ID   TORD_ACTP7              Reviewed;         199 AA.
AC   B3GZ49;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=APP7_1883;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACE62535.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001091; ACE62535.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_005616167.1; NC_010939.1.
DR   AlphaFoldDB; B3GZ49; -.
DR   SMR; B3GZ49; -.
DR   EnsemblBacteria; ACE62535; ACE62535; APP7_1883.
DR   KEGG; apa:APP7_1883; -.
DR   HOGENOM; CLU_077650_4_0_6; -.
DR   BioCyc; APLE537457:APP7_RS09825-MON; -.
DR   Proteomes; UP000001226; 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_0000414888"
SQ   SEQUENCE   199 AA;  22980 MW;  FEB4F6C4ABFB9CEE CRC64;
     MAHSQLLSSE ERLFCYRWFH SLLAKELSEP QLQALQAGQF ASFFALLAEL GFQPQVTDLQ
     NELAKLTAYD SPRLELAADF AQCFLLEGKL SALPYASYYL DERDLSENLA VMDQWLTKFQ
     LKINRLHNEP SDHLCIYLEV LIKLIETEQP VQVQQQFIRQ QLLGWLPQWA EKTAQIHSST
     AFYQIISNLL LGFLQQDIA