDO763.";
RL Mol. Microbiol. 3:359-369(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19257 / DSM 20069 / BCRC 12586 / JCM 16167 / LMG 6897 / NBRC
RC 100676 / NCDO 607 / NCIMB 8662 / HP; 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 proteinase
RT 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; DOI=10.1128/aem.54.1.231-238.1988;
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; 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).
RN [6]
RP CHARACTERIZATION, SUBCELLULAR LOCATION, DIACYLGLYCEROL AT CYS-24,
RP PALMITOYLATION AT CYS-24, AND MUTAGENESIS OF CYS-24.
RC STRAIN=Wg2;
RX PubMed=1906066; DOI=10.1128/jb.173.14.4517-4525.1991;
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 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|PubMed:1906066};
CC Lipid-anchor {ECO:0000305|PubMed:1906066}.
CC -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000305}.
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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; WP_011114710.1; NZ_VERZ01000069.1.
DR RefSeq; WP_015083008.1; NZ_WJUX01000082.1.
DR RefSeq; YP_006965817.1; NC_019377.1.
DR AlphaFoldDB; P0C2B5; -.
DR SMR; P0C2B5; -.
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 1: Evidence at protein level;
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_0000029305"
FT DOMAIN 144..236
FT /note="PpiC"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:1906066"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:1906066"
FT MUTAGEN 24
FT /note="C->A: Leads to very low amounts of secreted foldase;
FT it is degraded by PrtP."
FT /evidence="ECO:0000269|PubMed:1906066"
FT CONFLICT 46
FT /note="L -> F (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="N -> Y (in Ref. 4; AAA17676)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="A -> S (in Ref. 3; AAK27980)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="A -> V (in Ref. 3; AAK27980)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="R -> P (in Ref. 4; AAA17676)"
FT /evidence="ECO:0000305"
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
