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Database: UniProt
Entry: A0A2W7NWE3_9RHOB
LinkDB: A0A2W7NWE3_9RHOB
Original site: A0A2W7NWE3_9RHOB 
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
//
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