PRSA2_LISIN
ID PRSA2_LISIN Reviewed; 291 AA.
AC Q929F4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Foldase protein PrsA 2;
DE EC=5.2.1.8;
DE Flags: Precursor;
GN Name=prsA2; OrderedLocusNames=lin2322;
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; AL596171; CAC97550.1; -; Genomic_DNA.
DR PIR; AF1722; AF1722.
DR RefSeq; WP_003769842.1; NC_003212.1.
DR AlphaFoldDB; Q929F4; -.
DR SMR; Q929F4; -.
DR STRING; 272626.lin2322; -.
DR EnsemblBacteria; CAC97550; CAC97550; CAC97550.
DR GeneID; 61171940; -.
DR KEGG; lin:lin2322; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_6_1_9; -.
DR OMA; TMKGSTI; -.
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 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; Rotamase;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..291
FT /note="Foldase protein PrsA 2"
FT /id="PRO_0000029310"
FT DOMAIN 135..226
FT /note="PpiC"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 291 AA; 32360 MW; 85B0E3E5FC5A4FA1 CRC64;
MKKKLILGLV MMMALFSLAA CGGGGNVVKT DSGDVTQDEL YDAMKDKYGS EFVQQLTFEK
ILGDKYKVSD EDVDKKFKEY KSQYGDQFSA VLAQSGLTEK SFKSQLKYNL LVQKATEANA
DTSDKALKEY YKTWQPDITV SHILVADENK AKEVEQKLKD GAKFADLAKE YSTDTATKEN
GGQLAPFGSG KMDPAFEKAA YALKNKGDIS APVKTQYGYH IIQMDKPATK TTFDKDKKAV
KEAYLASQLT TENMQKTLKK EYKDANVKVE DKDLKDAFKD FDGSASKDSS K