ID A0A372EUT6_9RHOB Unreviewed; 516 AA.
AC A0A372EUT6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=DZK27_09280 {ECO:0000313|EMBL:RFP88272.1};
OS Rhodobacteraceae bacterium 63075.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2301226 {ECO:0000313|EMBL:RFP88272.1, ECO:0000313|Proteomes:UP000264392};
RN [1] {ECO:0000313|Proteomes:UP000264392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=63075 {ECO:0000313|Proteomes:UP000264392};
RA Han S.;
RT "Wenzhouxiangella salilacus sp. nov., a novel bacterium isolated from a
RT saline lake in Xinjiang Province, China.";
RL Submitted (AUG-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:RFP88272.1}.
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DR EMBL; QVMW01000008; RFP88272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372EUT6; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000264392; 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:UP000264392};
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 38..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..186
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 206..229
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 241..259
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 265..289
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 301..326
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 361..382
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 388..409
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 421..438
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 458..480
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..344
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 516 AA; 54123 MW; 8D056D32B676C9A2 CRC64;
MAHLYLPLVS PLLLLAAALL AARNPGLRPG RVPHLAEAAA FAAFVVASAS AALLVLEGPG
TSALIGLFGI GLTVQLDAVS AVMLVLVSFV GWIVLRYSRT YMDGEARQGA FTAWMSATLA
AVLFLVMSGN LFQLFAAWAL TSLSLNRLLL FYPERATARR ADRKKALIAR LSEAALAGAA
ILLFAATGTS QIETILATAE ANWMTMAAAL LIALSAVLAS AQFPLHGWLT EVMEAPTPVS
ALLHAGVINA GGFLLIRFAD VMLLAPGVMA LLVMLGGFTA LFAGLVMLTQ PAVKTSLAWS
TIAQMAFMVM QCGLALFPLA LLHIVAHSLY KAHAFLFSGE AVRNVAAIRR PGPIAVPSAR
NVLQAFVIAT IVYGLVGAIL GFDGKSVQAI ALGVILIFGV AYLFAQGFAD AAPRALMRRT
VIYALVTSVS YFALQIVAQS LTAGTLPPTP APGPLEWALI VLALVSFGCV AVAQATFPLW
ASHPAAAGLR VHLTNGLYAN AIFDKLLDGW SRRETA
//
