ID A0A365UA85_9RHOB Unreviewed; 514 AA.
AC A0A365UA85;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=DRV85_10905 {ECO:0000313|EMBL:RBI85154.1};
OS Rhodosalinus halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodosalinus.
OX NCBI_TaxID=2259333 {ECO:0000313|EMBL:RBI85154.1, ECO:0000313|Proteomes:UP000253370};
RN [1] {ECO:0000313|EMBL:RBI85154.1, ECO:0000313|Proteomes:UP000253370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E84 {ECO:0000313|EMBL:RBI85154.1,
RC ECO:0000313|Proteomes:UP000253370};
RA Liu Z.-W., Lu D.-C.;
RT "Rhodosalinus sp. strain E84T genomic sequence and assembly.";
RL Submitted (JUL-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 -!- 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}.
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:RBI85154.1}.
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DR EMBL; QNTQ01000008; RBI85154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365UA85; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000253370; 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:UP000253370};
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 35..55
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 67..89
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 109..140
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 202..219
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 239..257
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 263..284
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 305..324
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 359..380
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 386..407
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 419..436
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 456..480
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT DOMAIN 67..106
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 123..339
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 514 AA; 53396 MW; B77DFD23DE0AC58B CRC64;
MDIYTLSLLA PLALIAAAAA GFLNSGRRPE WVPQIAEGAA LVAVAVAVVS GLVLAANGPG
TGEVIGLMVR LDLLSVIMLL LVSFVGWVVL RYTRTYLDGE DRQGAFTGWM ALTLASVLVF
VQAGHLALFV VAFIATSVFL QRLLLFYPER VQAQRAAKKK FVTSRLGEAA LITAAVLLYN
GYGTAEIGEI LAAARIGVTP EAALWAAGFL ALAALLKSAQ FPTHGWLTEV METPTPVSAL
LHAGVINAGG FLLIRFADVL LLAPGVLAVL VMIGGFTAVF GGLVMLTQPA VKTSLAWSTV
AQMGFMILQC GLALFPLALL HIVAHSLYKA HAFLASGQAV DGVAAIRRPG PVAIPNGAAV
LKAFVAALAI YGVVGAGFGF ESKSPQAIAL GAILIFGVAY LLAQGLADQA PKVLTQRTAL
YSVAASIAYF ALQRGAEAAM AGTLPATPAP GPLEWALIVL AVISFGAVAV AQAMFPLWAY
HPAAAGLRVH LSNGLYANAV MDRILGGWAL RRSN
//
