ID A3TUQ1_PSEBH Unreviewed; 954 AA.
AC A3TUQ1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=pH adaption potassium efflux system, PhaA/B subunit {ECO:0000313|EMBL:EAQ04247.1};
GN ORFNames=OB2597_08894 {ECO:0000313|EMBL:EAQ04247.1};
OS Pseudooceanicola batsensis (strain ATCC BAA-863 / DSM 15984 / KCTC 12145 /
OS HTCC2597) (Oceanicola batsensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=252305 {ECO:0000313|EMBL:EAQ04247.1, ECO:0000313|Proteomes:UP000004318};
RN [1] {ECO:0000313|EMBL:EAQ04247.1, ECO:0000313|Proteomes:UP000004318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-863 / DSM 15984 / KCTC 12145 / HTCC2597
RC {ECO:0000313|Proteomes:UP000004318};
RX PubMed=20418400; DOI=10.1128/JB.00412-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT batsensis HTCC2597(TDelta).";
RL J. Bacteriol. 192:3549-3550(2010).
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:EAQ04247.1}.
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DR EMBL; AAMO01000002; EAQ04247.1; -; Genomic_DNA.
DR AlphaFoldDB; A3TUQ1; -.
DR STRING; 252305.OB2597_08894; -.
DR eggNOG; COG1009; Bacteria.
DR eggNOG; COG2111; Bacteria.
DR HOGENOM; CLU_007100_2_0_5; -.
DR Proteomes; UP000004318; 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:UP000004318};
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..592
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 604..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 630..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 693..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..813
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 825..846
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 858..876
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 896..921
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..115
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 131..409
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..765
FT /note="MrpA C-terminal/MbhE"
FT /evidence="ECO:0000259|Pfam:PF20501"
FT DOMAIN 797..917
FT /note="Na+/H+ antiporter MnhB subunit-related protein"
FT /evidence="ECO:0000259|Pfam:PF04039"
SQ SEQUENCE 954 AA; 102480 MW; F24226AC402BD73F CRC64;
MSAEHYSLIV IALLPFAGAL MPGLMIRAGR NACAVFTALP TLLALTMLIL LAPRVMQGEV
ITAELDWIPQ LGLSASFFLD GLGLLFSCMI LGVGLLITLY ARFYLSGEDP MGQFYTYLLL
FQGAMLGIVL SDNILLLLIF WELTSLSSFL LIGYWKHLPE GRQGARMALA VTGAGGLAMI
GGMLILGNIV GSYNLTDILA AGDRIRASEW YLPALILILL GAFTKSAQFP FHFWLPHAMA
APTPVSAYLH SATMVKAGVF LMARMWPALA GTDAWFYIVT TAGLITMVLG ALIALFKDDL
KALLAFSTVS HLGLLTMLLG FGTPVAALVA VFHIINHLTF KAALFMTAGI IDHEAHTRDI
KRLGGLRTLM PVTFVIGTLA ALSMAGIPLL NGFLSKEMML EEASHTDWAG SHYAVPVLAT
LGALLSVAYS FRFVAHVFLG PVRDDYPHKP HDPPFGMWAA PALLVVLVVL IGVLPHLAEP
VVMMAAGAVT GGVLPDIHLK IWHGITPALF MSGIAILGGL VLLALHRPLD RAWIATPRPE
AKAIFDRLVG GAVSLSGRIA GGSHDGAMSR YLAIFVAATL ALGYIAFSGS GLPAPTRDLL
PVPPVVLVGW VMLLVATGTV VLVHRDRFRA LVIIGVIGLT ISFGFVYLSA PDLALTQISV
ETVTIMLLLL ALHYMPKASP VESTAGRRIR DGIIALGAGG GVGALAWMFL LRDTASISDY
HLANSYKGGG GTNVVNVILV DFRGYDTYGE IIVLGIAGLI IYAVMDALLN GPAARKLRNT
DYSRDRSRDR HPLMTVIATR VMMPIALMVG VFIFLRGHNE PGGGFVAGLV VSIALLMQYM
ASGFAWTQSR QRIEYHSMIG WGVLIAGLTG AGAWLGGKPF LTSGYDYYHF PPIEEFELAT
AMLFDLGVFL AVLGAVMLML YSLSRIARYA GETVNPEPMD YDPSTRIRAL REEE
//
