ID   TORD_HAES1              Reviewed;         193 AA.
AC   Q0I508;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=HS_1674;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(2007).
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; CP000436; ABI25942.1; -; Genomic_DNA.
DR   RefSeq; WP_011609819.1; NC_008309.1.
DR   AlphaFoldDB; Q0I508; -.
DR   SMR; Q0I508; -.
DR   STRING; 205914.HS_1674; -.
DR   EnsemblBacteria; ABI25942; ABI25942; HS_1674.
DR   KEGG; hso:HS_1674; -.
DR   eggNOG; COG3381; Bacteria.
DR   HOGENOM; CLU_077650_4_0_6; -.
DR   OMA; CHFTFLE; -.
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..193
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_0000414895"
SQ   SEQUENCE   193 AA;  22533 MW;  86183E415E1927BB CRC64;
     MITLNTEEKI FIYSWLKNIL SHELTEQQLQ QYQQGVFTPL FDFLSEQDLA EQINTVRNSL
     MQLSNLPLAH LELAADFAQL FLLNGENSAL PYASAYLSEK ELNQHIAFID HLLLKYQLKF
     DHSLREPSDH LAVYLELLIT LEKSGQKEKS FNFIQHYLLA WLIPFNKKVQ KIKTETSFYQ
     AITEILITLL NKT