ID A0A1I0CZ97_9BACI Unreviewed; 620 AA.
AC A0A1I0CZ97;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=NADH-quinone oxidoreductase subunit L {ECO:0000313|EMBL:SET24821.1};
GN ORFNames=SAMN05421676_103334 {ECO:0000313|EMBL:SET24821.1};
OS Salinibacillus kushneri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salinibacillus.
OX NCBI_TaxID=237682 {ECO:0000313|EMBL:SET24821.1, ECO:0000313|Proteomes:UP000199095};
RN [1] {ECO:0000313|EMBL:SET24821.1, ECO:0000313|Proteomes:UP000199095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3566 {ECO:0000313|EMBL:SET24821.1,
RC ECO:0000313|Proteomes:UP000199095};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit A
CC family. {ECO:0000256|ARBA:ARBA00008483}.
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DR EMBL; FOHJ01000003; SET24821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0CZ97; -.
DR STRING; 237682.SAMN05421676_103334; -.
DR OrthoDB; 9807568at2; -.
DR Proteomes; UP000199095; 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 3: Inferred from homology;
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..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 495..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 598..616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..114
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 130..419
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 620 AA; 68128 MW; C7F925DF15DCF19A CRC64;
MIEFVWLIPT LPLLTFILLT ILRDKVNQTG SYMAICLTGM AFILSVLVFI QLIDAGTAVQ
EWEWITIGSI QISFGTLLNP LNGLMLILVA FISLLIHIYS LGYMERDQRM TTFFAYLSLF
TAAMLGLVIS PNLLQFYVFW ELVGLGSFLL IGFYYYKNSA KNAAQKAFIM TRVGDMGLLI
GLILLFWQTG SLQFEAIFSA ITGGDVEGSM LTLIAILIFI GAIGKSGQFP LHTWLPDAME
GPTPVSALIH AATMVAAGVY LVAVMYPLYM ASTTALMVVT VVGGFTAIYA ASIGLVQNDI
KQVLAYSTIS QLGFMMLAMG TLGYTAGVFH LFTHAFFKAL LFLAAGVVIH AIHTQNIKQM
GGLHQRLKLT SITFAIGALA ISGFPLFSGF FSKEEILSAV WADGQYGLWL VALVAAFLTS
LYMFRLYFLV FHGESKQRLD QIGLVPKTMK IPMSILAVFS IFSGFFNTSW FGSYLGDWLI
GDNQMLTNTH HGSSIGVMLI ASIISIGGII LAYMIYVKKS FDQTSLQSSF SGTYKLLANK
FFMDEFYHTS FVKGAKGVGK IFVYVERYGV GFLLAFIREM LTTLSKSGSK TQTGQTQTYA
AVAFLGMVLF TAIYILKGGY
//