PRSA1_LISIN
ID PRSA1_LISIN Reviewed; 294 AA.
AC Q92BR2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Foldase protein PrsA 1;
DE EC=5.2.1.8;
DE Flags: Precursor;
GN Name=prsA1; OrderedLocusNames=lin1482;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL596168; CAC96713.1; -; Genomic_DNA.
DR PIR; AI1617; AI1617.
DR RefSeq; WP_010991555.1; NC_003212.1.
DR AlphaFoldDB; Q92BR2; -.
DR SMR; Q92BR2; -.
DR STRING; 272626.lin1482; -.
DR EnsemblBacteria; CAC96713; CAC96713; CAC96713.
DR KEGG; lin:lin1482; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_6_1_9; -.
DR OMA; SEFGPGM; -.
DR OrthoDB; 1838755at2; -.
DR Proteomes; UP000002513; 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 GO; GO:0015031; P:protein transport; IEA:InterPro.
DR Gene3D; 1.10.3120.10; -; 1.
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; IPR037041; Trigger_fac_C_sf.
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; Rotamase;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..294
FT /note="Foldase protein PrsA 1"
FT /id="PRO_0000029309"
FT DOMAIN 135..226
FT /note="PpiC"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 294 AA; 32552 MW; 0E3F4653EB63D009 CRC64;
MTKLKKVMIS LVAATLLLLA GCGSSAVVKT DAGNVTQDEL YEAMKTTYGN EVVQQLTFKK
ILEDKYTVTE KEVNAEYKKY EEQYGDSFES TLSSNNLTKT SFKENLEYNL LVQKATEANM
NVSESKLKTY YKTWEPNITV RHILVDDEAT AKEIQTKLKN GEKFADLAKE YSTDTATSTN
GGLLDPFGPG EMDETFEKAA YALKNKDDVS GIVKSTYGYH LIQLVKKTEK GTYAKEKANV
KAAYIKSQLT SENMTAALKK ELKAANIDIK DSDLKDAFAD YTSTSSSSST STSN