ID A0A1I6L4I6_9RHOB Unreviewed; 529 AA.
AC A0A1I6L4I6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Probable inorganic carbon transporter subunit DabB {ECO:0000256|HAMAP-Rule:MF_00862};
GN Name=dabB {ECO:0000256|HAMAP-Rule:MF_00862};
GN ORFNames=SAMN05444714_0173 {ECO:0000313|EMBL:SFR98369.1};
OS Yoonia litorea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=1123755 {ECO:0000313|EMBL:SFR98369.1, ECO:0000313|Proteomes:UP000198926};
RN [1] {ECO:0000313|EMBL:SFR98369.1, ECO:0000313|Proteomes:UP000198926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29433 {ECO:0000313|EMBL:SFR98369.1,
RC ECO:0000313|Proteomes:UP000198926};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- FUNCTION: Part of an energy-coupled inorganic carbon pump.
CC {ECO:0000256|HAMAP-Rule:MF_00862}.
CC -!- SUBUNIT: Forms a complex with DabA. {ECO:0000256|HAMAP-Rule:MF_00862}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00862};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00862}. 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 -!- SIMILARITY: Belongs to the inorganic carbon transporter (TC 9.A.2) DabB
CC family. {ECO:0000256|HAMAP-Rule:MF_00862}.
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DR EMBL; FOZM01000001; SFR98369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6L4I6; -.
DR STRING; 1123755.SAMN05444714_0173; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000198926; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR HAMAP; MF_00862; DabB; 1.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR InterPro; IPR046396; Transporter_DabB.
DR PANTHER; PTHR42829:SF1; INORGANIC CARBON TRANSPORTER SUBUNIT DABB-RELATED; 1.
DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00862};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00862};
KW Reference proteome {ECO:0000313|Proteomes:UP000198926};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00862};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00862};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00862}.
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 63..93
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 113..146
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 199..221
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 242..261
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 267..289
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 310..329
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 364..383
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 464..487
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT DOMAIN 66..111
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 128..347
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 529 AA; 55399 MW; B26C9370C4828C9B CRC64;
MFVNALPLLA PLLLLAAAFA PRYLDDVTPQ KNAWLAEMAS LGAVLVAVGS AFVLALGGAG
DSFLFGLFGV GLSVRLDIVS VVMLLLVSFI GWVVVRYSRT YLDGEARHDE FTFWLLVTLA
TVLTLVQSGN VVQFVAAWVA TSMFLHKLLV FYPERQAAQR AARKKYVMAR VGDISLVSAA
ALLIIAYGTT QISEILAEAS LGMGGAAAIG AAALIALSAI LKSAQFPTHG WLTEVMEAPT
PVSALLHAGV VNAGGFALIR FADLMLLSPL TLAALVMVGG FTALFGGLVM LTQPTVKASL
AWSTIAQMGF MILQCGLALF PLALLHIVAH SLYKAHAFLS AGGAVERIVA IRKPGPVAVP
DLGAVLRAFL VAIGIYGVVY AILGVGFDFG GKSPQAVALG AILIFGVAYL LAQGFADEAP
KALTQRTATY AAAVTLSYLL LQRASEWLTS GTLPATPAAG PLEWSLIILA LISFGLVAVA
QATLPLWSYH PAAQGLRVHL SNGLYINAIS DRILGGWDRT TSSDKGAAK
//
