PRSA_EXIS2
ID PRSA_EXIS2 Reviewed; 304 AA.
AC B1YK87;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Foldase protein PrsA {ECO:0000255|HAMAP-Rule:MF_01145};
DE EC=5.2.1.8 {ECO:0000255|HAMAP-Rule:MF_01145};
DE Flags: Precursor;
GN Name=prsA {ECO:0000255|HAMAP-Rule:MF_01145}; OrderedLocusNames=Exig_0687;
OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS 255-15).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a major role in protein secretion by helping the post-
CC translocational extracellular folding of several secreted proteins.
CC {ECO:0000255|HAMAP-Rule:MF_01145}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01145};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01145};
CC Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01145}.
CC -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000255|HAMAP-
CC Rule:MF_01145}.
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DR EMBL; CP001022; ACB60168.1; -; Genomic_DNA.
DR RefSeq; WP_012369592.1; NC_010556.1.
DR AlphaFoldDB; B1YK87; -.
DR SMR; B1YK87; -.
DR STRING; 262543.Exig_0687; -.
DR EnsemblBacteria; ACB60168; ACB60168; Exig_0687.
DR KEGG; esi:Exig_0687; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_6_1_9; -.
DR OMA; VESRNEP; -.
DR OrthoDB; 1838755at2; -.
DR Proteomes; UP000001681; 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..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT CHAIN 20..304
FT /note="Foldase protein PrsA"
FT /id="PRO_1000213648"
FT DOMAIN 140..231
FT /note="PpiC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT REGION 285..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
SQ SEQUENCE 304 AA; 34500 MW; 4186DE12C6B8A973 CRC64;
MKKKLLSVAA VASVFTLAAC GSNDEAVINY KGGEVNKADV QDEAYQKAGA QIAFQQTMNK
LLEKEYGKKV TDKEVEAEVK KTKDQFPDKE QFNTTLQTAG IKNEKEFEKV LRTQMLLKEA
KSAKSKVTDK EIEDRFNQEK VEVKASHILV EKESEAKAIK KQLDEGGDFA KIAKAKSTDT
GSATKGGDLG YFTKGKMVEE FENYAFKDGV EGKISDPIKT QFGYHIIKVT DRKEKKDFTL
EKESDRIKKA LAEEKSAQVN PNDIYRSLMK KYDVKVENKD FKDAFDLDKQ EQQQMQQQMQ
QQQQ