ID A0A2M8N4C2_9RHOB Unreviewed; 962 AA.
AC A0A2M8N4C2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Monovalent cation/H+ antiporter subunit A {ECO:0000313|EMBL:PJF11291.1};
GN ORFNames=CUR21_01450 {ECO:0000313|EMBL:PJF11291.1};
OS Pseudorhodobacter sp. MZDSW-24AT.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudorhodobacter.
OX NCBI_TaxID=2052957 {ECO:0000313|EMBL:PJF11291.1, ECO:0000313|Proteomes:UP000230388};
RN [1] {ECO:0000313|EMBL:PJF11291.1, ECO:0000313|Proteomes:UP000230388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZDSW-24AT {ECO:0000313|EMBL:PJF11291.1,
RC ECO:0000313|Proteomes:UP000230388};
RA Mayilraj S.;
RT "Pseudorhodobacter sp. nov., strain MZDSW-24AT genome sequence and
RT assembly.";
RL Submitted (NOV-2017) 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:PJF11291.1}.
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DR EMBL; PGOI01000001; PJF11291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8N4C2; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000230388; 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:UP000230388};
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 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 506..527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 580..599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 611..630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 702..723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 761..779
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 812..830
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 836..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..896
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 916..939
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..114
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 130..407
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 620..684
FT /note="MrpA C-terminal/MbhD"
FT /evidence="ECO:0000259|Pfam:PF13244"
FT DOMAIN 699..793
FT /note="MrpA C-terminal/MbhE"
FT /evidence="ECO:0000259|Pfam:PF20501"
FT DOMAIN 810..932
FT /note="Na+/H+ antiporter MnhB subunit-related protein"
FT /evidence="ECO:0000259|Pfam:PF04039"
SQ SEQUENCE 962 AA; 103014 MW; 9D3B34AB501D698B CRC64;
MIEENLLLIL VGLPFAAALA ASTVPTTAHS AAAWVSGGLL AMGLAILAVL HAPIAEGEVL
RSTLAWVPSL GLTLTFRMDG FVWLFASLVF GIGILVLIYA RYYLSKSDPV PRFYAFLMAF
TGAMLGVLLS GNILMLVVFW ELTSILSFLL IGYWHQGQAA RDGARMALIV TGLGGLGLLL
GMVLLGQIVG SYDLDRVLAS GDVVRAHPLY PLVLALFLLG CFTKSAQMPF HFWLPGAMAA
PTPVSAFLHS ATMVKAGVFL LVRFSPVLGQ TELWFFAVTG TGMLTLVLGS VIALFRHDLK
GLLAYSTISH LGLITALAGI GSNGAILAAI FHIVNHAVFK ASLFMAAGIL DHETGTRDMR
RLSGLIRFMP VTGSLAIVAS AAMAGVPLLN GFISKEMFFA EAADWHNGTW LDNALPYLAT
LAGVFAVAYS LRFIATVFFG PPATDLPKSP HEPPAWMRRP VELLVLVCLL VGIAPGLTLG
PVLNLAAQAV LGPDLPYKAI HVWHGFNLPL GMSLIALGAG VALYALAGGR VSQGPEGPPL
LHRLRAQRVF ERLLLLFTWK LPRQLHRFIG TERLQPQLRL ILLLALAAGL ATLWGGLRVS
PSPLETPLNP AFAAMWLVGA VCAIGAATLA KYHRFASVVL LGGAGAVTCL TFAWLSAPDL
AVTQLLVEIV TTVLLLLGLR WMPKRREEIA EDKLRPARIR RLRDFIIAVV AGAGLAAISY
VVMTSPLIPN VGDWFLRNAY AEGGGTNVVN VILVDFRAFD TFGEITVLAI VGVTVFALLR
RFRPSAESVA LAEAAARLED TSLAHALRVP AVIMRWMFPV MMVLAAYLFF RGHDLPGGGF
SAGVTMSIAF LLQYLAHDVR WIEDRLTILP IRWMGIGLVI AGLTGMGAFV FGYPFLTAHA
QYITLPLIGK VPAATALLFD AGVFALVVGA TVLMLIAIAH QSLRVARLRD RDSGGQAETE
GA
//
