ID A0A1H3NWC1_9PROT Unreviewed; 531 AA.
AC A0A1H3NWC1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=NADH-quinone oxidoreductase subunit M {ECO:0000256|ARBA:ARBA00019906};
DE AltName: Full=NADH dehydrogenase I subunit M {ECO:0000256|ARBA:ARBA00031584};
DE AltName: Full=NDH-1 subunit M {ECO:0000256|ARBA:ARBA00032798};
GN ORFNames=SAMN05421754_103213 {ECO:0000313|EMBL:SDY93202.1};
OS Nitrosomonas sp. Nm58.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=200126 {ECO:0000313|EMBL:SDY93202.1, ECO:0000313|Proteomes:UP000199646};
RN [1] {ECO:0000313|Proteomes:UP000199646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm58 {ECO:0000313|Proteomes:UP000199646};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU000320}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU000320}.
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DR EMBL; FNPQ01000032; SDY93202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3NWC1; -.
DR STRING; 200126.SAMN05421754_103213; -.
DR Proteomes; UP000199646; 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; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR43507:SF1; NAD(P)H-QUINONE OXIDOREDUCTASE CHAIN 4, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43507; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199646};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..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..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 139..432
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 531 AA; 58183 MW; 3D19DBFC1ED9E9B3 CRC64;
MNTANIIFWS EVTTFPLLTT LTIVPLATVI AVLLSPSSVI ALRLGLASAV ATALLSIYMV
SIFDSGHKGI QLFEHVENIN FTYSVGLDGA NILFVLLTAI LSFLALVYLL TTRRSRDKIQ
VACILGYEGI LIGAFVAMNA MQFWFWCLLE LVPIVLITIR AGSGQKRRWV VGLLLQHWGS
GLLMTFTGFM LLAFGVMGSG DTLTFEWLVL IENKNVLEYS TLIFFLLFFG FAIRMPLFPF
HGWLPVLAEH GSVASATIFI VGLKLGIYAV IRFILPILPD VAQQWSWFVL TLGLIGIFYG
VVLALMQINI RRLLAFSVIG HTGMLIIGVF DFNLYGLESS ILLSTGFGLA AAGIALSIGM
IYKRTHTAYI PRLGGMFETS AALAFLFVIS ALSTMGMPGT PGFDGVHLLI DGTIKNHGWI
LSIAILIGNV LTAALLLRAF QQIFIATPKR LQPPYTYSAL PGSAGPSPRN ERVIAVVVCS
LLVGIGFYTT PWLQMIDQNV SAISKLHPVK YNNKHAELMI VPNHNKDNKH E
//
