ID A0A1H4EQG4_ALKAM Unreviewed; 499 AA.
AC A0A1H4EQG4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Multicomponent K+:H+ antiporter subunit D {ECO:0000313|EMBL:SEA87303.1};
GN ORFNames=SAMN04488051_107191 {ECO:0000313|EMBL:SEA87303.1};
OS Alkalimonas amylolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alkalimonas.
OX NCBI_TaxID=152573 {ECO:0000313|EMBL:SEA87303.1, ECO:0000313|Proteomes:UP000198773};
RN [1] {ECO:0000313|EMBL:SEA87303.1, ECO:0000313|Proteomes:UP000198773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3430 {ECO:0000313|EMBL:SEA87303.1,
RC ECO:0000313|Proteomes:UP000198773};
RA de Groot N.N.;
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}.
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; FNRM01000007; SEA87303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4EQG4; -.
DR STRING; 152573.SAMN04488051_107191; -.
DR OrthoDB; 9768329at2; -.
DR Proteomes; UP000198773; 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; PTHR42703:SF1; NA(+)_H(+) ANTIPORTER SUBUNIT D1; 1.
DR PANTHER; PTHR42703; NADH DEHYDROGENASE; 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:UP000198773};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 405..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 447..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 125..408
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 499 AA; 53630 MW; 240197BF6A4AF8DA CRC64;
MHLMILPVLI PLFAGALLTL LYGLSMRQQR ALSLLSILGQ LLVALLLMQQ ALSGDYFFYQ
LGNWQPPFGI VLVLDQLSAM MLLLLAGLAL FSTLYACVGD DRKGAHFHAL IQFQLLGLNG
AVLTGDLFNL FVFFEILLIA SYALLLHGGG RERSRAGLRY VIMNLVGSAF FLIALGVLYG
ITGTLNMADM AVKVQQLPAA DRPLIHAAAA LLLVVFGIKG ALLPLLFWLP RAYAAAAAPV
AALFAVMTKI GIYAMIRVFY LVFGGEDGIH LSLWQWLWPL ALATMVIGAI GALGARSLRG
LTAWMVIVSV GTLMAAIAEA SIPALASALL YLCHSTLLTA TFFLLADLVQ RYRPGPRDYF
VTGARVRHPV LLGALFFTAA VAFAGLPPLS GFISKVWLLS SVTSFWGYAV FWPLLLASSL
VIIVALSRAG SALLWRQSKQ EPLQAKAPAS ATSLVVCLLT LSVLFSVLAQ PLMTFATSTA
TQILTTERYL HAIPLGGGL
//
