PRSA2_LISMO
ID PRSA2_LISMO Reviewed; 293 AA.
AC Q8Y557;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Foldase protein PrsA 2;
DE EC=5.2.1.8;
DE Flags: Precursor;
GN Name=prsA2; OrderedLocusNames=lmo2219;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
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; AL591982; CAD00297.1; -; Genomic_DNA.
DR PIR; AC1352; AC1352.
DR RefSeq; NP_465743.1; NC_003210.1.
DR RefSeq; WP_010989927.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y557; -.
DR SMR; Q8Y557; -.
DR STRING; 169963.lmo2219; -.
DR PaxDb; Q8Y557; -.
DR EnsemblBacteria; CAD00297; CAD00297; CAD00297.
DR GeneID; 984626; -.
DR KEGG; lmo:lmo2219; -.
DR PATRIC; fig|169963.11.peg.2271; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_6_1_9; -.
DR OMA; TMKGSTI; -.
DR PhylomeDB; Q8Y557; -.
DR BioCyc; LMON169963:LMO2219-MON; -.
DR PHI-base; PHI:6413; -.
DR Proteomes; UP000000817; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..293
FT /note="Foldase protein PrsA 2"
FT /id="PRO_0000029314"
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 293 AA; 32698 MW; 172EDF444A8F7EFB CRC64;
MKKKLILGLV MMMALFSLAA CGGGGDVVKT DSGDVTKDEL YDAMKDKYGS EFVQQLTFEK
ILGDKYKVSD EDVDKKFNEY KSQYGDQFSA VLTQSGLTEK SFKSQLKYNL LVQKATEANT
DTSDKTLKKY YETWQPDITV SHILVADENK AKEVEQKLKD GEKFADLAKE YSTDTATKDN
GGQLAPFGPG KMDPAFEKAA YALKNKGDIS APVKTQYGYH IIQMDKPATK TTFEKDKKAV
KASYLESQLT TENMQKTLKK EYKDANVKVE DKDLKDAFKD FDGSSSSDSD SSK