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Database: UniProt
Entry: I0HQW8_RUBGI
LinkDB: I0HQW8_RUBGI
Original site: I0HQW8_RUBGI 
ID   I0HQW8_RUBGI            Unreviewed;       507 AA.
AC   I0HQW8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
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   OrderedLocusNames=RGE_20640 {ECO:0000313|EMBL:BAL95405.1};
OS   Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Rubrivivax.
OX   NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL95405.1, ECO:0000313|Proteomes:UP000007883};
RN   [1] {ECO:0000313|EMBL:BAL95405.1, ECO:0000313|Proteomes:UP000007883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX   PubMed=22689232; DOI=10.1128/JB.00511-12;
RA   Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA   Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA   Shimada K., Hanada S., Nagashima K.V.P.;
RT   "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT   gelatinosus IL144.";
RL   J. Bacteriol. 194:3541-3542(2012).
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 inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00862}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00862}. Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, 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; AP012320; BAL95405.1; -; Genomic_DNA.
DR   RefSeq; WP_014428268.1; NC_017075.1.
DR   AlphaFoldDB; I0HQW8; -.
DR   STRING; 983917.RGE_20640; -.
DR   KEGG; rge:RGE_20640; -.
DR   PATRIC; fig|983917.3.peg.1993; -.
DR   eggNOG; COG1009; Bacteria.
DR   HOGENOM; CLU_007100_11_1_4; -.
DR   Proteomes; UP000007883; Chromosome.
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; 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   PRINTS; PR01434; NADHDHGNASE5.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00862};
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:UP000007883};
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..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT   TRANSMEM        38..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT   TRANSMEM        67..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT   TRANSMEM        103..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT   TRANSMEM        126..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT   TRANSMEM        168..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT   TRANSMEM        238..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT   TRANSMEM        268..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT   TRANSMEM        302..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT   TRANSMEM        356..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT   TRANSMEM        384..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00862"
FT   DOMAIN          122..346
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
SQ   SEQUENCE   507 AA;  52847 MW;  4A26C38B987B70B2 CRC64;
     MDLPPLLPAA VALLPALAMF AVALLAPRAD APVAWRRWHW ASGTALLAAL ASLVLQLAGV
     ATAPLPGLAA TLTGAWVALL VQGLATVIGG FSSRYLDGEA GQPCFVAALG GVLAAVHLLL
     LADHWLVLIA AWAAVGVVLQ RLLCFYPERP FALLAAHKKR LADRLADVLL VVAAALAWHE
     VGSGSFGYLW RHLEAGPPSP ALQAAALCLA AAVVLRTALL PVHGWLMQVM EAPTPVSALL
     HAGVVNLGGV VLIRFAPLLE TVPAARWLLV GLGLATALLA GLVMLTRVSI KLRLAWSTAA
     QMGFMVMECG LGLYTLALLH LLGHSLYKAH AFLSASGAVA QARARDMRPP APPSAASLLA
     APVLAAPVLA AAALLPVAGV AWPWWWSALL ALAWAPMLWW PATRATDATG ALRRVLAGLA
     MVALLGAAAL AGHALPFGVH DAPDDSAGPV ALAAMALLYA GLALLQARPQ ALAGWRRWSY
     AGFYVDEYAT RAALRLWPTR WTPASTD
//
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