ID A0A1H2SE44_9RHOB Unreviewed; 519 AA.
AC A0A1H2SE44;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=SAMN04488238_101581 {ECO:0000313|EMBL:SDW29901.1};
OS Roseicitreum antarcticum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Roseicitreum.
OX NCBI_TaxID=564137 {ECO:0000313|EMBL:SDW29901.1, ECO:0000313|Proteomes:UP000198539};
RN [1] {ECO:0000313|EMBL:SDW29901.1, ECO:0000313|Proteomes:UP000198539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8894 {ECO:0000313|EMBL:SDW29901.1,
RC ECO:0000313|Proteomes:UP000198539};
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; FNOM01000001; SDW29901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2SE44; -.
DR STRING; 564137.SAMN04488238_101581; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000198539; 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:UP000198539};
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 40..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 70..95
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 115..145
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 166..189
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 195..220
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 241..264
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 270..295
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 307..328
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 363..387
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 393..412
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 424..446
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 458..483
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT DOMAIN 73..107
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 128..346
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 519 AA; 52995 MW; BC3981F8063F6753 CRC64;
MSDLFPVTAL GPVVLLGAAA VALARPGPRP GAFPKLAEGA ALTAFALALA GLMQFLFAGP
AQLTLAQGPL ALILRADAVS ATMALLVGFI GWIVMRYARS YLDGSAREGT FHGQMLATLA
AVLVLVQAGS LLVLILAFVA VGTGVRHLLL FYPDRPAARR AATKFAWVWH AGDAALILAA
ALLLLAFGTG DLAQITAAAG AGLPIAAHIA VALVVLAAAL KTATFPLHGW LTEVMEAPTP
VSALLHAGII NAGGVLLITL SPLMQASPGA MAALVMVGGL TALFGAVVML TQSAVKTALA
WSTVSQMGFM LLQCGLGLWP LALLHIVAHS MYKAHAFLSS GGAITAVGDL RRPGPIAVPD
VAAVARAFAL ALALYGVVAL GFTLIAGSKT PQALALGGIL IFGVAYLVAQ GLADAAPVAL
MRRVGLASIG AALAYFGFQQ IAGVLWADLP AAPTAGPLEW ALIVLTVLSF GLVAVAQALF
PLWAHHPAMT GLRVHLANGL YLNAALDRLI GGFRRTRTD
//
