ID   TORD_PSYWF              Reviewed;         221 AA.
AC   A5WBY3;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   OrderedLocusNames=PsycPRwf_0215;
OS   Psychrobacter sp. (strain PRwf-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=349106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRwf-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL   Submitted (MAY-2007) 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; CP000713; ABQ93174.1; -; Genomic_DNA.
DR   RefSeq; WP_011959508.1; NC_009524.1.
DR   AlphaFoldDB; A5WBY3; -.
DR   SMR; A5WBY3; -.
DR   STRING; 349106.PsycPRwf_0215; -.
DR   EnsemblBacteria; ABQ93174; ABQ93174; PsycPRwf_0215.
DR   KEGG; prw:PsycPRwf_0215; -.
DR   eggNOG; COG3381; Bacteria.
DR   HOGENOM; CLU_077650_4_0_6; -.
DR   OMA; PYASMYI; -.
DR   OrthoDB; 1995553at2; -.
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..221
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_0000414897"
SQ   SEQUENCE   221 AA;  25280 MW;  C313FEF029ED2D7D CRC64;
     MNNSQQWQAA NTARAALYRW FAELFARELT KTNLTQLQAQ YPSLHAAFSD LNLEPQSAAL
     QTALENLQVI PAPDRALELA ADFAHLFLLS GHQSAPPYAS YYLESDQMLY GKPAQQMSEF
     LASHKLDLHP EFREPKDHLS IYLQVMSLWI KSSVDEQANL IEMAVQQQHF LEDALLSWLP
     KFAARCQHIR VKTQVYPAII DLLLHFVQED RQALEDMAEA E