(data stored in ACNUC7421 zone)

SWISSPROT: C5BCT4_EDWI9

ID   C5BCT4_EDWI9            Unreviewed;       212 AA.
AC   C5BCT4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   RecName: Full=Chaperone protein TorD {ECO:0000256|HAMAP-Rule:MF_01150, ECO:0000256|SAAS:SAAS00014573};
GN   Name=torD {ECO:0000256|HAMAP-Rule:MF_01150};
GN   OrderedLocusNames=NT01EI_0298 {ECO:0000313|EMBL:ACR67540.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67540.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biogenesis of TorA. Acts on TorA before
CC       the insertion of the molybdenum cofactor and, as a result,
CC       probably favors a conformation of the apoenzyme that is competent
CC       for acquiring the cofactor. {ECO:0000256|HAMAP-Rule:MF_01150,
CC       ECO:0000256|SAAS:SAAS00014569}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01150,
CC       ECO:0000256|SAAS:SAAS00014570}.
CC   -!- SIMILARITY: Belongs to the TorD/DmsD family. TorD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01150, ECO:0000256|SAAS:SAAS00633853}.
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DR   EMBL; CP001600; ACR67540.1; -; Genomic_DNA.
DR   RefSeq; WP_015869749.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0298; -.
DR   EnsemblBacteria; ACR67540; ACR67540; NT01EI_0298.
DR   GeneID; 7960078; -.
DR   KEGG; eic:NT01EI_0298; -.
DR   PATRIC; fig|634503.3.peg.269; -.
DR   eggNOG; ENOG4108SBI; Bacteria.
DR   eggNOG; COG3381; LUCA.
DR   HOGENOM; HOG000281891; -.
DR   KO; K03533; -.
DR   OMA; AFNEQRA; -.
DR   OrthoDB; POG091H05EX; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.3480.10; -; 1.
DR   HAMAP; MF_01150; TorD; 1.
DR   InterPro; IPR023069; Chaperone_TorD.
DR   InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
DR   Pfam; PF02613; Nitrate_red_del; 1.
DR   SUPFAM; SSF89155; SSF89155; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BCT4.
DR   SWISS-2DPAGE; C5BCT4.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01150,
KW   ECO:0000256|SAAS:SAAS00014572};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01150,
KW   ECO:0000256|SAAS:SAAS00014571};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
SQ   SEQUENCE   212 AA;  23732 MW;  044F1CD852884C25 CRC64;
     MSAASPLTAQ HYACLYAWLA GLFAHETDDA QLARLRSPDT QAWFALLRQL APLRPALQCL
     QEALVALEAR PDARLELAAD FAGLFLLSQK RAALPYASCY QGETPRFRQA PCDEVQSLLQ
     RAGMQLNADF HEPEDHLSIF LELLSHLSFA SAEQPGQEDV LVPLRQRTLA LLLEWLPEFN
     ARCLRYDTFG FYAALSQLLL ALVRLDANHR AA
//

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