SERD_THASE
ID SERD_THASE Reviewed; 193 AA.
AC Q9S1G8;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Selenate reductase assembly chaperone protein;
GN Name=serD;
OS Thauera selenatis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=33058;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10826693; DOI=10.3109/10425170009015604;
RA Krafft T., Bowen A., Theis F., Macy J.M.;
RT "Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-
RT containing selenate reductase of Thauera selenatis.";
RL DNA Seq. 10:365-377(2000).
CC -!- FUNCTION: May function as a system-specific chaperone protein essential
CC for the assembly of an active selenate reductase SerABC.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- BIOTECHNOLOGY: Has potential use in bioremediation of waste sites
CC contaminated with selenate, such as agricultural drainage waters.
CC -!- SIMILARITY: Belongs to the type II DMSO reductase enzyme chaperone
CC family. {ECO:0000305}.
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DR EMBL; AJ007744; CAB53374.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S1G8; -.
DR SMR; Q9S1G8; -.
DR PRIDE; Q9S1G8; -.
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="Selenate reductase assembly chaperone protein"
FT /id="PRO_0000097691"
SQ SEQUENCE 193 AA; 21788 MW; 72AF51D41F7D8035 CRC64;
MNALIDNPEA LASGYLAMAQ VFSYPDAGAW SRLTERGLVD PALTHETLEA EYLAAFEMGG
GKATVSLYEG QNRPDLGRDG ILQELLRFYE FFDAQLSEDD REYPDHLVTE LEFLAWLCLQ
EHAAVRDGRD AEPFRRAARD FLDRHLAAWL PEFRRRLEAT DSAYAQYGPA LGELVEAHRS
RLGEQAPQLG ELQ