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Database: UniProt
Entry: A0A132MGB2_HYDSH
LinkDB: A0A132MGB2_HYDSH
Original site: A0A132MGB2_HYDSH 
ID   A0A132MGB2_HYDSH        Unreviewed;       177 AA.
AC   A0A132MGB2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN   ORFNames=HSCHL_1933 {ECO:0000313|EMBL:PTQ54990.1}, KM312_01925
GN   {ECO:0000313|EMBL:MBT9281412.1}, SA87_09490
GN   {ECO:0000313|EMBL:OAR04734.1};
OS   Hydrogenibacillus schlegelii (Bacillus schlegelii).
OC   Bacteria; Bacillota; Bacilli; Bacillales;
OC   Bacillales Family X. Incertae Sedis; Hydrogenibacillus.
OX   NCBI_TaxID=1484 {ECO:0000313|EMBL:PTQ54990.1, ECO:0000313|Proteomes:UP000244180};
RN   [1] {ECO:0000313|EMBL:OAR04734.1, ECO:0000313|Proteomes:UP000243024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MA 48 {ECO:0000313|EMBL:OAR04734.1,
RC   ECO:0000313|Proteomes:UP000243024};
RA   Hemp J.;
RT   "Draft genome sequence of Hydrogenibacillus schlegelii DSM 2000.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PTQ54990.1, ECO:0000313|Proteomes:UP000244180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL33 {ECO:0000313|EMBL:PTQ54990.1};
RA   Kadnikov V.V., Mardanov A.V., Ivasenko D., Beletsky A.V., Karnachuk O.V.,
RA   Ravin N.V.;
RT   "Burning lignite coal seam in the remote Altai Mountains harbors a
RT   hydrogen-driven thermophilic microbial community.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:MBT9281412.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RBS10-49 {ECO:0000313|EMBL:MBT9281412.1};
RA   Kadnikov V., Mardanov A.V., Beletsky A.V., Karnachuk O.V., Ravin N.V.;
RT   "Metagenomic Analysis of the Microbial Community in the Underground Coal
RT   Fire Area (Kemerovo Region, Russia) Revealed Predominance of Thermophilic
RT   Members of the Phyla Deinococcus-thermus, Aquificae, and Firmicutes.";
RL   Microbiology 0:0-0(2021).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC       reaction to proton translocation (for every two electrons transferred,
CC       four hydrogen ions are translocated across the cytoplasmic membrane),
CC       and thus conserves the redox energy in a proton gradient.
CC       {ECO:0000256|RuleBase:RU004429}.
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|RuleBase:RU004429};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU004429};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU004429}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 6 family.
CC       {ECO:0000256|ARBA:ARBA00005698, ECO:0000256|RuleBase:RU004429}.
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:PTQ54990.1}.
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DR   EMBL; JAHHQF010000039; MBT9281412.1; -; Genomic_DNA.
DR   EMBL; JXBB01000012; OAR04734.1; -; Genomic_DNA.
DR   EMBL; PEBV01000001; PTQ54990.1; -; Genomic_DNA.
DR   RefSeq; WP_066200130.1; NZ_PEBV01000001.1.
DR   AlphaFoldDB; A0A132MGB2; -.
DR   STRING; 1484.SA87_09490; -.
DR   OrthoDB; 9814997at2; -.
DR   Proteomes; UP000243024; Unassembled WGS sequence.
DR   Proteomes; UP000244180; Unassembled WGS sequence.
DR   Proteomes; UP000748108; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.1200; NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ; 1.
DR   InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR   InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR   PANTHER; PTHR33269:SF5; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 6, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR33269; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 6; 1.
DR   Pfam; PF00499; Oxidored_q3; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|RuleBase:RU004429};
KW   Membrane {ECO:0000256|RuleBase:RU004429};
KW   NAD {ECO:0000256|RuleBase:RU004429};
KW   Quinone {ECO:0000256|RuleBase:RU004429};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243024};
KW   Transmembrane {ECO:0000256|RuleBase:RU004429};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU004429};
KW   Ubiquinone {ECO:0000313|EMBL:PTQ54990.1}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        32..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        59..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        90..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        141..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
SQ   SEQUENCE   177 AA;  18492 MW;  BA02CDD1FD3FF254 CRC64;
     MESNVVVFLT VAALALFGGV MMLSLRRVLH MALAVALSFL SVAGVFFLLG AEFLGVMQII
     VYTGAVTVLA VFGIMLTRHD AVDVQTARGA VQRGLAGIVA AGGFLFLFYL LLRSPLEPDG
     AGGPPVVSIG AIGEALFSPE FILAFELVGV MLLAALIGAV TVAREEAPEA DREEEGR
//
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