ID A0A2T7G2Q1_9RHOB Unreviewed; 630 AA.
AC A0A2T7G2Q1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:PVA08703.1};
GN ORFNames=DC366_17700 {ECO:0000313|EMBL:PVA08703.1};
OS Pelagivirga sediminicola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pelagivirga.
OX NCBI_TaxID=2170575 {ECO:0000313|EMBL:PVA08703.1, ECO:0000313|Proteomes:UP000244446};
RN [1] {ECO:0000313|EMBL:PVA08703.1, ECO:0000313|Proteomes:UP000244446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH-SD19 {ECO:0000313|EMBL:PVA08703.1,
RC ECO:0000313|Proteomes:UP000244446};
RA Ji X.;
RT "Pelagivirga bohaiensis gen. nov., sp. nov., a bacterium isolated from the
RT Bohai Sea.";
RL Submitted (APR-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:PVA08703.1}.
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DR EMBL; QCYH01000019; PVA08703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7G2Q1; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000244446; 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; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
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.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000244446};
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 66..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..104
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 120..402
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 630 AA; 64387 MW; 8E7838D6206DC891 CRC64;
MSFLALTLLA PLLSGLTILA LRRAPEALAL AGTVLGLIGA VGLFIAASDG TVEAVLPGLP
DMPLRLVATP LTAVLALVVA TVAVFVLTYA TGYMAGDPEK ARFFGTMLLF VTAMQGLVLA
GDWIMLLAAW EMIGFASYLL IGFWHGRAGV ASAATRAFLY TRSADLGLYL GAFLLIGVAG
TSEISATLAT TGAPALIAGL LMLVAAMGKS AQVPLQDWLQ RAMAGPTPVS ALLHSATLVA
AGAILLIRTA PMMPGGALLA IGIVGGLTAV ITGLIALAER DLKRLLAAST ASQYGLMLVA
IGAGVPIAAL LHLIAHAAIK SSLFLGAGVF QHDREGTGLD TLAGAGRARP GIFTGFAIAA
LALAGIPPLA AFFSKDAIIA AALASTAAPW LLPLALAGSV LTGTYMGRAL NVLWTGEAGP
ARTPVPFMAI GMGVLVALAA GLGFSFGALE HVLGAQIEKP GWIVPAMGLA VALGGLALGW
FMAPARLLGP LLAPAQNGFT VAGGMDGLIL RPSLSIAAAC EAFEQRLLAA QVGLIRNLGL
GTARLADRGD DTLFAFSIWI GQQSLRLGQD TRSIDTNFID AAIFGLVRRI VEAGARARHL
QSGLIHRELA LTVIGIGLIV IVLLTAPHYF
//
