ID A0A3P3D988_9RHOB Unreviewed; 737 AA.
AC A0A3P3D988;
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=DUF4040 domain-containing protein {ECO:0000313|EMBL:RRH70166.1};
GN ORFNames=EG244_17380 {ECO:0000313|EMBL:RRH70166.1};
OS Falsigemmobacter faecalis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Falsigemmobacter.
OX NCBI_TaxID=2488730 {ECO:0000313|EMBL:RRH70166.1, ECO:0000313|Proteomes:UP000282125};
RN [1] {ECO:0000313|EMBL:RRH70166.1, ECO:0000313|Proteomes:UP000282125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 102744-1 {ECO:0000313|EMBL:RRH70166.1,
RC ECO:0000313|Proteomes:UP000282125};
RA Li G., Jiang Y.;
RT "Gemmobacter sp. nov., YIM 102744-1 draft genome.";
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}.
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:RRH70166.1}.
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DR EMBL; RRAZ01000036; RRH70166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P3D988; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000282125; 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; 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; 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 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 50..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 536..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 563..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 591..612
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 650..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..727
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..84
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 100..383
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 575..638
FT /note="MrpA C-terminal/MbhD"
FT /evidence="ECO:0000259|Pfam:PF13244"
FT DOMAIN 648..733
FT /note="MrpA C-terminal/MbhE"
FT /evidence="ECO:0000259|Pfam:PF20501"
SQ SEQUENCE 737 AA; 78100 MW; 466929B2BB6058E7 CRC64;
MWSLLPALFA ASLFGALLLA LPAVLAGGTV QFGWDWLPAL GIRLSFLIDG LSLTFALLIS
GIGSAVLLYA SSYLAGHPHY LRFFLFLTSF MLSMLGLVLA ADLIALFVFW ELTSVTSYLL
IGFVHDDPRA RRNALQAMLV TGAGGLALLA GFILIGVAGG TWDLAELLAG EGLQAHPLYS
GILVLILLGA FTKSAQFPFH FWLPNAMSAP TPVSAYLHSA TMVKAGIYLL ARLHPTLSGT
AAWEVTLTCA GLMTAVMASL LAIRQTDLKT ALAYTTLMAL GTITLFLAGD TPYALTAAVT
FLIVHSLYKA ALFMVVGNID HGTGTRDAES LGGLARKMPL TAVAAGLAAL SMAGLPPFLG
WMGKELLYAG AQDLSPAALI TGGVLIANAL MFAVAAIVAL APFYGPLKRT PHAPHEADWR
MLAGPLLLGA LGLLAGLLAS GVQPLVDQTV TGSFAQSKAA GLHLWAGFNL PLLLSALTFL
LGTVFYLNRS RLRLVLGALL ERLPVFDRSW DRLLDRFRGF AGWQAELIQT GKLSHYLTVT
FAVVGAVLLA TVVLRLPQVR FDLSAPVVMW IIAAAIAGGA IFTLNPHSRL ANIAGIGTVG
IGVALVFILF GAPDVATTQL MVETLSAVLF GIAMLRLPGI RERRSGRRQL VHGAIAVSVG
LSVTLIILAI AAHPLDRNLT TFFEENSYLL AHGLNIVNVI LVDFRAFDTF GELTVVLLAS
IGAYALLKRR LPRGEAD
//
