ID   TORD_FERBD              Reviewed;         216 AA.
AC   E1SVR5;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=Fbal_2193;
OS   Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Ferrimonadaceae; Ferrimonas.
OX   NCBI_TaxID=550540;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9799 / CCM 4581 / KCTC 23876 / PAT;
RX   PubMed=21304747; DOI=10.4056/sigs.1161239;
RA   Nolan M., Sikorski J., Davenport K., Lucas S., Del Rio T.G., Tice H.,
RA   Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Tapia R., Brettin T., Detter J.C., Han C.,
RA   Yasawong M., Rohde M., Tindall B.J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Ferrimonas balearica type strain (PAT).";
RL   Stand. Genomic Sci. 3:174-182(2010).
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; CP002209; ADN76396.1; -; Genomic_DNA.
DR   RefSeq; WP_013345702.1; NC_014541.1.
DR   AlphaFoldDB; E1SVR5; -.
DR   SMR; E1SVR5; -.
DR   STRING; 550540.Fbal_2193; -.
DR   EnsemblBacteria; ADN76396; ADN76396; Fbal_2193.
DR   GeneID; 67182392; -.
DR   KEGG; fbl:Fbal_2193; -.
DR   eggNOG; COG3381; Bacteria.
DR   HOGENOM; CLU_077650_4_0_6; -.
DR   OMA; PYASMYI; -.
DR   OrthoDB; 1995553at2; -.
DR   Proteomes; UP000006683; 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; Reference proteome.
FT   CHAIN           1..216
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_0000414894"
SQ   SEQUENCE   216 AA;  23982 MW;  842A59246487D262 CRC64;
     MDEQEIREEV ALAERRATLY WWFASMLCRE LDSDQLNTLC SESGRVLLDA LAEEPSLAPG
     CQKLRRALAG VQVLATPQLE LAADYATAFL GDHLGSAPPY ASVYVEPGGM MFQHPHQQMV
     QWLQQWQLAV SFDGNEPADH FAIMLDLMGN LVLKGVDSPE AQSAQSALLA EMLPPMRRWV
     TQCQRQPGFY AALAELLLAF VSLDQTLIEG EFSLAQ