ID A0A0R0CHF2_9GAMM Unreviewed; 503 AA.
AC A0A0R0CHF2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=NADH:ubiquinone oxidoreductase subunit M {ECO:0000313|EMBL:KRG68880.1};
DE EC=1.6.5.11 {ECO:0000313|EMBL:KRG68880.1};
GN ORFNames=ABB29_10425 {ECO:0000313|EMBL:KRG68880.1};
OS Pseudoxanthomonas dokdonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=344882 {ECO:0000313|EMBL:KRG68880.1, ECO:0000313|Proteomes:UP000052052};
RN [1] {ECO:0000313|EMBL:KRG68880.1, ECO:0000313|Proteomes:UP000052052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21858 {ECO:0000313|EMBL:KRG68880.1,
RC ECO:0000313|Proteomes:UP000052052};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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 complex I subunit 4 family.
CC {ECO:0000256|ARBA:ARBA00009025}.
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:KRG68880.1}.
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; LDJL01000011; KRG68880.1; -; Genomic_DNA.
DR RefSeq; WP_057658770.1; NZ_LDJL01000011.1.
DR AlphaFoldDB; A0A0R0CHF2; -.
DR STRING; 344882.ABB29_10425; -.
DR PATRIC; fig|344882.3.peg.456; -.
DR OrthoDB; 9768329at2; -.
DR Proteomes; UP000052052; 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 InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR NCBIfam; TIGR01972; NDH_I_M; 1.
DR PANTHER; PTHR43507; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4; 1.
DR PANTHER; PTHR43507:SF20; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:KRG68880.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052052};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubiquinone {ECO:0000313|EMBL:KRG68880.1}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..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..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..427
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 503 AA; 54525 MW; 36C22BC40B6481F3 CRC64;
MSNWPLLSIL IWLPILGGAA VLALGSGRAS LARWTALAVA VLTFLLSLPL LSGFDAANPG
MQFVEKHAWI PSFNIWYALG ADGIAIALIL LTTLVTVLTL IGAWTSIDKR VNQYVAAFLI
LEGVTVGIFA ATDAMLFYVF FEAMLIPMFL IIGVWGGPRR IYAAVKFFLY TFLGSVFMLL
ALIYLYLKGG SFQIADLYAL PLSMKEQTWL FFAFLIAFAV KVPMFPVHTW LPDAHVEAPT
AGSVILAAIA LKIGGYGLIR FNLPIVPDAG HEYAWVVITL SLIAVIYVGL VALVQDDMKK
LIAYSSVSHM GFVTIGIFIA FGLVRDYGNL DGARLGLQGA MVQMISHGFV SGAMFSCVGV
LYDRMHTRMI RDYGGVANVM PWFAVFFVLF GMANAGLPGT SGFVGEFMVI LASFQKHPLI
ALAAASTLII GAAYTLWLVR RVMYGEVANA HVAELKDINR REALVLGLFA AGVLALGVYP
KPLTDLMEPS IAQLAMQLAN SKL
//