ID PRSA1_LACPL Reviewed; 298 AA.
AC Q88X05; F9UNJ3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 01-MAY-2013, entry version 62.
DE RecName: Full=Foldase protein PrsA 1;
DE EC=5.2.1.8;
DE Flags: Precursor;
GN Name=prsA1; Synonyms=prtM1; OrderedLocusNames=lp_1452;
OS Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D.,
RA Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M.,
RA Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A.,
RA Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B.,
RA De Vos W.M., Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
CC -!- FUNCTION: Plays a major role in protein secretion by helping the
CC post-translocational extracellular folding of several secreted
CC proteins (By similarity).
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor (Potential).
CC -!- SIMILARITY: Belongs to the PrsA family.
CC -!- SIMILARITY: Contains 1 PpiC domain.
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DR EMBL; AL935263; CCC78782.1; -; Genomic_DNA.
DR RefSeq; YP_004889296.1; NC_004567.2.
DR ProteinModelPortal; Q88X05; -.
DR STRING; 220668.lp_1452; -.
DR EnsemblBacteria; CCC78782; CCC78782; lp_1452.
DR GeneID; 1062391; -.
DR KEGG; lpl:lp_1452; -.
DR PATRIC; 22249145; VBILacPla27411_1215.
DR eggNOG; COG0760; -.
DR HOGENOM; HOG000014031; -.
DR KO; K07533; -.
DR OMA; YSSHISD; -.
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:HAMAP.
DR GO; GO:0006457; P:protein folding; IEA:HAMAP.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
DR HAMAP; MF_01145; Foldase_PrsA; 1; -.
DR InterPro; IPR023059; Foldase_PrsA.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR027304; Trigger_fact/SurA_dom.
DR SUPFAM; SSF109998; Trigger_fac_C_bac; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; FALSE_NEG.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Complete proteome; Isomerase; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Rotamase; Signal.
FT SIGNAL 1 19 Potential.
FT CHAIN 20 298 Foldase protein PrsA 1.
FT /FTId=PRO_0000029307.
FT DOMAIN 136 232 PpiC.
FT LIPID 20 20 N-palmitoyl cysteine (Potential).
FT LIPID 20 20 S-diacylglycerol cysteine (Potential).
SQ SEQUENCE 298 AA; 32619 MW; 342E76C1B8997326 CRC64;
MKKWLIALAG VLLTFTLAGC GSKTVASTSG GKITESQYYS SMKGTSSGKQ VLQQMILNKV
LEKDYGSKVS TKQVTKQYNT YKSQYGSSFS TVLSQNGLTT KTFKEQLRSN LLLKEAVKDK
VKITDKALKK QWKSYEPKVT VQHILVAKSA TADKVLDALK KDSSQANFTK LAKKYSTDTT
TKNDGGKLSA FDNTNTSYSS KFLTAAFKLK NGEYTTSAVK TSNGYEIIRM IKNPGKGKMS
DHTADLKKQI WDNDMSDSTV LQNVVSKVLK GGNVSIKDND LKDILSSYLS TSSSSSSN
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