TORD_HISS2
ID TORD_HISS2 Reviewed; 197 AA.
AC B0UWF1;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, 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}; OrderedLocusNames=HSM_1836;
OS Histophilus somni (strain 2336) (Haemophilus somnus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=228400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2336;
RG US DOE Joint Genome Institute;
RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA Dyer D.W., Inzana T.J.;
RT "Complete sequence of Haemophilus somnus 2336.";
RL Submitted (FEB-2008) 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; CP000947; ACA31623.1; -; Genomic_DNA.
DR RefSeq; WP_012340930.1; NC_010519.1.
DR AlphaFoldDB; B0UWF1; -.
DR SMR; B0UWF1; -.
DR STRING; 228400.HSM_1836; -.
DR EnsemblBacteria; ACA31623; ACA31623; HSM_1836.
DR GeneID; 56965793; -.
DR KEGG; hsm:HSM_1836; -.
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..197
FT /note="Chaperone protein TorD"
FT /id="PRO_0000414896"
SQ SEQUENCE 197 AA; 23034 MW; 0ECAD1166EEFC008 CRC64;
MITLNTEEKI FIYSWLKNIL SHELTEQQLQ QYQQGVFTPL FDFLSEQDLA KQINTVRNSL
MQLSNLPLAH LELAADFAQL FLLNGENSAL PYASAYLSEK ELNQHIAFID HLLFKYQLKF
DHNLREPSDH LAVYLELLIT LEKSGQKEKS FNFIQHYLLA WLIPFNKKVQ KIKTETSFYQ
AITEILITLL NKNVKLS