ID   TORD_SERP5              Reviewed;         212 AA.
AC   A8GJM1;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=Spro_4217;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) 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; CP000826; ABV43311.1; -; Genomic_DNA.
DR   RefSeq; WP_012146916.1; NC_009832.1.
DR   AlphaFoldDB; A8GJM1; -.
DR   SMR; A8GJM1; -.
DR   STRING; 399741.Spro_4217; -.
DR   EnsemblBacteria; ABV43311; ABV43311; Spro_4217.
DR   KEGG; spe:Spro_4217; -.
DR   eggNOG; COG3381; Bacteria.
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:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01150; TorD; 1.
DR   InterPro; IPR023069; Chaperone_TorD.
DR   InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
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..212
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_0000414899"
SQ   SEQUENCE   212 AA;  24437 MW;  2F8572E8CC4A80AB CRC64;
     MPLLNEVARQ RAIIYRWFSQ LLFQELSDEG LLRLRDKENL ALLNALKLIP ELSLLVTHFQ
     RRLRAMLKRE ECRLELAADF ASLFLLPAPS GVSPYAGHYP HTNSPEERQA LRQKLVEHRL
     APQNNEAVDH IAIQLALMTA LIEEGVEREQ QDLFLNRHLL SWLPLCTKRC YQRDRFGFYA
     AAMGLLTGFV QQDSEWLIAC RLATHPARPG QS