ID   TORD_ACTPJ              Reviewed;         199 AA.
AC   B0BSW9;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=APJL_1833;
OS   Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=434271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL03;
RX   PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA   Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA   Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA   Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA   Zhao G.-P., Chen H.;
RT   "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT   serotype 3 prevalent in China.";
RL   PLoS ONE 3:E1450-E1450(2008).
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; CP000687; ABY70383.1; -; Genomic_DNA.
DR   RefSeq; WP_012263391.1; NC_010278.1.
DR   AlphaFoldDB; B0BSW9; -.
DR   SMR; B0BSW9; -.
DR   EnsemblBacteria; ABY70383; ABY70383; APJL_1833.
DR   KEGG; apj:APJL_1833; -.
DR   HOGENOM; CLU_077650_4_0_6; -.
DR   OMA; PYASMYI; -.
DR   OrthoDB; 1995553at2; -.
DR   Proteomes; UP000008547; 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..199
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_0000414887"
SQ   SEQUENCE   199 AA;  23044 MW;  0C20B884EB519CE4 CRC64;
     MAHSQLLSSE ERLFCYRWFH SLLAKELSEP QLQALQAGQF ASFFAFLAEL GFQPQVTDLQ
     NELAKLTAYD SPRLELAADF AQCFLLEGKL SALPYASYYL DERDLSENLA VMDQWLTKFQ
     LKINRLHNEP SDHLCIYLEV LIKLIETEQP VQVQQQFIRQ QLLGWLPQWA EKTAQIHSST
     AFYQIISNLL LGFLQQDIT