TORD_SHEPA
ID TORD_SHEPA Reviewed; 221 AA.
AC A8H7X2;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=Spea_3344;
OS Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=398579;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700345 / ANG-SQ1;
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., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT "Complete sequence of Shewanella pealeana ATCC 700345.";
RL Submitted (OCT-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; CP000851; ABV88659.1; -; Genomic_DNA.
DR RefSeq; WP_012156558.1; NC_009901.1.
DR AlphaFoldDB; A8H7X2; -.
DR SMR; A8H7X2; -.
DR STRING; 398579.Spea_3344; -.
DR EnsemblBacteria; ABV88659; ABV88659; Spea_3344.
DR KEGG; spl:Spea_3344; -.
DR eggNOG; COG3381; Bacteria.
DR HOGENOM; CLU_077650_4_0_6; -.
DR OMA; PYASMYI; -.
DR Proteomes; UP000002608; 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..221
FT /note="Chaperone protein TorD"
FT /id="PRO_0000414902"
SQ SEQUENCE 221 AA; 24813 MW; 0757C688C3E99B87 CRC64;
MIKDAVNTET VEVNPVDQVR STIYQLLSSL FAKEIDHKIL HDLTSEQAQQ FWAQLGSEAE
FKADVDVLVA ELAKLNTDKA LLELAADYCG LFLVGTKYSA SPYASLYLDD KPAKKGDEPL
LFGEQHQQMT QFLKQSQLQV QSEFPEPADH LAVILAYVAH LCTHSDEAEQ HSFIKANLAN
WLGNFVAKVT EVDTGNFYQA LARLTYSWVK SDAEWLESEL N