TORD_COLP3
ID TORD_COLP3 Reviewed; 236 AA.
AC Q484F1;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=CPS_1834;
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H / ATCC BAA-681;
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ24720.1; -; Genomic_DNA.
DR RefSeq; WP_011042658.1; NC_003910.7.
DR AlphaFoldDB; Q484F1; -.
DR SMR; Q484F1; -.
DR STRING; 167879.CPS_1834; -.
DR EnsemblBacteria; AAZ24720; AAZ24720; CPS_1834.
DR KEGG; cps:CPS_1834; -.
DR HOGENOM; CLU_077650_4_0_6; -.
DR OMA; PYASMYI; -.
DR OrthoDB; 1995553at2; -.
DR Proteomes; UP000000547; 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..236
FT /note="Chaperone protein TorD"
FT /id="PRO_0000414893"
SQ SEQUENCE 236 AA; 26212 MW; 8E54E751CD7F8CFF CRC64;
MSHVSQETAQ EISEEREARA IVYNFLSSLF AKEVTSDLVA QLTSAQGQSF LKSLALDPSL
SASVNEINTK LVKLNSKESL LELAADFCGL FLVDGRTSVS PYAGQYLSVE QGGEPSEKLS
NAAINESGSK SKKNKAQLFG ELHQQMTEFL TDNKLQIHSD FPEPGDHIAV ILAYIAHLCV
TSGSEQQLNF INSYLMTWLS DFTQQVNKHD HGQFYCFVAD LTFEWLKVDT EFLLSD