位置:首页 > 蛋白库 > PRSA_EXIS2
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024