ID A0A099TFD1_9RHOB Unreviewed; 518 AA.
AC A0A099TFD1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=PM04_02550 {ECO:0000313|EMBL:KGL02869.1};
OS Thalassobacter sp. 16PALIMAR09.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassobacter.
OX NCBI_TaxID=1225651 {ECO:0000313|EMBL:KGL02869.1, ECO:0000313|Proteomes:UP000029829};
RN [1] {ECO:0000313|EMBL:KGL02869.1, ECO:0000313|Proteomes:UP000029829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16PALIMAR09 {ECO:0000313|EMBL:KGL02869.1,
RC ECO:0000313|Proteomes:UP000029829};
RA Mas-Llado M., Nogales B., Bosch R.;
RT "Draft genome sequence of Thalassobacter sp. 16PALIMAR09.";
RL Submitted (MAR-2014) 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:KGL02869.1}.
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DR EMBL; JHAK01000001; KGL02869.1; -; Genomic_DNA.
DR RefSeq; WP_038003321.1; NZ_JHAK01000001.1.
DR AlphaFoldDB; A0A099TFD1; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000029829; 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:UP000029829};
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 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 35..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 110..129
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 175..197
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 203..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 271..293
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 305..326
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 361..383
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 421..443
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT TRANSMEM 455..481
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT DOMAIN 69..112
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 128..342
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 518 AA; 53210 MW; EBBE701F049ECD47 CRC64;
MSSVILFGLA PLILLAAGGL MFARPPARGG QSLRVVESAA LAALTVCIVG AAIVIGQGPQ
TSALLGLAEL GFSIRLDAVS LTMALLVSFI GWVVSRYART YMDGEKTQAA FMGWLGVALG
SVLLLVTAGN IVQLIVGWIG AGVAVQRLLL TYATRTGAQL AGRKKAMVNK GSNGALVLAG
VMLYAAAGTG DIATLLAEAE TTWMWTFAAI LLAISAMLAS AQVPFHGWLT EVMEAPTPVS
ALLHAGVVNA GGFLLIRFAD LILLNPVLLS ALVFLGGASA LIGSIVMLTQ PAIKTALAWS
TIAQMGFMIL QCGLGLFALA LLHIVAHSLY KAHAFLSSGG AVGAVAAIPR PGPVAVPNGR
AVLRAFGIAV VIFAAIATLF GLGGKSPQAL AMGAVLVFGV AYMLAQGLAD TAPKALTRRM
AIASLATTIG YFTLQTLAVW ITAGTLPPAP IPGALGWFLI GITVISFGLL AMAQACFPLW
VHHPAAQGLR VHISNGFYLN AVLDRMIGSW SKSDAKGA
//
