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Database: UniProt
Entry: A0A1D7VEH4_9ACTN
LinkDB: A0A1D7VEH4_9ACTN
Original site: A0A1D7VEH4_9ACTN 
ID   A0A1D7VEH4_9ACTN        Unreviewed;       287 AA.
AC   A0A1D7VEH4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN   ORFNames=SL103_01890 {ECO:0000313|EMBL:AOP45154.1};
OS   Streptomyces lydicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=47763 {ECO:0000313|EMBL:AOP45154.1, ECO:0000313|Proteomes:UP000094094};
RN   [1] {ECO:0000313|EMBL:AOP45154.1, ECO:0000313|Proteomes:UP000094094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=103 {ECO:0000313|EMBL:AOP45154.1,
RC   ECO:0000313|Proteomes:UP000094094};
RA   Jia N., Ding M.-Z., Gao F., Yuan Y.-J.;
RT   "Complete genome sequencing of Streptomyces lydicus 103 and metabolic
RT   pathways analysis of antibiotic biosynthesis.";
RL   Submitted (SEP-2016) 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. 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}.
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DR   EMBL; CP017157; AOP45154.1; -; Genomic_DNA.
DR   RefSeq; WP_069567023.1; NZ_CP017157.1.
DR   AlphaFoldDB; A0A1D7VEH4; -.
DR   KEGG; slc:SL103_01890; -.
DR   OrthoDB; 13239at2; -.
DR   Proteomes; UP000094094; Chromosome.
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:UP000094094};
KW   Transmembrane {ECO:0000256|RuleBase:RU004429};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU004429};
KW   Ubiquinone {ECO:0000313|EMBL:AOP45154.1}.
FT   TRANSMEM        14..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        40..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        67..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        142..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   REGION          176..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   287 AA;  30365 MW;  F9250B70D75917D1 CRC64;
     MSTLAAAAST GEAVQFWLLG TVAVIGALCT ILMKRAVHSA LSLAGTMIVL AVFYLANGAY
     FLGVVQIVVY TGAIMMLFLF VVMLVGVTAA DSLKETLKGQ RWLAAGLGIG FGILLIAGIG
     NASLKEFNGL GEANAGGNVQ GLAALIFTKY VFAFEITGAL LITAAVGAMV LTHRERTERA
     RTQREQSEAR IREGKQVPPL PAPGVYARHN AVDIPGLLPD GTPSDLTVSP TLRERGQIRD
     VSGESLAELK ALERRTEDWL GRTSGEEPRP SSSGGTTPTE RKEEAKK
//
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