ID A0A3D9BQG2_9RHOB Unreviewed; 686 AA.
AC A0A3D9BQG2;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:REC55755.1};
GN ORFNames=DRV84_11065 {ECO:0000313|EMBL:REC55755.1};
OS Rhodosalinus sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodosalinus.
OX NCBI_TaxID=1940533 {ECO:0000313|EMBL:REC55755.1, ECO:0000313|Proteomes:UP000257131};
RN [1] {ECO:0000313|EMBL:REC55755.1, ECO:0000313|Proteomes:UP000257131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDN1C137 {ECO:0000313|EMBL:REC55755.1,
RC ECO:0000313|Proteomes:UP000257131};
RX PubMed=29043957; DOI=10.1099/ijsem.0.002424;
RA Guo L.Y., Ling S.K., Li C.M., Chen G.J., Du Z.J.;
RT "Rhodosalinus sediminis gen. nov., sp. nov., isolated from marine
RT saltern.";
RL Int. J. Syst. Evol. Microbiol. 67:5108-5113(2017).
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:REC55755.1}.
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DR EMBL; QOHR01000016; REC55755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9BQG2; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000257131; 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:UP000257131};
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 260..282
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..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..580
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 661..681
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..446
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 686 AA; 74958 MW; 86D0953FBE79E183 CRC64;
METLLLFAPL AGALIAGFGW RAIGETAAMW VATGLLFFSA LLSWIVFLTF DGITETIQIL
RWIESGTLAT DWAIRLDRLT AVMLIVVTSV SALVHLYSFG YMAHDENFRE GEAYKARFFA
YLSLFTFAML MLVTADNLVQ LFFGWEGVGL ASYLLIGFYY RKPSANAAAI KAFVVNRVGD
FGFALGIFAI FFLVDSVRFE DVFAAAPTIA ETQITFLWGS WNAAELVAVL LFIGAMGKSA
QLLLHTWLPD AMEGPTPVSA LIHAATMVTA GVFLVCRMSP VMEFAPNAMT FVTWLGAATA
FFAATVGLVQ TDIKRVIAYS TCSQLGYMFV AAGVGAYPVA MYHLLTHAFF KAMLFLGAGS
VIHGMHHEQD MRNYGGLRAK FPYTFWAMLI GTLAITGVGI PAVLFTLGGV PIGFAGFLSK
DAVVESAYAG AGGVPFWLLV IAALLTSFYS WRLMFLTFWG KPRGDKHTHA HAHESPAVMT
VPLGVLAVGS VLAGMIWYNA FFGHTDSVAK FFGMPYAEAE AEGGEEAYGY VFAGEPGQGA
LYMAPENTVI ADAHAVPKWV KVSPFFAMLI GLGLAWLFYI RDPAIPKRLA ESQRPLYLFL
LNKWYFDELY EFVFVRPARG VARTLWKRGD GAVIDGTING VSMGAIPWLT RLAGRAQTGY
IFSYAFWMVV GIVAMITWMT LTGGAR
//
