ID A0A2W7NWE3_9RHOB Unreviewed; 712 AA.
AC A0A2W7NWE3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:PZX17626.1};
GN ORFNames=LX81_01351 {ECO:0000313|EMBL:PZX17626.1};
OS Palleronia aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Palleronia.
OX NCBI_TaxID=568105 {ECO:0000313|EMBL:PZX17626.1, ECO:0000313|Proteomes:UP000248916};
RN [1] {ECO:0000313|EMBL:PZX17626.1, ECO:0000313|Proteomes:UP000248916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22009 {ECO:0000313|EMBL:PZX17626.1,
RC ECO:0000313|Proteomes:UP000248916};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-2018) 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. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient. {ECO:0000256|ARBA:ARBA00002378}.
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 -!- 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:PZX17626.1}.
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DR EMBL; QKZL01000004; PZX17626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W7NWE3; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000248916; 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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000248916};
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..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 586..607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 689..710
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..109
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 135..431
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT REGION 518..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 712 AA; 78018 MW; BC449F9B6844A035 CRC64;
METIILFAPL VGALICGFGW RFMGEVPAQW TATGLLFLTA LLSWIVFFGF DGETQRIQIL
RWIESGSLST DWAIRMDRLT AIMLVVITTV SSLVHLYSFG YMAHDENFRD DESYRPRFFA
YLSFFTFAML MLVTADNLVQ MFFGWEGVGV ASYLLIGFYY RKPSANAAAI KAFVVNRVGD
FGFALGIFAI FFLVDSINFE DIFAAAPELA QTQMSFLWRE WNAMEVICVL LFVGAMGKSA
QLFLHTWLPD AMEGPTPVSA LIHAATMVTA GVFLVCRMSP LMEFAPTATA FVTVIGATTA
FFAATIGLVQ NDIKRVIAYS TCSQLGYMFA AAGVGVYSAA MFHLFTHAFF KAMLFLGAGS
VIHGMHHEQD MRNYGGLRHK MPYTFWAMMI GTLAITGVGI PLTHIGFAGF LSKDAIIEST
WGAHSGPGVY AFWLLVVAAA FTSFYSWRLM FLTFFGDARG DRHTHDHAHE SPKIMLAPLG
ALALGAVFSG MLWFNSFFGD EEAVANFFGL PHVEQTEEAA AGEGEGASSA VEDLAEGDAG
EAAEAVTEPE AGPSEHSDFA GNAPGVGAIY IAPDNHVLDE AHHSPVWVAV SPFVAMLLGL
GAAYMMYVRR TDLPRKFADS QPALYRFLLN KWYFDEIYNA IFTRPSKALG AFLWKRGDGN
VIDGGINGIA MGIIPFFTRL AGRAQSGYLF HYAFAMVLGI ALFITLMTLL GS
//