CLRD_IDEDE
ID CLRD_IDEDE Reviewed; 193 AA.
AC P60001;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Chlorate reductase assembly chaperone protein;
GN Name=clrD;
OS Ideonella dechloratans.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Ideonella.
OX NCBI_TaxID=36863;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=12957948; DOI=10.1128/aem.69.9.5585-5592.2003;
RA Danielsson Thorell H., Stenklo K., Karlsson J., Nilsson T.;
RT "A gene cluster for chlorate metabolism in Ideonella dechloratans.";
RL Appl. Environ. Microbiol. 69:5585-5592(2003).
CC -!- FUNCTION: May function as a system-specific chaperone protein essential
CC for the assembly of an active chlorate reductase ClrABC.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- BIOTECHNOLOGY: Has potential use in bioremediation of waste sites
CC contaminated with chlorate, such as pulp and paper industry wastewater.
CC -!- SIMILARITY: Belongs to the type II DMSO reductase enzyme chaperone
CC family. {ECO:0000305}.
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DR EMBL; AJ566363; CAD97449.1; -; Genomic_DNA.
DR RefSeq; WP_013516313.1; NZ_VZPB01000026.1.
DR AlphaFoldDB; P60001; -.
DR SMR; P60001; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
DR InterPro; IPR017843; DMSO_Rdtase_II_chaperone.
DR InterPro; IPR036411; TorD-like_sf.
DR Pfam; PF02613; Nitrate_red_del; 1.
DR SUPFAM; SSF89155; SSF89155; 1.
DR TIGRFAMs; TIGR03482; DMSO_red_II_cha; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm.
FT CHAIN 1..193
FT /note="Chlorate reductase assembly chaperone protein"
FT /id="PRO_0000089872"
SQ SEQUENCE 193 AA; 22249 MW; 385AE072B856131C CRC64;
MNTLIDNPKA MASGYLAMAQ MFSYPDADAW RRLTENGLVD PALGRETLEA EYLGLFEMGG
GTSTMSLYEG QNRPERGRDG ILQELLRFYE FFDVHLNQDE REYPDHLVTE LEFLAWLCLQ
EHAALRDGRD AEPFQNAARD FLVRHLAAWL PDFRQRLEAT ETTYAQYGPT LGELVETHRS
RLGDQPQKSR EMQ