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Database: UniProt
Entry: A0A2A9CXZ2_9MICO
LinkDB: A0A2A9CXZ2_9MICO
Original site: A0A2A9CXZ2_9MICO 
ID   A0A2A9CXZ2_9MICO        Unreviewed;       183 AA.
AC   A0A2A9CXZ2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=NADH-quinone oxidoreductase subunit B {ECO:0000256|HAMAP-Rule:MF_01356};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01356};
DE   AltName: Full=NADH dehydrogenase I subunit B {ECO:0000256|HAMAP-Rule:MF_01356};
DE   AltName: Full=NDH-1 subunit B {ECO:0000256|HAMAP-Rule:MF_01356};
GN   Name=nuoB {ECO:0000256|HAMAP-Rule:MF_01356};
GN   ORFNames=ATL40_0435 {ECO:0000313|EMBL:PFG18885.1};
OS   Serinibacter salmoneus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC   Serinibacter.
OX   NCBI_TaxID=556530 {ECO:0000313|EMBL:PFG18885.1, ECO:0000313|Proteomes:UP000224915};
RN   [1] {ECO:0000313|EMBL:PFG18885.1, ECO:0000313|Proteomes:UP000224915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21801 {ECO:0000313|EMBL:PFG18885.1,
RC   ECO:0000313|Proteomes:UP000224915};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2017) 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 a
CC       menaquinone. 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:0000256|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:0000256|HAMAP-Rule:MF_01356};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01356};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01356}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01356};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01356};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01356}.
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00009173, ECO:0000256|HAMAP-Rule:MF_01356,
CC       ECO:0000256|RuleBase:RU004464}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PFG18885.1}.
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DR   EMBL; PDJD01000001; PFG18885.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9CXZ2; -.
DR   OrthoDB; 9786737at2; -.
DR   Proteomes; UP000224915; Unassembled WGS sequence.
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   Gene3D; 3.40.50.12280; -; 1.
DR   HAMAP; MF_01356; NDH1_NuoB; 1.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR   NCBIfam; TIGR01957; nuoB_fam; 1.
DR   PANTHER; PTHR11995; NADH DEHYDROGENASE; 1.
DR   PANTHER; PTHR11995:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL; 1.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   SUPFAM; SSF56770; HydA/Nqo6-like; 1.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01356};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01356,
KW   ECO:0000256|RuleBase:RU004464}; Membrane {ECO:0000256|HAMAP-Rule:MF_01356};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01356,
KW   ECO:0000256|RuleBase:RU004464};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464};
KW   Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_01356};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224915};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01356};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01356}.
FT   DOMAIN          36..145
FT                   /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT                   /evidence="ECO:0000259|Pfam:PF01058"
FT   BINDING         36
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT   BINDING         37
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT   BINDING         102
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
FT   BINDING         131
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01356"
SQ   SEQUENCE   183 AA;  19620 MW;  7E37083F7E9AB7AA CRC64;
     MGLEEKAPGF MLGTIGDLVG LARKTSMWPV TMGLACCAIE MMATGGARFD ISRFGMEVFR
     ASPRHADLMI VSGRLSQKMA PVVRQVYDQM SEPKWVISMG ACASSGGMFN NYAVVQGCDH
     VVPVDIYLPG CPPRPEMLLH AILELHKQVG KEPLGANRVE IARAAEAAAL MATPTSDQKG
     LLA
//
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