ID   TORD_VIBC3              Reviewed;         220 AA.
AC   A5F7G9; C3M1B8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   OrderedLocusNames=VC0395_A1323, VC395_1837;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ20810.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP09834.1; -; Genomic_DNA.
DR   RefSeq; WP_000983169.1; NZ_JAACZH010000016.1.
DR   AlphaFoldDB; A5F7G9; -.
DR   SMR; A5F7G9; -.
DR   STRING; 345073.VC395_1837; -.
DR   EnsemblBacteria; ABQ20810; ABQ20810; VC0395_A1323.
DR   KEGG; vco:VC0395_A1323; -.
DR   KEGG; vcr:VC395_1837; -.
DR   PATRIC; fig|345073.21.peg.1780; -.
DR   eggNOG; COG3381; Bacteria.
DR   HOGENOM; CLU_077650_4_0_6; -.
DR   OMA; PYASMYI; -.
DR   Proteomes; UP000000249; Chromosome 2.
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..220
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_1000073062"
SQ   SEQUENCE   220 AA;  25099 MW;  EBB29DE457E69F83 CRC64;
     MMQELKILNE KRAEIYWWLS SLFFKELSEQ DIARYHSAEV RTFLSGLADE QSLSREVKHL
     VEALNRLQDR QDAQLELAAD FCDLFLKSDR DSALPYASVY TDQGLLNGKP AQQMRELLSA
     HGVKVEQNLN EPEDHLAIQL DFLAHLAISA NQIEHSAQLS LALQAQSDFI SQHLLTWLPA
     FAERCTQFDA FGLYSAAARL ALAFIQQDKH CLDELIQETH