ID A0A368Z3J1_9RHOB Unreviewed; 947 AA.
AC A0A368Z3J1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Multisubunit potassium/proton antiporter PhaA subunit /multisubunit potassium/proton antiporter PhaB subunit {ECO:0000313|EMBL:RCW85014.1};
GN ORFNames=DFP89_10632 {ECO:0000313|EMBL:RCW85014.1};
OS Paracoccus lutimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1490030 {ECO:0000313|EMBL:RCW85014.1, ECO:0000313|Proteomes:UP000253345};
RN [1] {ECO:0000313|EMBL:RCW85014.1, ECO:0000313|Proteomes:UP000253345}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8525 {ECO:0000313|EMBL:RCW85014.1,
RC ECO:0000313|Proteomes:UP000253345};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-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:RCW85014.1}.
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DR EMBL; QPJL01000006; RCW85014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368Z3J1; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000253345; 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:UP000253345};
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..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 495..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 566..587
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 599..618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 625..643
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 649..667
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 687..705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 748..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 791..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 818..838
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 850..875
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 895..917
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..105
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 126..408
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 607..672
FT /note="MrpA C-terminal/MbhD"
FT /evidence="ECO:0000259|Pfam:PF13244"
FT DOMAIN 682..762
FT /note="MrpA C-terminal/MbhE"
FT /evidence="ECO:0000259|Pfam:PF20501"
FT DOMAIN 792..914
FT /note="Na+/H+ antiporter MnhB subunit-related protein"
FT /evidence="ECO:0000259|Pfam:PF04039"
SQ SEQUENCE 947 AA; 102049 MW; B132F5F5859F3D78 CRC64;
MSPALIAVLP FIGALLPGLL IRSGRDVAAI SCGAATFIAL LGLCLHIPAI MAGEVITSRI
EWLPSLGLNA NFRIDGLGLL FGILILGIGL LIITYARYYL SRNDPVGVFY TYLMLFQGAM
MGIVLSDNIL LLLVFWELTS LSSFLLIGYW KHLPEGRQGA RMALTVTGMG GLAMIAGMLI
LGSIAGSYEI SDILLAREAI QASPLYLPAL ILILIGAFTK SAQFPFHFWL PHAMAAPTPV
SAYLHSATMV KAGLFLMARL WPVLSGTPEW FYIVATTGLV TMVMAAWIGM FRDDLKSLLA
FSTVSHLGLI TMLLGFGTEA AAVAAVFHII NHATFKAALF MTAGIIDHEA GTRSIRRLGG
LRKLMPITFI IGTIAALSMA GVAPLNGFLS KELMLEEASH MVWMGHPALI VTMATIGACF
SVCYSLRFIW QVFFGPERHD YPHHPHDPGF GMWVGPALLV VLVVLIGLFP NQMAGWLVEA
SASAVTGAHP HPHFALWHGL TLALKLSVTA LLVGVVLLNL NHRMIALRDM VWRPDGKRSF
DAITRACTCV AAWITPRLTN GSMSRALAAL SLTIVLCGLW AFSTGGYQGA TRPMLEITAV
PFIGWLLLIV ATACMVMFHR LRIMALVLVG IIGLIVSCSF LYLSAPDLAL TQISVEVVTV
ILLLLALNFL PKYTVLDSRD RKRGMDAFVA TVSGLGFGAL AYIIMRSDFA FPSIAGYMLE
NSHKLGGGDN VVNVILVDFR GYDTFGEITV LGIAALTIFA LTETLLMGSS GKRLRNWVHD
SLRAGDRHPQ MLVVATRLIL PISLVVGLYI FLRGHNQPGG GFIAGLVVAI ALVSQYMASG
YAWAQERQKI NYHALIGAGV IAAGITGIGA WFAGLPFLTS TYGYVKLPGL EKFELASAMG
FDLGVFLCVV GAVMLALNSL SRIARQAGET VNLHPMDIDP SKEAERP
//
