ID A0A0K2GFQ2_NITMO Unreviewed; 571 AA.
AC A0A0K2GFQ2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative NADH-quinone oxidoreductase, subunit L {ECO:0000313|EMBL:ALA59412.1};
DE EC=1.6.99.5 {ECO:0000313|EMBL:ALA59412.1};
GN ORFNames=NITMOv2_3007 {ECO:0000313|EMBL:ALA59412.1};
OS Nitrospira moscoviensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA59412.1, ECO:0000313|Proteomes:UP000069205};
RN [1] {ECO:0000313|EMBL:ALA59412.1, ECO:0000313|Proteomes:UP000069205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA59412.1,
RC ECO:0000313|Proteomes:UP000069205};
RX PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA Nielsen P.H., Wagner M., Daims H.;
RT "Expanded metabolic versatility of ubiquitous nitrite-oxidizing bacteria
RT from the genus Nitrospira.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(2015).
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 ---------------------------------------------------------------------------
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; CP011801; ALA59412.1; -; Genomic_DNA.
DR RefSeq; WP_053380428.1; NZ_CP011801.1.
DR AlphaFoldDB; A0A0K2GFQ2; -.
DR STRING; 42253.NITMOv2_3007; -.
DR KEGG; nmv:NITMOv2_3007; -.
DR PATRIC; fig|42253.5.peg.2970; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000069205; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR PANTHER; PTHR42829:SF1; INORGANIC CARBON TRANSPORTER SUBUNIT DABB-RELATED; 1.
DR PANTHER; PTHR42829; 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 Oxidoreductase {ECO:0000313|EMBL:ALA59412.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000069205};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 486..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..117
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 133..364
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 571 AA; 63176 MW; FEB852A0FA6AE94F CRC64;
MSLPIWILAP LLPLVAGVLI GLLGTRLRDQ SYKIGVPAVA GAFAVAIWAL FNVGRQEAPL
SSLFWSLPLP ASPWFRFGLQ LDRLSAVMMV LITGVSLTIH LYSRNYMQGD RGYARFYALL
GLITAVLLFL VTSANLFLLF VCWQLVSWLL YLLLVHNYGY GPAVKSAMKT WIILRLGDVA
FLSGVVLAYH TYGTLELSEL FERAAQHAAV VSLWPQGPEI DAVTAVTLLL FVGAMSKSAQ
FPLHVWLPDT MDTPTPVSAL MHAGIVNAGG FLFNRLAPLF GQALDTLHVA FVIGGLTAIV
GATIMLTQPD VKKMLGFSTM GQMGYMTMEC GLGAFALAIF HLVAHGIFKA TLFLHAGNIV
HQARREPKFP PGFEREDVDV HPHLPWLTGV AVTLVLPLAI LLAAHGLLHI PLQSQQGAIV
FLFFAWVTSS QAILSLYRLR AVGSWKVAGL MVIAIALVVA TYLWAAEAFT HFLYPSPGEA
ARYFEVAAFP LWLFDLFVMT VTLFVVMGWV VVYTNIKGQR SFMPGWIAGL MPRLYVWFWN
RLFIDALYER IVQAMARWAF RVNAKLPEWL P
//