DABB2_HALNC
ID DABB2_HALNC Reviewed; 551 AA.
AC D0KWS8;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Probable inorganic carbon transporter subunit DabB2 {ECO:0000305|PubMed:31406332};
GN Name=dabB2 {ECO:0000303|PubMed:31406332};
GN OrderedLocusNames=Hneap_0212 {ECO:0000312|EMBL:ACX95075.1};
OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS neapolitanus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Halothiobacillaceae; Halothiobacillus.
OX NCBI_TaxID=555778;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23641 / c2;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Kerfeld C., Cannon G., Heinhort S.;
RT "Complete sequence of Halothiobacillus neapolitanus c2.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBSTRATE SPECIFICITY, AND ACTIVITY REGULATION.
RC STRAIN=DSM 15147 / CIP 104769 / NCIMB 8539 / c2 / X;
RX DOI=10.1007/BF00463489;
RA Holthuijzen Y.A., van Dissel-Emiliani F.F.M., Kuenen J.G., Konings W.N.;
RT "Energetic aspects of CO2 uptake in Thiobacillus neapolitanus.";
RL Arch. Microbiol. 147:285-290(1987).
RN [3]
RP FUNCTION, EXPRESSION IN ECOLI, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=31406332; DOI=10.1038/s41564-019-0520-8;
RA Desmarais J.J., Flamholz A.I., Blikstad C., Dugan E.J., Laughlin T.G.,
RA Oltrogge L.M., Chen A.W., Wetmore K., Diamond S., Wang J.Y., Savage D.F.;
RT "DABs are inorganic carbon pumps found throughout prokaryotic phyla.";
RL Nat. Microbiol. 4:2204-2215(2019).
CC -!- FUNCTION: Part of an energy-coupled inorganic carbon pump; its
CC substrate may be carbon dioxide. Expression of both dabA2 and dabB2
CC (DAB2) restores growth in ambient air to E.coli deleted of its carbonic
CC anhydrase genes (called CAfree, deletion of 'can' and 'cynT'); neither
CC dabA2 or dabB2 alone is sufficient. Rescue is pH-independent,
CC suggesting it transports CO(2) and not carbonate ions. Together the
CC genes allow greater than normal uptake of inorganic carbon by E.coli
CC (PubMed:31406332). Uptake of carbon dioxide rather than bicarbonate has
CC been suggested based on kinetic calculations (Probable).
CC {ECO:0000269|PubMed:31406332, ECO:0000305|Ref.2}.
CC -!- ACTIVITY REGULATION: Uptake of inorganic carbon by cells in the
CC presence of thiosulphate is fully inhibited by the uncouplers carbonyl
CC cyanide m-chlorophenyl hydrazone (CCCP), carbonyl cyanide p-
CC trifluoromethoxyphenyl hydrazone (FCCP), S13 or SF6847. Not inhibited
CC by the ATPase inhibitor N,N-dicyclohexylcarbodiimide (DCCD) (Ref.2).
CC Inorganic carbon uptake is inhibited by the ionophore carbonyl cyanide
CC m-chlorophenyl hydrazone (CCCP), suggesting uptake is coupled to a
CC cation gradient (PubMed:31406332). {ECO:0000269|PubMed:31406332,
CC ECO:0000269|Ref.2}.
CC -!- SUBUNIT: Forms a complex with DabA2, possibly a heterodimer.
CC {ECO:0000269|PubMed:31406332}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00862, ECO:0000305|PubMed:31406332}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00862}.
CC -!- DISRUPTION PHENOTYPE: Required for growth in ambient air.
CC {ECO:0000269|PubMed:31406332}.
CC -!- SIMILARITY: Belongs to the inorganic carbon transporter (TC 9.A.2) DabB
CC family. {ECO:0000255|HAMAP-Rule:MF_00862}.
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DR EMBL; CP001801; ACX95075.1; -; Genomic_DNA.
DR RefSeq; WP_012823111.1; NC_013422.1.
DR SMR; D0KWS8; -.
DR STRING; 555778.Hneap_0212; -.
DR TCDB; 9.A.2.1.2; the putative dissolved inorganic carbon concentrating transporter (dic-ct) family.
DR EnsemblBacteria; ACX95075; ACX95075; Hneap_0212.
DR KEGG; hna:Hneap_0212; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_11_1_6; -.
DR OMA; DERPNAY; -.
DR OrthoDB; 1274678at2; -.
DR Proteomes; UP000009102; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; PTHR42829; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..551
FT /note="Probable inorganic carbon transporter subunit DabB2"
FT /id="PRO_0000453157"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
SQ SEQUENCE 551 AA; 59136 MW; BE41AA5151A5B764 CRC64;
MTIEFSHTTG LLLLAMPALL LMAAVIKPKQ GAAYARAYRQ RVQWTSFAAF GLALLAVVSF
LFARQQNLML GAGSLPAGLG LLALSIQVNG LTLVLASLVS FVLSVIARYS VQYLDGDPQQ
ARFFRLLAVT GGFFLLVVIS GNLGLFTLAI IATGFGLHRL LSFYADRPRA IMATHKKSIF
SRTADALLLA ATVLIGHQIG SLEFSQISAY VHAQDHLSIA LHVAAWLIVL AAILKSAQFP
FHGWLIQVME APTPVSALMH AGVVYSGAII VLRTSELLAA DGTALLLLAL IGLMTLAIGS
LVMLTQSAIK SSLAWSTAAQ LGFMMLELGL GLFGLALLHL VGHSLYKAHA FLSSGSMTDH
LRQAKVLKNR PISVVAWFTT VIVSGLFTLG IAAAMGLSID QEPMLPAVLT IIALATAQLM
LKALSHGTWR EILVAAGAAI AMTGVYVFLH EVFITGFADT LAATPQRAPL LDLLLMAITI
ITFLFVAWLQ GPGKTLMSPE RQFALFVHLN NGLYLDRWVE RLAFRFWPEK VGRAPKKSCA
VIPPNPSGIE P
