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Database: UniProt
Entry: B5YKJ0_THEYD
LinkDB: B5YKJ0_THEYD
Original site: B5YKJ0_THEYD 
ID   B5YKJ0_THEYD            Unreviewed;       630 AA.
AC   B5YKJ0;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=NADH-quinone oxidoreductase chain l {ECO:0000313|EMBL:ACI21670.1};
DE            EC=1.6.99.5 {ECO:0000313|EMBL:ACI21670.1};
GN   OrderedLocusNames=THEYE_A0919 {ECO:0000313|EMBL:ACI21670.1};
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC   Bacteria; Nitrospirota; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC   Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX   NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI21670.1, ECO:0000313|Proteomes:UP000000718};
RN   [1] {ECO:0000313|Proteomes:UP000000718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87
RC   {ECO:0000313|Proteomes:UP000000718};
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT   ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACI21670.1, ECO:0000313|Proteomes:UP000000718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87
RC   {ECO:0000313|Proteomes:UP000000718};
RX   PubMed=25635016;
RA   Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA   Robb F.T., Ward N.L., Eisen J.A.;
RT   "Genome Sequence of the Sulfate-Reducing Thermophilic Bacterium
RT   Thermodesulfovibrio yellowstonii Strain DSM 11347T (Phylum Nitrospirae).";
RL   Genome Announc. 3:0-0(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}.
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DR   EMBL; CP001147; ACI21670.1; -; Genomic_DNA.
DR   RefSeq; WP_012546379.1; NC_011296.1.
DR   RefSeq; YP_002248755.1; NC_011296.1.
DR   AlphaFoldDB; B5YKJ0; -.
DR   STRING; 289376.THEYE_A0919; -.
DR   EnsemblBacteria; ACI21670; ACI21670; THEYE_A0919.
DR   KEGG; tye:THEYE_A0919; -.
DR   PATRIC; fig|289376.4.peg.905; -.
DR   eggNOG; COG1009; Bacteria.
DR   HOGENOM; CLU_007100_6_0_0; -.
DR   InParanoid; B5YKJ0; -.
DR   OrthoDB; 9807568at2; -.
DR   Proteomes; UP000000718; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR   Gene3D; 1.20.5.2700; -; 1.
DR   InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   InterPro; IPR003945; NU5C-like.
DR   InterPro; IPR001516; Proton_antipo_N.
DR   NCBIfam; TIGR01974; NDH_I_L; 1.
DR   PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR   PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   Pfam; PF00662; Proton_antipo_N; 1.
DR   PRINTS; PR01434; NADHDHGNASE5.
DR   PRINTS; PR01435; NPOXDRDTASE5.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000313|EMBL:ACI21670.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000718};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000320};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        33..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        138..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        255..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        284..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        313..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        345..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        380..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        421..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        466..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        509..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        612..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          66..116
FT                   /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          133..432
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
SQ   SEQUENCE   630 AA;  69947 MW;  24D3E5CCE7B59456 CRC64;
     MEKYYILILL FPLAGFLFNI LIGRFISPKV VSWAGVLSIL GSLVVALFAI AQVFSGKTIE
     YNIYTWILSD DLKVSFGYLI DQLTAVMLFV VCFVGWLIHI YSVGYMHGDP GYPRYFAYLN
     LFVFSMLMLV MGNNLVMLYF GWEAVGLCSY FLIGFWYHKK TASDAGKKAF IVNRIGDFGF
     ALGIFLLFIN VYALNYTDIF PKIPGLQGHT LNIFGWNIDL ITLIALLLFC GAVGKSAQIP
     LHVWLPDAME GPTPVSALIH AATMVTAGVF MVARLNPIYG MSEIALAVVA ITGAVTSFFA
     ATIALVQRDM KRIIAYSTIS QIGYMFIGCG MAAYGAGIFH LYTHAFFKAL LFMGAGSVMH
     AMAGELDIYK MGGLRKKMPI TYITFLIASL TIAGIPGFSG FFSKDEILWA AFASAKPYGK
     FIWLLGTITA ALTAFYTFRI LFVAFHGKFR GTPEEFKHVH ESPPIMTVPL IVLAIGSVIV
     GYFSIPHFLE PVIPKPVFAA PHEQERVVMT MSIIAGVTGI LIAGYIYIVK STVSARLAKT
     FSGVYKVLWN KYYVDELYSF LFVKPTLWIA EKFIERFADI KIIEGIVNGI PKLIYKTGLL
     IRPIQTGQLQ QYAIFMIAGI IIFVLIILNI
//
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