ID A0A399J3R2_9RHOB Unreviewed; 703 AA.
AC A0A399J3R2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:RII39079.1};
GN ORFNames=DL237_07895 {ECO:0000313|EMBL:RII39079.1};
OS Pseudooceanicola sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=2211117 {ECO:0000313|EMBL:RII39079.1, ECO:0000313|Proteomes:UP000265848};
RN [1] {ECO:0000313|EMBL:RII39079.1, ECO:0000313|Proteomes:UP000265848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CY03 {ECO:0000313|EMBL:RII39079.1,
RC ECO:0000313|Proteomes:UP000265848};
RA Zhang Y.-J.;
RT "Pseudooceanicola sediminis CY03 in the family Rhodobacteracea.";
RL Submitted (AUG-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:RII39079.1}.
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DR EMBL; QWJJ01000006; RII39079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399J3R2; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000265848; 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 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..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..248
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..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 575..596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..108
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 135..440
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT REGION 514..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 77289 MW; 2D205EA16AB8EEF6 CRC64;
MVSIILFAPL IGALIAGFGW RLITVKGAQY LTTGLLFLAC FLSWITFFTT PELVQHIELM
RWIESGSLST SWGIRLDRLT STMLIVVTTV SALVHLYSLG YMAHDENFTD AEEYRPRFFA
YLSFFTFAML MLVTSDNLVQ MFFGWEGVGV ASYLLIGFYY KKPSANAAAM KAFVVNRVGD
FGFALGIFGL FYLTDSIHLD DVFAAAPQIA ETSISFLWQD WNAANLLAFL LFIGAMGKSA
QLFLHTWLPD AMEGPTPVSA LIHAATMVTA GVFLVCRMSP LMEYAPQTLA FITFMGATTA
FFAATVGLVQ TDIKRVIAYS TCSQLGYMFV AAGVGVYSAA MFHLLTHAFF KALLFLCAGS
VIHAMHHEQD MRNYGGLRKK IPYTFYAMVI GTLAITGVGI PFTGIGLAGF LSKDAIIESA
YAGTQGGYAF WMLVIAALFT SFYSWRLIFL TFYGTPRGDK HTHDHAHESP KVMLIPLGVL
SLGAIFSGML WYNSFFGDHD KVLSFFGMPE HHAEASEGTS EGDTHAVASA QGEGAEAEHG
AAGDHDVVTP GIAPQGAIFM APDNHTLEEA HHAPAWVKLS PFIAMLLGFI IAWAMYIKDT
TLPKRMADAN RPLYLFLLNK WYFDELYDFI FVRPAFWIGR TLWKSGDGKV VDGGINGLAM
GIIPFFTRLA GRAQNGYIFT YAFAMVIGIA VFVTWMSLTG GAE
//
