ID   TORD_AGGAN              Reviewed;         207 AA.
AC   C6AN26;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=NT05HA_0851;
OS   Aggregatibacter aphrophilus (strain NJ8700) (Haemophilus aphrophilus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=634176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJ8700;
RX   PubMed=19447908; DOI=10.1128/jb.00447-09;
RA   Di Bonaventura M.P., DeSalle R., Pop M., Nagarajan N., Figurski D.H.,
RA   Fine D.H., Kaplan J.B., Planet P.J.;
RT   "Complete genome sequence of Aggregatibacter (Haemophilus) aphrophilus
RT   NJ8700.";
RL   J. Bacteriol. 191:4693-4694(2009).
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; CP001607; ACS97236.1; -; Genomic_DNA.
DR   RefSeq; WP_012771506.1; NZ_CP009230.1.
DR   AlphaFoldDB; C6AN26; -.
DR   SMR; C6AN26; -.
DR   KEGG; aap:NT05HA_0851; -.
DR   HOGENOM; CLU_077650_4_0_6; -.
DR   OMA; PYASMYI; -.
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..207
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_0000414892"
SQ   SEQUENCE   207 AA;  23958 MW;  A4D407BD850CA096 CRC64;
     MLHHNQMVLM GLLNMLKISI QERQFVYSWI CSLLSKELTQ DQLAHYQRGD FDSLFAFLKE
     LGFTEQTEQL IATLRPMEFQ QLELAADFAH TFLLEGNISA IPYMSAYLQG EELGVALNLV
     DQWMTHYQLG VNREQNEPSD HVSVLLAILI RLIGEQPFHV QQDFAQKALL NWLPEFVRKA
     NNTSCETKFY AMLCNLFLAF MTEDFAV