ID   TORD_VIBVU              Reviewed;         215 AA.
AC   Q8DAQ4;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=VV1_2139;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SEQUENCE REVISION.
RC   STRAIN=CMCP6;
RX   PubMed=21245845; DOI=10.1038/msb.2010.115;
RA   Kim H.U., Kim S.Y., Jeong H., Kim T.Y., Kim J.J., Choy H.E., Yi K.Y.,
RA   Rhee J.H., Lee S.Y.;
RT   "Integrative genome-scale metabolic analysis of Vibrio vulnificus for drug
RT   targeting and discovery.";
RL   Mol. Syst. Biol. 7:460-460(2011).
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; AE016795; AAO10524.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q8DAQ4; -.
DR   SMR; Q8DAQ4; -.
DR   EnsemblBacteria; AAO10524; AAO10524; VV1_2139.
DR   KEGG; vvu:VV1_2139; -.
DR   HOGENOM; CLU_077650_4_0_6; -.
DR   Proteomes; UP000002275; 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.
FT   CHAIN           1..215
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_0000211647"
SQ   SEQUENCE   215 AA;  24760 MW;  C94975D085E65858 CRC64;
     MMQEIKAFNE KRAEIYWWLS SLFAKELTQE ELDKYQSMEI RAFLTGLAEN DALRPSVNAF
     VDALNRLVDR QDAQLELAAD FCDLFLKTAK HGALPYASIY LTKDGLLNGE PAQKMDAWLK
     KHGVQVNQQL NEPADHLAIM LDFLGNLIIR SNEFEQDRHM EEAFIEQNAF IQEMLLSWLP
     SFSQRAAEYD EFGFYNSAIK LLVAFCMLDS DYLVG