ID A0A420XL01_9ACTN Unreviewed; 631 AA.
AC A0A420XL01;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:RKS69216.1};
GN ORFNames=CLV35_3390 {ECO:0000313|EMBL:RKS69216.1};
OS Motilibacter peucedani.
OC Bacteria; Actinomycetota; Actinomycetes; Motilibacterales;
OC Motilibacteraceae; Motilibacter.
OX NCBI_TaxID=598650 {ECO:0000313|EMBL:RKS69216.1, ECO:0000313|Proteomes:UP000281955};
RN [1] {ECO:0000313|EMBL:RKS69216.1, ECO:0000313|Proteomes:UP000281955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RP-AC37 {ECO:0000313|EMBL:RKS69216.1,
RC ECO:0000313|Proteomes:UP000281955};
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 (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RKS69216.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RBWV01000015; RKS69216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420XL01; -.
DR InParanoid; A0A420XL01; -.
DR Proteomes; UP000281955; 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:UP000281955};
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..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 33..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 507..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 611..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..123
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 139..425
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 631 AA; 66253 MW; 4531661726545646 CRC64;
MTSTSYALAP ALLALPVAGA AVLLLGGRRT DRFGHVIGTL ASVAAFVVAA VVWVQMIGRD
EADRPAVQKL WTFVHTGGFR VDVGLQLDQL SIVFALLITG VGSLIHVYSI AYMEHDAHRR
RFFAYLNLFV AAMLLLVLAS DYLLVYVGWE GVGLASYLLI GFWSHNPPYA TAAKKAFVAN
RVGDIGMSLA IVMMFTTFGA TDFARVLPNA GSASDGRLTA IGLLLLLAAC GKSAQLPLQS
WLGDAMAGPT PVSALIHAAT MVTAGVYLIV RSGAIFDESP DARLVVTIVG AATLLFGALI
GTAKDDVKKA LAASTMSQIG YMVLAAGLGP AGYAIAIFHL LTHGFFKAGL FLGAGSVMHA
MGDRTDMRRF GGLWRVMPVT GATFGLGYLA IIGCPPFSGF WSKDKIIEAA FDKGGTSGWI
LGLVALLGAG ITAFYMTRVF VMTFLGPRRW RDDVHPHEAP TLMTAPMVVL ALGSVFLGGV
LTIGATLQNW LEPAVGKSAE EGAHTMSPLV LSLLTLLVVL GGVAGAAAMY ARREVPLTAP
VAGPLTVAAR NDLYQDAVNE AVLMRPGQYV TRSLVFGDLR GVDGLVNGFA AVIGGTSGRL
RRLQTGFVRS YALSVLGGAV LLAGALLIVR I
//