TORD_SHEB9
ID TORD_SHEB9 Reviewed; 209 AA.
AC A9KZ67;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN Name=torD {ECO:0000255|HAMAP-Rule:MF_01150};
GN OrderedLocusNames=Sbal195_3353;
OS Shewanella baltica (strain OS195).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=399599;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS195;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS195.";
RL Submitted (NOV-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; CP000891; ABX50515.1; -; Genomic_DNA.
DR RefSeq; WP_006086921.1; NC_009997.1.
DR AlphaFoldDB; A9KZ67; -.
DR SMR; A9KZ67; -.
DR EnsemblBacteria; ABX50515; ABX50515; Sbal195_3353.
DR GeneID; 11773398; -.
DR KEGG; sbn:Sbal195_3353; -.
DR HOGENOM; CLU_077650_4_0_6; -.
DR OMA; PYASMYI; -.
DR Proteomes; UP000000770; 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.
FT CHAIN 1..209
FT /note="Chaperone protein TorD"
FT /id="PRO_1000085103"
SQ SEQUENCE 209 AA; 23486 MW; C09155441C75E5D1 CRC64;
MSQVDINHAR ALVYQLLSSL FAREVDEQRL KELTSEAAQQ FWEQLSLEAN FTQSVDKIRS
TLNGIKDDEA LLELAADYCG LFLVGTKHSA SPYASLYLSG EDEPLLFGQQ HQQMSEFLHQ
SKLQVQSHFP EPADHLAVML AYMAHLCCHS EDSVQLSFLQ TCIDSWLAKF INQLTQCDKN
GFYSAVATLT LAWVKQDIAQ LEPAEAVIS