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Database: UniProt
Entry: Q83RZ7
LinkDB: Q83RZ7
Original site: Q83RZ7 
ID   DMSB_SHIFL              Reviewed;         205 AA.
AC   Q83RZ7;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-APR-2018, entry version 93.
DE   RecName: Full=Anaerobic dimethyl sulfoxide reductase chain B;
DE   AltName: Full=DMSO reductase iron-sulfur subunit;
GN   Name=dmsB; OrderedLocusNames=SF0854, S0895;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Electron transfer subunit of the terminal reductase
CC       during anaerobic growth on various sulfoxide and N-oxide
CC       compounds. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250};
CC   -!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer
CC       (DmsAB) and a membrane anchor protein (DmsC). {ECO:0000250}.
DR   EMBL; AE005674; AAN42487.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16359.1; -; Genomic_DNA.
DR   RefSeq; NP_706780.1; NC_004337.2.
DR   ProteinModelPortal; Q83RZ7; -.
DR   SMR; Q83RZ7; -.
DR   EnsemblBacteria; AAN42487; AAN42487; SF0854.
DR   EnsemblBacteria; AAP16359; AAP16359; S0895.
DR   GeneID; 1023813; -.
DR   KEGG; sfl:SF0854; -.
DR   KEGG; sfx:S0895; -.
DR   PATRIC; fig|198214.7.peg.985; -.
DR   eggNOG; ENOG4105QAX; Bacteria.
DR   eggNOG; COG0437; LUCA.
DR   HOGENOM; HOG000163387; -.
DR   KO; K07307; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
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:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR014297; DMSO_DmsB.
DR   Pfam; PF13247; Fer4_11; 1.
DR   Pfam; PF12800; Fer4_4; 1.
DR   TIGRFAMs; TIGR02951; DMSO_dmsB; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Reference proteome; Repeat; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    205       Anaerobic dimethyl sulfoxide reductase
FT                                chain B.
FT                                /FTId=PRO_0000159243.
FT   DOMAIN        5     33       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       59     89       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       90    119       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        14     14       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        17     17       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        20     20       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        24     24       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        67     67       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL        70     70       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL        75     75       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL        79     79       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL        99     99       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       102    102       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       105    105       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       109    109       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       126    126       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       129    129       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       141    141       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       145    145       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   CONFLICT     15     15       A -> T (in Ref. 2; AAP16359).
FT                                {ECO:0000305}.
SQ   SEQUENCE   205 AA;  22839 MW;  72A54C139D1470A3 CRC64;
     MTTQYGFFID SSRCAGCKTC ELACKDYKDL TPEVSFRRIY EYAGGDWQED NGVWHQNVFA
     YYLSISCNHC EDPACTKVCP SGAMHKREDG FVVVDEDVCI GCRYCHMACP YGAPQYNETK
     GHMTKCDGCY DRVAEGKKPI CVESCPLRAL DFGPIDELRK KHGDLAAVAP LPRAHFTKPN
     IVIKPNANSR PTGDTTGYLA NPKEV
//
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