ID   TORD_SHEMA              Reviewed;         209 AA.
AC   O87949;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150};
OS   Shewanella massilia.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=76854;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9813127; DOI=10.1006/jmbi.1998.2155;
RA   Dos Santos J.P., Iobbi-Nivol C., Couillault C., Giordano G., Mejean V.;
RT   "Molecular analysis of the trimethylamine N-oxide (TMAO) reductase
RT   respiratory system from a Shewanella species.";
RL   J. Mol. Biol. 284:421-433(1998).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=12192070; DOI=10.1110/ps.0202902;
RA   Tranier S., Mortier-Barriere I., Ilbert M., Birck C., Iobbi-Nivol C.,
RA   Mejean V., Samama J.P.;
RT   "Characterization and multiple molecular forms of TorD from Shewanella
RT   massilia, the putative chaperone of the molybdoenzyme TorA.";
RL   Protein Sci. 11:2148-2157(2002).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=12575936; DOI=10.1016/s0969-2126(03)00008-x;
RA   Tranier S., Iobbi-Nivol C., Birck C., Ilbert M., Mortier-Barriere I.,
RA   Mejean V., Samama J.-P.;
RT   "A novel protein fold and extreme domain swapping in the dimeric TorD
RT   chaperone from Shewanella massilia.";
RL   Structure 11:165-174(2003).
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.
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; AJ006085; CAA06852.1; -; Genomic_DNA.
DR   PDB; 1N1C; X-ray; 2.40 A; A/B=1-209.
DR   PDBsum; 1N1C; -.
DR   AlphaFoldDB; O87949; -.
DR   SMR; O87949; -.
DR   DrugBank; DB04447; 1,4-Dithiothreitol.
DR   EvolutionaryTrace; O87949; -.
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   1: Evidence at protein level;
KW   3D-structure; Chaperone; Cytoplasm.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..209
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_0000211642"
FT   HELIX           7..22
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   HELIX           27..34
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   HELIX           36..46
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   HELIX           52..64
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   HELIX           68..82
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   HELIX           94..97
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   HELIX           108..110
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   HELIX           111..121
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   HELIX           132..134
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   HELIX           136..149
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   HELIX           152..162
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   TURN            163..166
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   HELIX           167..177
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   HELIX           182..206
FT                   /evidence="ECO:0007829|PDB:1N1C"
FT   HELIX           207..209
FT                   /evidence="ECO:0007829|PDB:1N1C"
SQ   SEQUENCE   209 AA;  23555 MW;  DB6E4BA005E47C6D CRC64;
     MSQVDINHAR ALVYQLLSSL FAREVDEQRL KELTSEAAQQ FWEQLSLEAN FTQSVDKIRS
     TLNGIKDDEA LLELAADYCG LFLVGTKHSA SPYASLYLSG EDEPLLFGEQ HQQMSEFLHQ
     SKLQVQSHFP EPADHLAVML AYMAHLFCHS ENSVQLSFLQ TCFNSWLAKF INHLTQCNKN
     GFYSAVATLT LAWVKQDIAQ LEPAVAIIS