ID C9MQ80_9BACT Unreviewed; 503 AA.
AC C9MQ80;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Proton-translocating NADH-quinone oxidoreductase, chain M {ECO:0000313|EMBL:EEX18336.1};
GN ORFNames=HMPREF0973_01779 {ECO:0000313|EMBL:EEX18336.1};
OS Prevotella veroralis F0319.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=649761 {ECO:0000313|EMBL:EEX18336.1, ECO:0000313|Proteomes:UP000003327};
RN [1] {ECO:0000313|EMBL:EEX18336.1, ECO:0000313|Proteomes:UP000003327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0319 {ECO:0000313|EMBL:EEX18336.1,
RC ECO:0000313|Proteomes:UP000003327};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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:EEX18336.1}.
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DR EMBL; ACVA01000040; EEX18336.1; -; Genomic_DNA.
DR RefSeq; WP_004383451.1; NZ_GG698714.1.
DR AlphaFoldDB; C9MQ80; -.
DR STRING; 649761.HMPREF0973_01779; -.
DR eggNOG; COG1008; Bacteria.
DR HOGENOM; CLU_007100_4_2_10; -.
DR OrthoDB; 9811718at2; -.
DR Proteomes; UP000003327; 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:SF4; PROTON-TRANSLOCATING NADH-QUINONE OXIDOREDUCTASE, CHAIN M; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003327};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 459..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..415
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 503 AA; 55224 MW; 64A71483174768D0 CRC64;
MSWILTVFVI IPVLMLCGLW VAKNDNQVRG MMVAGSTALL IGAIWLTVYF VQQRNAGNHD
AMLLANSVMW FKPMHIAFSV GVDGISVVMI LLSAIIVFTG TFASWQLEPM KKEYFLWFVL
LASGVFGFFI STDMFTMFMF YEVALIPMYL LIGVWGTGPK EYSAMKLTLM LMGGSALLIL
GILGIYYFSG ATTMDVIELA RMHAMPKNIQ NIFFPFVFIG FGVLGALFPF HTWSPDGHAS
APTAVSMLHA GVLMKLGGYG CLRIAMFLMP DALQTWAPIF LVLTTISVVY GALSACVQTD
LKYINAYSSV SHCGMVLFAL VMTTQTAITG AILQMLSHGL MTALFFACIG MIYHRAGTRD
VRYLGGLMKV IPFLAVSYVV AGLANLGLPG FSGFVAEMTI FVGSFENAGT FHRVATIIAC
TAIVITAVYI LRVVGKILFQ KIPNKKFYEL HDATWDERFA IGCLIFCVAG LGLCPLFFEN
MIIDAVHPIF DHIITYVPTL GNL
//
