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NUOB2_ROSS1
ID   NUOB2_ROSS1             Reviewed;         167 AA.
AC   A5UZH9;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=NADH-quinone oxidoreductase subunit B 2 {ECO:0000255|HAMAP-Rule:MF_01356};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01356};
DE   AltName: Full=NADH dehydrogenase I subunit B 2 {ECO:0000255|HAMAP-Rule:MF_01356};
DE   AltName: Full=NDH-1 subunit B 2 {ECO:0000255|HAMAP-Rule:MF_01356};
GN   Name=nuoB2 {ECO:0000255|HAMAP-Rule:MF_01356};
GN   OrderedLocusNames=RoseRS_3677;
OS   Roseiflexus sp. (strain RS-1).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=357808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Roseiflexus sp. RS-1.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_01356}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01356};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01356};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01356};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC       D, E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01356}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01356};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01356};
CC       Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01356}.
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01356}.
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DR   EMBL; CP000686; ABQ92032.1; -; Genomic_DNA.
DR   RefSeq; WP_011958374.1; NC_009523.1.
DR   AlphaFoldDB; A5UZH9; -.
DR   SMR; A5UZH9; -.
DR   STRING; 357808.RoseRS_3677; -.
DR   EnsemblBacteria; ABQ92032; ABQ92032; RoseRS_3677.
DR   KEGG; rrs:RoseRS_3677; -.
DR   eggNOG; COG0377; Bacteria.
DR   HOGENOM; CLU_055737_7_3_0; -.
DR   OMA; GWARKYS; -.
DR   OrthoDB; 1904620at2; -.
DR   Proteomes; UP000006554; 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:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_01356; NDH1_NuoB; 1.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   TIGRFAMs; TIGR01957; nuoB_fam; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding; NAD;
KW   Quinone; Reference proteome; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..167
FT                   /note="NADH-quinone oxidoreductase subunit B 2"
FT                   /id="PRO_0000376351"
FT   BINDING         38
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   BINDING         39
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   BINDING         104
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   BINDING         133
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
SQ   SEQUENCE   167 AA;  18336 MW;  C6C0CC5C932D357F CRC64;
     MGIEQKAGDM GIVTASLEQL VNWSRSSAMW PLLFGLACCA IEMMGAQGAN YDLSRFGMEI
     NRASPRQADL MIVAGRVSRK MAPVVRRLYD QMADPKWVIA MGDCAACGGV FNNYAIVQGV
     DEIVPVDVYV AGCPPRPEAL IDGIIHLHEK VKRMRLDGEL REPVRLS
 
 
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