PRSA1_LACJO
ID PRSA1_LACJO Reviewed; 298 AA.
AC P60750;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Foldase protein PrsA 1;
DE EC=5.2.1.8;
DE Flags: Precursor;
GN Name=prsA1; OrderedLocusNames=LJ_1673;
OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=257314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533;
RX PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT johnsonii NCC 533.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
CC -!- FUNCTION: Plays a major role in protein secretion by helping the post-
CC translocational extracellular folding of several secreted proteins.
CC {ECO:0000250}.
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; AE017198; AAS09446.1; -; Genomic_DNA.
DR RefSeq; WP_004897825.1; NC_005362.1.
DR AlphaFoldDB; P60750; -.
DR SMR; P60750; -.
DR STRING; 257314.LJ_1673; -.
DR EnsemblBacteria; AAS09446; AAS09446; LJ_1673.
DR GeneID; 66435837; -.
DR KEGG; ljo:LJ_1673; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_6_1_9; -.
DR OMA; TMKGSTI; -.
DR Proteomes; UP000000581; Chromosome.
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; IPR027304; Trigger_fact/SurA_dom_sf.
DR SUPFAM; SSF109998; SSF109998; 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;
KW Reference proteome; Rotamase; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..298
FT /note="Foldase protein PrsA 1"
FT /id="PRO_0000029315"
FT DOMAIN 141..234
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 298 AA; 33048 MW; B962E8B1AF0B5043 CRC64;
MNKTWKKAAT VLAFAGIALS ATACSGGKAV VTYKGGKITE SQYYDKMKES QAGQSTLASM
IVSDALESQY GKDVTQKQVD KEYNKYKKQY GSQFDSVLEQ NGMTASTFKD NLKTNLLTEA
ALKHIKKITP AQEKKAWKNY QPEVTVQHIL VSKKSTAEDV IKQLQDGGDF KKLAKKYSTD
TATKNDAGKL PAFDSTDSTL DSSFKTAAFK LKTGEITTTP VKTQYGYHVI KMIKHPAKGT
FKEHKKQIDN QIYQSMSEDQ NVMRSVIATV LKRADVSIKD KDLKNVLSQY VSSDSLSK