ID N0AS91_9BACI Unreviewed; 1270 AA.
AC N0AS91;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:AGK54034.1};
GN ORFNames=B1NLA3E_11410 {ECO:0000313|EMBL:AGK54034.1};
OS Bacillus sp. 1NLA3E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK54034.1, ECO:0000313|Proteomes:UP000013300};
RN [1] {ECO:0000313|EMBL:AGK54034.1, ECO:0000313|Proteomes:UP000013300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLA3E {ECO:0000313|EMBL:AGK54034.1};
RX PubMed=23833140;
RA Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA Brooks S., Kostka J.E., Green S.J.;
RT "Genome sequences for three denitrifying bacterial strains isolated from a
RT uranium- and nitrate-contaminated subsurface environment.";
RL Genome Announc. 1:e00449-13(2013).
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}.
CC -!- SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit A
CC family. {ECO:0000256|ARBA:ARBA00008483}.
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DR EMBL; CP005586; AGK54034.1; -; Genomic_DNA.
DR RefSeq; WP_015594092.1; NC_021171.1.
DR AlphaFoldDB; N0AS91; -.
DR STRING; 666686.B1NLA3E_11410; -.
DR KEGG; baci:B1NLA3E_11410; -.
DR eggNOG; COG0651; Bacteria.
DR eggNOG; COG1008; Bacteria.
DR HOGENOM; CLU_265453_0_0_9; -.
DR Proteomes; UP000013300; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR001516; Proton_antipo_N.
DR PANTHER; PTHR42682; HYDROGENASE-4 COMPONENT F; 1.
DR Pfam; PF00361; Proton_antipo_M; 3.
DR Pfam; PF00662; Proton_antipo_N; 2.
DR PRINTS; PR01437; NUOXDRDTASE4.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000013300};
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 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 366..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 400..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 512..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 540..562
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 574..596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 657..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 707..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 733..752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 758..779
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 791..808
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 814..831
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 843..864
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 884..904
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 938..958
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 964..984
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 991..1020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1026..1045
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1057..1075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1095..1115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1136..1157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1191..1212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..147
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 277..314
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 335..630
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 755..792
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 808..1110
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 1270 AA; 137738 MW; D0AD5D288DFE99BC CRC64;
MNALPLVGVL ILLLFEVIAV MKTKKLMALL IYSSLAEVGY ILLGIGNGTF VGQTGGLLHL
EYQILMRGLV FLAAFVIIKH GGTQNIAKLK GMGRTSPFIA TMFAFGIFSV MGLSPFKGSI
SKFLIVYSCI ENSHYVSASL AIMGSIIEAW YFIKILHQIC FAEAEEGEQS PDRPDHTSVM
FKKISYGVVI VLGTLTALTS LFPEPLIAFS GNLANLLFGT TELELPVFDS LWPILVLVPY
IGAFIVFIAG HFLPKLSGTL AVCIGAATVG MVWMDGKIDG LSKFFALIIS VIMSLAIIYS
IGYFKNEKRN NRYFFFMLLT LGSLIGVATS TKFGNFYVFW ELMTWASYLL IVHVPTQKAL
NAGFKYFMMC TTGAYFMQFG ILLLQHSAGT IDMGAVSDKL PLIAPSMLIA IIVMFVIGTG
VKTGLVPMHS WLPEAHPAAP SPVSSILSGI LTKIGLYGLV RVLFAVFGVG LLTQLGSTGK
FSYIGLSISI LGIITSLYGE IMALRQKDIK RLLAYSTMGQ LGEIVTTLGL GTYLSMVAGL
YHVLNHAVMK GMLFLAVGLL VHKLKSRDIT AFKGVGKVMP FTAGCLSIGI LAIMGLPPFN
GFISKFLMLY AAVSSGYWYI AALILLGSII AAIYYIRLIK TIFFEKYEGH AVKEGPLTML
IPIGLLTGVV IFNGLFPQFA LKLVISAANS VAAKGGLAIT SIPEIQVSWP VIIIIPMLGG
LLAFFLGKRS PKIAGWISVA VMSVTLVVIA VSHAKFDIYS LSFALLIAFI GLLNILFSLG
YMGHGHSQNR YYMFFLMMIG GLIGVATSNE FFSFFIYWEI MSSWTLYFSI IHEETKGALK
EGFKYFIFNY IGASIAFLGI LILTVKTGVF DMSILVERLK EIDLGTSGLG LTLITVGFLM
KAAVLPFRID YQMHPSTAPT PVSGYISSVL LKSAPYSLIK LFFIMGGAVV VGRLGMVFNN
STLMYTVSWI AGLSIVGAGA MGLVQKGIKR LLIYSTVSQI GYIILGLSLG STLGLTGAML
HFVNHMFFKD LLFLAAGAIM VQAHVRNLDD VTGLGRKMPV TLAFFMIGAL SLAGIPPFSG
FTSKWIIYEA AMEKGYVFLA ILSLVGSVLT MAYFVKFMHS AFFGIPSKNS ENVKEASWTM
LVPMGVLSAV SIIFGIMPGL PLTVISKVLS LAGFAQPTYT LFSVDTPIGS WQVGTITITI
LLALVVGLVL LLSGNKKVRY TDAYTCGVTD LDAEKINVAS ENMYETPAKL VKRLHRIIIP
VFGNGEEEEE
//
