ID   A0A3A6QT17_9VIBR        Unreviewed;       215 AA.
AC   A0A3A6QT17;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Chaperone protein TorD {ECO:0000256|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000256|HAMAP-Rule:MF_01150,
GN   ECO:0000313|EMBL:RJX73756.1};
GN   ORFNames=DZ860_05905 {ECO:0000313|EMBL:RJX73756.1};
OS   Vibrio sinensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2302434 {ECO:0000313|EMBL:RJX73756.1, ECO:0000313|Proteomes:UP000273252};
RN   [1] {ECO:0000313|EMBL:RJX73756.1, ECO:0000313|Proteomes:UP000273252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BEI233 {ECO:0000313|EMBL:RJX73756.1,
RC   ECO:0000313|Proteomes:UP000273252};
RA   Li Y.;
RT   "Vibrio isolated from the Eastern China Marginal Seas.";
RL   Submitted (AUG-2018) 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:0000256|HAMAP-Rule:MF_01150}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01150}.
CC   -!- SIMILARITY: Belongs to the TorD/DmsD family. TorD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01150}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RJX73756.1}.
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DR   EMBL; QVMU01000003; RJX73756.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A6QT17; -.
DR   OrthoDB; 7849731at2; -.
DR   Proteomes; UP000273252; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.1820; -; 1.
DR   Gene3D; 1.20.1280.20; HscB, C-terminal domain; 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   PANTHER; PTHR34227:SF11; CHAPERONE PROTEIN TORD; 1.
DR   PANTHER; PTHR34227; CHAPERONE PROTEIN YCDY; 1.
DR   Pfam; PF02613; Nitrate_red_del; 1.
DR   SUPFAM; SSF89155; TorD-like; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01150};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01150}.
SQ   SEQUENCE   215 AA;  24570 MW;  FD74C099A0895A4B CRC64;
     MQEIKAFNEK RAEIYWWFSS LFAKELTEAE LEQYHSPEIR TFLTGLGENP TLNVAATRVN
     DALNRLLDRE DAQLELSADF CDLFLKSDKD SALPYASMYI GETGLLDDKP ARDIEAVMAQ
     YNVAVQKDLN EPADHLAIEL DLLGNIIIRS NELEQERHLD EALADQHTFI EQHLLSWVPK
     FSTKCQSFDE FGFYSAVVAL LVSFLELDRD YLAGE
//