ID A0A372I9A8_9RHOB Unreviewed; 954 AA.
AC A0A372I9A8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Monovalent cation/H+ antiporter subunit A {ECO:0000313|EMBL:RFU11512.1};
GN ORFNames=DZD18_16690 {ECO:0000313|EMBL:RFU11512.1};
OS Rhodobacteraceae bacterium W635.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2303578 {ECO:0000313|EMBL:RFU11512.1, ECO:0000313|Proteomes:UP000264655};
RN [1] {ECO:0000313|EMBL:RFU11512.1, ECO:0000313|Proteomes:UP000264655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W635 {ECO:0000313|EMBL:RFU11512.1,
RC ECO:0000313|Proteomes:UP000264655};
RA Hou X.J.;
RT "Ayaqqumibacter halotolerans gen. nov., sp. nov., isolated from a saline
RT lake in Xinjiang province, China.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient. {ECO:0000256|ARBA:ARBA00002378}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU000320}.
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:RFU11512.1}.
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DR EMBL; QVQC01000083; RFU11512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372I9A8; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000264655; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR007182; MnhB.
DR InterPro; IPR025383; MrpA_C/MbhD.
DR InterPro; IPR046806; MrpA_C/MbhE.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR001516; Proton_antipo_N.
DR PANTHER; PTHR43373:SF1; ANTIPORTER SUBUNIT MNHA2-RELATED; 1.
DR PANTHER; PTHR43373; NA(+)/H(+) ANTIPORTER SUBUNIT; 1.
DR Pfam; PF13244; MbhD; 1.
DR Pfam; PF20501; MbhE; 1.
DR Pfam; PF04039; MnhB; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
PE 4: Predicted;
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000264655};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 33..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 413..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 501..525
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 571..590
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 602..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 654..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 692..710
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 751..771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 792..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 821..841
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 853..876
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 896..920
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..115
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 131..408
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 613..677
FT /note="MrpA C-terminal/MbhD"
FT /evidence="ECO:0000259|Pfam:PF13244"
FT DOMAIN 687..766
FT /note="MrpA C-terminal/MbhE"
FT /evidence="ECO:0000259|Pfam:PF20501"
FT DOMAIN 796..917
FT /note="Na+/H+ antiporter MnhB subunit-related protein"
FT /evidence="ECO:0000259|Pfam:PF04039"
SQ SEQUENCE 954 AA; 101921 MW; 8AFE3A8F3F3732BC CRC64;
MDLIDHSLIV IALLPFAGAL VPGLMIRAGR NACAVFTALP TALALTMLLL LAPSVMAGDV
ITAELRWLPQ LGLSAAFFLD GLGLLFAAMI LGVGLLITLY ARFYLSGEDP MGQFYTYLLL
FQGAMLGIVL SDNILLLLVF WELTSLSSFL LIGYWKHLPE GRQGARMALA VTGAGGLAMI
GGMLILGNIV GSYNLTDILA AGDQIRASEW YLPALILILL GAFTKSAQFP FHFWLPHAMA
APTPVSAYLH SATMVKAGVF LMARMWPALS GTDAWFYIVS SVGLITMVIG ALIALFKDDL
KALLAFSTVS HLGLLTMLLG FGTPIAAVVA VFHIINHLTF KAALFMTAGI VDHEAHTRDI
KRLGGLRHLM PVTFVIGTLA ALSMAGIPLL NGFISKEMML EEAAHTGWAG SPYAVPVLAT
LGALLSVAYS FRFIAHVFLG PVRDDYPAKP HDPPFGMWAA PALLVGLVVL IGVLPHLAEP
LVRTAAGAVT GSDLPYFSLK IWHGVTPALF MSGIAVIGGA ALLAIHAPLD RVWAALPRPE
AKVIFDRLVA GVVGLSRRIT ERSHDGAMSR YLAIFVVATT VLGAIAWRGG GVPAATRELL
PIPPVVLVGW VLLLGATGAI VLLHRQRFIA LVVIGVIGLM ISVGFVYLSA PDLALTQISV
ETVTIMLLLL ALHYLPKTSP VESGVARRLR DGVIAVAAGG GVGALAYTFL LRDTATISQY
HLDNSYSGGG GTNVVNVILV DFRGYDTYGE IIVLGIAGLV IYAVMHALLN GPAARKLRNS
DYTSTLSRDR HPLMVVIATR VMMPVAVMVG IYIFLRGHNQ PGGGFVAGLV VSIALLMQYM
ASGYAWTQQR QRIEYHVLIG WGVVIAGLTG VGSWLAGRPF LTSAFDYYHF PPIEEFELAT
AMLFDIGVLL AVLGAVMLML ESLSRIARYA GETVNPEPMD YDPSQRPVAA KEES
//
