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TORD_VIBA3
ID   TORD_VIBA3              Reviewed;         215 AA.
AC   B7VMG5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=VS_1089;
OS   Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=575788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LGP32;
RA   Mazel D., Le Roux F.;
RT   "Vibrio splendidus str. LGP32 complete genome.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biogenesis of TorA. Acts on TorA before the
CC       insertion of the molybdenum cofactor and, as a result, probably favors
CC       a conformation of the apoenzyme that is competent for acquiring the
CC       cofactor. {ECO:0000255|HAMAP-Rule:MF_01150}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01150}.
CC   -!- SIMILARITY: Belongs to the TorD/DmsD family. TorD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01150}.
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DR   EMBL; FM954972; CAV18204.1; -; Genomic_DNA.
DR   RefSeq; WP_012603615.1; NC_011753.2.
DR   AlphaFoldDB; B7VMG5; -.
DR   SMR; B7VMG5; -.
DR   STRING; 575788.VS_1089; -.
DR   EnsemblBacteria; CAV18204; CAV18204; VS_1089.
DR   KEGG; vsp:VS_1089; -.
DR   eggNOG; COG3381; Bacteria.
DR   HOGENOM; CLU_077650_4_0_6; -.
DR   OMA; PYASMYI; -.
DR   OrthoDB; 1995553at2; -.
DR   Proteomes; UP000009100; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.1280.20; -; 1.
DR   HAMAP; MF_01150; TorD; 1.
DR   InterPro; IPR023069; Chaperone_TorD.
DR   InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
DR   InterPro; IPR036386; HscB_C_sf.
DR   InterPro; IPR036411; TorD-like_sf.
DR   Pfam; PF02613; Nitrate_red_del; 1.
DR   SUPFAM; SSF89155; SSF89155; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Reference proteome.
FT   CHAIN           1..215
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_1000164173"
SQ   SEQUENCE   215 AA;  24654 MW;  008CEAAB472E11B0 CRC64;
     MKDTKAFNEQ RAEIYWWLSS LFAKELTQEE LDHYHSVEIR SFLTGLGENE TLKPAIDSLV
     DALNRLQTRE DAQLELSADF CDLFLKTDKH GALPYASMYI GQTGLLNDKP AKDMEEIMAK
     HNLVVNQDLK EPADHIAIEL DFLGNLIIRS NETELEEELE KSFAVQQQFI EQQLLTWVPK
     FNVKCHDIDT FGFYASVSSL LLAFCKLDTQ YLAGE
 
 
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