DMSB_HALSA
ID DMSB_HALSA Reviewed; 262 AA.
AC Q9HR73;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Putative dimethyl sulfoxide reductase iron-sulfur subunit B;
DE Short=DMSO reductase subunit B;
GN Name=dmsB; Synonyms=hmoA; OrderedLocusNames=VNG_0830G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2]
RP PUTATIVE FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=15716436; DOI=10.1128/jb.187.5.1659-1667.2005;
RA Muller J.A., DasSarma S.;
RT "Genomic analysis of anaerobic respiration in the archaeon Halobacterium
RT sp. strain NRC-1: dimethyl sulfoxide and trimethylamine N-oxide as terminal
RT electron acceptors.";
RL J. Bacteriol. 187:1659-1667(2005).
CC -!- FUNCTION: Dimethyl sulfoxide (DMSO) reductase catalyzes the reduction
CC of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS) during anaerobic
CC respiration; it can also use trimethylamine N-oxide (TMAO) as terminal
CC electron acceptor. Subunit B is proposed to be involved in electron
CC transfer.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250};
CC -!- SUBUNIT: Probable multiprotein complex that likely consists of DmsA,
CC DmsB and DmsC.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By anaerobic conditions. Its expression is under the control
CC of DmsR. {ECO:0000269|PubMed:15716436}.
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DR EMBL; AE004437; AAG19285.1; -; Genomic_DNA.
DR PIR; A84240; A84240.
DR RefSeq; WP_010902581.1; NC_002607.1.
DR AlphaFoldDB; Q9HR73; -.
DR SMR; Q9HR73; -.
DR STRING; 64091.VNG_0830G; -.
DR TCDB; 5.A.3.3.3; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR PaxDb; Q9HR73; -.
DR EnsemblBacteria; AAG19285; AAG19285; VNG_0830G.
DR GeneID; 5953698; -.
DR GeneID; 62884252; -.
DR KEGG; hal:VNG_0830G; -.
DR PATRIC; fig|64091.14.peg.638; -.
DR HOGENOM; CLU_043374_1_2_2; -.
DR InParanoid; Q9HR73; -.
DR OMA; CENTPCL; -.
DR OrthoDB; 105930at2157; -.
DR PhylomeDB; Q9HR73; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR Pfam; PF13247; Fer4_11; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Reference proteome; Repeat; Transport.
FT CHAIN 1..262
FT /note="Putative dimethyl sulfoxide reductase iron-sulfur
FT subunit B"
FT /id="PRO_0000428977"
FT DOMAIN 4..34
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 62..93
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 94..123
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT REGION 209..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 13
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 262 AA; 28824 MW; B0F6C9C959FBC1BC CRC64;
MTNYGLVIDQ ERCIGCQSCS LTCKQENNVP MGQFWNRVLT QGGDHVDTPS GDYPEGGDGG
TLEMTYQPTA CQHCENAPCV KVCPVNATYT RDDGIVEIDY DKCMGCRYCM AACPYNARVF
NWDEPEHRPE DGTGDVAERP QGVVEKCTFC SHRVEDGLDP ACVVNCPADA RIFGDLDDDD
STVSKYIAEY DTHQLLDEKG TDPSTYYING EMSPGRPWKS KKLESELDDD EAAKAARRRS
GSVENGYDVT PHVPAETAGG DD
