ID   NUOB_BLOPB              Reviewed;         236 AA.
AC   Q492H7;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=NADH-quinone oxidoreductase subunit B {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 {ECO:0000255|HAMAP-Rule:MF_01356};
DE   AltName: Full=NDH-1 subunit B {ECO:0000255|HAMAP-Rule:MF_01356};
GN   Name=nuoB {ECO:0000255|HAMAP-Rule:MF_01356}; OrderedLocusNames=BPEN_508;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPEN;
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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 13 different subunits. Subunits NuoB, CD,
CC       E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01356}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01356}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01356}; 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; CP000016; AAZ41122.1; -; Genomic_DNA.
DR   RefSeq; WP_011283033.1; NC_007292.1.
DR   AlphaFoldDB; Q492H7; -.
DR   SMR; Q492H7; -.
DR   STRING; 291272.BPEN_508; -.
DR   EnsemblBacteria; AAZ41122; AAZ41122; BPEN_508.
DR   KEGG; bpn:BPEN_508; -.
DR   eggNOG; COG0377; Bacteria.
DR   HOGENOM; CLU_055737_7_3_6; -.
DR   OMA; GPYWEHG; -.
DR   BioCyc; CBLO291272:BPEN_RS02510-MON; -.
DR   Proteomes; UP000007794; 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.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; NAD; Quinone; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..236
FT                   /note="NADH-quinone oxidoreductase subunit B"
FT                   /id="PRO_0000376152"
FT   BINDING         68
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   BINDING         69
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   BINDING         134
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT   BINDING         163
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
SQ   SEQUENCE   236 AA;  26957 MW;  E9318C1BA35B1D36 CRC64;
     MKYTLTTART DNSEDEQYPL QEKKIVTDPL EKNIQRNVFF GKLSAFLHKI VNWGRGNSLW
     PYNFGLSCCY VEMTTAFTAI HDVARFGSEV LRASPRQADF MVIAGTPFLK MVPVIQRLYD
     QMLEPKWVIS MGACANSGGM YDIYSVVQGV DKFLPVDLYI PGCPPRPEAY IQGLLLLKKS
     INEERRPLSW VLGDQGIYRK NMESERQRKR NTRIAETVLS SPDDELNIYS KQNGEA