ID A0A0D6TFN2_9RHOB Unreviewed; 965 AA.
AC A0A0D6TFN2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Monovalent cation/H+ antiporter subunit A {ECO:0008006|Google:ProtNLM};
GN ORFNames=SY26_09330 {ECO:0000313|EMBL:KIX18617.1};
OS Paracoccus sp. 228.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1192054 {ECO:0000313|EMBL:KIX18617.1, ECO:0000313|Proteomes:UP000032743};
RN [1] {ECO:0000313|EMBL:KIX18617.1, ECO:0000313|Proteomes:UP000032743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=361 {ECO:0000313|EMBL:KIX18617.1,
RC ECO:0000313|Proteomes:UP000032743};
RA Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA Madanecki P., Markert S., Piotrowski A., Schweder T., Szalewska-Palasz A.;
RT "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT Genomic and a Proteomic Perspective.";
RL Submitted (FEB-2015) 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:KIX18617.1}.
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DR EMBL; JYGY01000002; KIX18617.1; -; Genomic_DNA.
DR RefSeq; WP_046000367.1; NZ_JYGY01000002.1.
DR AlphaFoldDB; A0A0D6TFN2; -.
DR STRING; 1192054.SY26_09330; -.
DR PATRIC; fig|1603292.4.peg.1932; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000032743; 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:UP000032743};
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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 458..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 614..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 664..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 707..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 764..782
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 809..832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 838..858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 879..899
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 919..942
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..117
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 133..410
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 624..687
FT /note="MrpA C-terminal/MbhD"
FT /evidence="ECO:0000259|Pfam:PF13244"
FT DOMAIN 703..799
FT /note="MrpA C-terminal/MbhE"
FT /evidence="ECO:0000259|Pfam:PF20501"
FT DOMAIN 813..935
FT /note="Na+/H+ antiporter MnhB subunit-related protein"
FT /evidence="ECO:0000259|Pfam:PF04039"
SQ SEQUENCE 965 AA; 102823 MW; F05DC6C2BEBE8D78 CRC64;
MITPTALAQQ NLLVLLAVLP FLSALLLISV SGRAAGILAG ITMLAGIALS AGLGGPVMSG
EVLRASLDWV PSAGLSLSLR MDGFAWMFAT LVSTIGLLVV VYAQVYMAGK ERPPRFFALL
MAFTGAMQGI LLSGNLLMLV VFWELTSVVS FLLIGFWHQG QSARDGARTA LLITAMGGLC
LLLAMLMLGH VVGSHDLDVV LAAGPQVREH PMYGAILALF LLGAFTKSAQ VPFHFWLPGA
MSAPTPVSAF LHSATMVKAG VFLLIHFSPV LGGTEAWFLA VTGIGMATFL TGGVIALFRH
DLKGLLAYST ISHLGLITAL AGIGSQGAIL AAIFHICNHA VFKASLFMTA GIIDHQTGTR
DLRKLGGLAR VMPFTATLAI IASAAMAGVP LLNGFLSKEM FLAEAVAWHN GSWLDDSLPY
LAVVASAFSA AYAIRFIASV FFGPLPDALR GRVSEAPVLL RLPVSLLAAA CLAVGILPAP
VIGPVINRAA RAVLGPDLPY YDIAIWHGVN AALMLSLVSL GVGTLIYAMT RTRIPLGPEG
PPLLHRLRGQ RVFDRLMLKG AWVLPRRVLG RLATERLQPQ LRLLVAVALF LAVAAIGARF
PWAPPARVTD FSPAFALMWL IGGACAVGAA WQAKYHRFAA LAMLGGAGLV TCLTFAWLSA
PDLAVTQLLV EVVTTVLLLL GLRWLPQRRA GLPEDNLASA RRRRMRDLVM AVAGGSGIAL
VAHSVMTRPL VPNVGDWFLA NAYYEGGGTN VVNVILVDFR AFDTFGEIAV LAIVGLTVYS
LLRRFRPAPE SVDQPNQQQA TSQQALDDYL MVPSVIMLWM FPVLIMVAAY FFFRGHDLPG
GGFAAGVTMA IAFLLQYLAT NVRWVEARLT ILPIRWMGIG LLIAVGTGMG SWIFGYPFLS
AHARYVSIPL IGNVPAATAL LFDLGVFALV VGATVLMLIA IAHQSLRAAR LREQDDATPA
TKEIR
//
