ID A0A0U1NXB6_9BACI Unreviewed; 654 AA.
AC A0A0U1NXB6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=NADH dehydrogenase subunit L {ECO:0000313|EMBL:CRK82653.1};
GN Name=nuoL {ECO:0000313|EMBL:CRK82653.1};
GN ORFNames=BN000_02586 {ECO:0000313|EMBL:CRK82653.1};
OS Neobacillus massiliamazoniensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1499688 {ECO:0000313|EMBL:CRK82653.1, ECO:0000313|Proteomes:UP000199087};
RN [1] {ECO:0000313|Proteomes:UP000199087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LF1 {ECO:0000313|Proteomes:UP000199087};
RA Urmite Genomes;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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; CVRB01000002; CRK82653.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1NXB6; -.
DR STRING; 1499688.BN000_02586; -.
DR Proteomes; UP000199087; Unassembled WGS sequence.
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 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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199087};
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 36..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 404..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 438..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 527..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 578..597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 631..653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..145
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 161..450
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 71210 MW; 55D4F49DC20D94AA CRC64;
MKWVSGTEGV STPDGQMSTG GVRHRKKGIV IMMENAWIIP LFPLLSFLIL LLFGKRLKEA
SAYVGILLTL ASLVFSILVL FERFTSPSYG ANFDWLTIGD IHLTAGFEVN QLNALMLFIV
SLISFLVHTY SKGYMHGDER IPVFYAYLGL FTFGMLGLVI SPNLLQTYVF WEIVGLGSFL
LIGFYFYKEE AKAAAKKAFI MTRIGDVGLF IGMILLFWQT KSFDYSDIFK AVESGSISPS
MITLTAILIF IGAIGKSGQF PLHTWLPDAM EGPTPVSALI HAATMVVAGV YLVAALFPLF
LASKTALMTI AVIGAFTAIF AASIGLVQTD IKRVLAYSTV SQLGYMMLAL GSAGYVAGVF
HLMTHAFFKA LLFLAAGSVI HAVHTQNIEE MGGLWKKLKL TGPLFLIGTL AISGVPLLSG
FFSKDEILAA AWEGGHPILF ILALIAAFFT AFYMFRLFFM VFTGEARSDI SKAHESPSVM
TFPMIILGVL AIFAGYVNTP WFGNFLGDWL VAGNPILAAN NHEASPIWIM ILATVVSLGG
IYLAWLIYGK RSIARNWLGS TGEKLHTVLL NKYYIDEFYQ MTVVAIASGI SYFLQFIDTF
LVQGLVNGVT GIVQGLGKIG SKMQSGQVQT YGAVAFIGLA LLAIVFALTG GYLK
//
