ID A0A0S4L6G3_9BACT Unreviewed; 432 AA.
AC A0A0S4L6G3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative NADH-quinone oxidoreductase, subunit M {ECO:0000313|EMBL:CUS33315.1};
DE EC=1.6.5.11 {ECO:0000313|EMBL:CUS33315.1};
GN ORFNames=COMA1_11090 {ECO:0000313|EMBL:CUS33315.1};
OS Candidatus Nitrospira nitrosa.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1742972 {ECO:0000313|EMBL:CUS33315.1, ECO:0000313|Proteomes:UP000199032};
RN [1] {ECO:0000313|EMBL:CUS33315.1, ECO:0000313|Proteomes:UP000199032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COMA1 {ECO:0000313|EMBL:CUS33315.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU000320}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU000320}.
CC -!- SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit D
CC family. {ECO:0000256|ARBA:ARBA00005346}.
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DR EMBL; CZQA01000001; CUS33315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4L6G3; -.
DR STRING; 1742972.COMA1_11090; -.
DR OrthoDB; 9792095at2; -.
DR Proteomes; UP000199032; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR42703:SF1; NA(+)_H(+) ANTIPORTER SUBUNIT D1; 1.
DR PANTHER; PTHR42703; NADH DEHYDROGENASE; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:CUS33315.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199032};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 156..341
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 432 AA; 46445 MW; 237D9234B9411DF1 CRC64;
MTSAVLFSWL ATCIPLIGAL AGRLLWEDVP QLKKSCIIWS LITVAPILKL KTNLPEGALL
LGLLPVVAMI SILGQPVQKD HRLSWLMTLI CLGLGIGVIA HPAPLSQLFL LALLVTMAGL
LMRYHTILWP ISWWGISLFY LTALGVVVTL TNPSLSSFGA LMTAAVLIPL LPFHIGYLTA
LTRLPGNLPS FSAFLLPAVG LHVMASALQT VPTAVTGIVG LLALIGGLYG AVKALAQTRI
RLMLSYSSLS FFSMLWWHTA ASSLATSRAA VFVASIGLAT CGLLIAWQII RTRYGDDVDP
SSISGLASSM PRYAVLLSLL ALAAMGLPPF GVFAGLMGLL LHSPIPSLIG LMIMLSAWLA
ASWYLLSAVQ RLLFGTRRGD LRYRDVVQQE WAALTMTIVI LTVLGLAPIE WWTSTATQSM
AGTFSRAIPW HQ
//
