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Database: UniProt
Entry: A0A3P5X5H1_9RHOB
LinkDB: A0A3P5X5H1_9RHOB
Original site: A0A3P5X5H1_9RHOB 
ID   A0A3P5X5H1_9RHOB        Unreviewed;       966 AA.
AC   A0A3P5X5H1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Na(+)/H(+) antiporter subunit A {ECO:0000313|EMBL:VDC23439.1};
GN   Name=mrpA_1 {ECO:0000313|EMBL:VDC23439.1};
GN   ORFNames=XINFAN_01045 {ECO:0000313|EMBL:VDC23439.1};
OS   Pseudogemmobacter humi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudogemmobacter.
OX   NCBI_TaxID=2483812 {ECO:0000313|EMBL:VDC23439.1, ECO:0000313|Proteomes:UP000277498};
RN   [1] {ECO:0000313|EMBL:VDC23439.1, ECO:0000313|Proteomes:UP000277498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACIP111625 {ECO:0000313|EMBL:VDC23439.1};
RA   Criscuolo A.;
RL   Submitted (NOV-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}.
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DR   EMBL; UXAW01000048; VDC23439.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P5X5H1; -.
DR   OrthoDB; 9811798at2; -.
DR   Proteomes; UP000277498; 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:UP000277498};
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..234
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..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        413..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        463..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        578..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        609..628
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..682
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        842..861
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        873..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          70..114
FT                   /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00662"
FT   DOMAIN          130..408
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
FT   DOMAIN          621..684
FT                   /note="MrpA C-terminal/MbhD"
FT                   /evidence="ECO:0000259|Pfam:PF13244"
FT   DOMAIN          699..796
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   966 AA;  104983 MW;  EB7CAB6B11DD1E82 CRC64;
     MIEQNLILIL VLLPFLGAIL AATLPVNAHN AAAWVSGLSL GAGLLLLAVL YPRIAEDEVV
     RGVVRWLPIL SLNLNFRMDG FAWLFTGLVL SIGVLVVIYA RYYLSKTDPV PRFYSFLMAF
     TGAMIGMLLS GNILMLVVFW ELTSILSFLL IGYWHQSQAA RDGARMALIV TAGGGVALTV
     AMIVLGQIVG GYDLDLVLRS GEIIRAHPLY PVVLGLFLLG AFTKSAQFPF HFWLPGAMAA
     PTPVSAYLHS ATMVKMGVFL LIRFQPALGG TELWFYTVTG TGVITLTVGA MIALFRHDLK
     GLLAYSTISH LGLITALAGM SSTGAIVAAI FHICNHAVFK ASLFMAAGII DHETGTRDLR
     RLSGLMKAMP ITGALAIVAS AAMAGVPLLN GFLSKEMFFA EAVGWHNGTW LDSALPWIAT
     FASIFSVAYS LRFIMQVFFG PEATDLPKAP HEPPPWMRRP VEFLVLTCLA VGILPALTLE
     PVLNIAGRSV LGPDLPEIHI AIWHGFNTPL IMSIIAMTAG IVLYFAFARR IDAGPEGPPI
     LWRIRAQKIY EWLLLRLSWA WPRFLHKLFG TERLQPQLRL MMLIGLVAAM IAVWGGLTVA
     EKPLTNDLSP AFAIMWLVGG ACAIGAAWQA KYHRFAALVL LGGAGLVTCV TFAWFSAPDL
     AVTQLVVEIV TTVLLLLGLR WLPKRREEIP GDELLSARIR RLRDLGIATV GGLGLAGLAY
     VVMTRPLVPN IGDWFLRNAY YEGGGTNTVN VILVDFRAFD TFGEITVLAI VGLTVYALLR
     RFRPGAESIA LPEQQQGDTA DRLGNYMLVP ATIMRWMFPV TLVIAAYLFF RGHDLPGGGF
     SAGVTVAIGL LLQYIAANVR WIEARIVILP IRWMGFGLLI AAATGIGAWL FGYPFLTAHA
     RYVDVPLVGK VPMATAMAFD LGVFLAVVGA TVLLLIAIAH QSLRSARLRE LEEEKTPEKS
     AQKEAV
//
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