ID   TORD_SHEAM              Reviewed;         235 AA.
AC   A1S487;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-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}; OrderedLocusNames=Sama_0986;
OS   Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=326297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1098 / SB2B;
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   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella amazonensis SB2B.";
RL   Submitted (DEC-2006) 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; CP000507; ABL99193.1; -; Genomic_DNA.
DR   RefSeq; WP_011759102.1; NC_008700.1.
DR   AlphaFoldDB; A1S487; -.
DR   SMR; A1S487; -.
DR   STRING; 326297.Sama_0986; -.
DR   EnsemblBacteria; ABL99193; ABL99193; Sama_0986.
DR   KEGG; saz:Sama_0986; -.
DR   eggNOG; COG3381; Bacteria.
DR   HOGENOM; CLU_077650_4_0_6; -.
DR   OrthoDB; 1995553at2; -.
DR   Proteomes; UP000009175; Chromosome.
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; Reference proteome.
FT   CHAIN           1..235
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_0000414900"
SQ   SEQUENCE   235 AA;  25561 MW;  A0309C4E1C257CE4 CRC64;
     MNKMSHSEEF AAGEMNAIRA SVWQLLSSLY AKELSRERIC ELAGAELWQA FAAQVELQAS
     ASQIQAALAH AAKYDASQGG DDARLELAAD FCSAFLQNAE HCAAPYASLY LGDAGKTERN
     ETASYDTESQ DKAARSLYGE KHQLMSDYLR SAGLGLDADF REPSDHLAVI LGLMAHLCTS
     ATEESQRAFL ESAILSWLPE FNARLGKLKL ESPLYGALGD FTLAWARLDT ELLGG