ID A0A1C2HBN2_9RHOB Unreviewed; 705 AA.
AC A0A1C2HBN2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:OCX61130.1};
GN ORFNames=BFP70_16945 {ECO:0000313|EMBL:OCX61130.1};
OS Thioclava sp. SK-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1889770 {ECO:0000313|EMBL:OCX61130.1, ECO:0000313|Proteomes:UP000094269};
RN [1] {ECO:0000313|EMBL:OCX61130.1, ECO:0000313|Proteomes:UP000094269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-1 {ECO:0000313|EMBL:OCX61130.1,
RC ECO:0000313|Proteomes:UP000094269};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Thioclava sp. strain SK-1.";
RL Submitted (AUG-2016) 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:OCX61130.1}.
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DR EMBL; MDHA01000069; OCX61130.1; -; Genomic_DNA.
DR RefSeq; WP_066012866.1; NZ_MDHA01000069.1.
DR AlphaFoldDB; A0A1C2HBN2; -.
DR STRING; 1889770.BFP70_16945; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000094269; 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:UP000094269};
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..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 577..598
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 680..700
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 134..439
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT REGION 516..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 77306 MW; 8913A369DBD4BACA CRC64;
MASIILFAPL LGAIIGGFGW RLITEKGAMA LTTGLLFLSC VLSWVLFLGH DGTLQQIDLF
TWVTSGDLDT SWSIRLDRLT VIMLIVITSV SALVHLYSWG YMAHDENFPD QAYKARFFAY
LSLFTFMMLM LVTADNVLQM FFGWEGVGLA SYLLIGFYFK KPSAGAAAMK AFIVNRVGDF
GFLLGIFALF FLVGSIDFNT IFAAGPQLAE TQLHFLWRDW NAAELIAMLL FIGAMGKSAQ
LLLHTWLPDA MEGPTPVSAL IHAATMVTAG VFLVCRMSPI FEFAPHAKMF IVFLGGTTAF
FAATVGLVQN DIKRVIAYST CSQLGYMFVA AGVGVYSVAM FHLLTHAFFK AMLFLGAGSV
IHAMHHEQDM RNYGNLRKKI PVTFWAMMIG TLAITGVGIP LTHIGFAGFL SKDAVIESAY
AGTNGGYAFW MLVIAALFTS FYSWRLIFMT FFGKERGDRH THEHAHESPL VMTIPLGVLA
LGAVFSGMVW YNSFFGDHSK VLSFFGLPAH HEEMAEGHGA QADAHASTTV DSHAEPAEAA
TADAHGAHDV VAGVAPQGAI FMAADNTVLD DAHHVPVWVK ISPFIAMLIG LATAWLFYIK
DTSLPVRLAK AQPGLYQFLL NKWYFDELYD FVFVRPAKWL GKFLWKKGDV GVIDGGINGL
ALGLIPALTR LAGRFQSGYL FHYAFAMVVG IVVLMFWVVM TGGSH
//
