DABB_HYDCU
ID DABB_HYDCU Reviewed; 518 AA.
AC Q31HC4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Probable inorganic carbon transporter subunit DabB {ECO:0000255|HAMAP-Rule:MF_00862, ECO:0000305|PubMed:28115547};
DE Short=DIC transporter subunit DabB {ECO:0000305|PubMed:28115547};
GN Name=dabB {ECO:0000255|HAMAP-Rule:MF_00862};
GN OrderedLocusNames=Tcr_0853 {ECO:0000312|EMBL:ABB41449.1};
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA Tinkham L.E., Zeruth G.T.;
RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT XCL-2.";
RL PLoS Biol. 4:1-17(2006).
RN [2]
RP ACTIVITY REGULATION.
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=26581415; DOI=10.1007/s00203-015-1172-6;
RG USF MCB4404L 2012;
RA Menning K.J., Menon B.B., Fox G., Scott K.M.;
RT "Dissolved inorganic carbon uptake in Thiomicrospira crunogena XCL-2 is
RT Deltap- and ATP-sensitive and enhances RubisCO-mediated carbon fixation.";
RL Arch. Microbiol. 198:149-159(2016).
RN [3]
RP PROTEIN SEQUENCE OF 329-344; 495-503 AND 508-518, SUBCELLULAR LOCATION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=28115547; DOI=10.1128/jb.00871-16;
RG USF MCB4404L;
RA Mangiapia M., Brown T.W., Chaput D., Haller E., Harmer T.L., Hashemy Z.,
RA Keeley R., Leonard J., Mancera P., Nicholson D., Stevens S., Wanjugi P.,
RA Zabinski T., Pan C., Scott K.M.;
RT "Proteomic and Mutant Analysis of the CO2 Concentrating Mechanism of
RT Hydrothermal Vent Chemolithoautotroph Thiomicrospira crunogena.";
RL J. Bacteriol. 199:0-0(2017).
CC -!- FUNCTION: Part of an energy-coupled inorganic carbon pump involved in
CC transport of dissolved inorganic carbon (DIC) with downstream gene dabA
CC (Tcr_0854); has been suggested to be a proton-DIC symporter.
CC {ECO:0000305|PubMed:28115547}.
CC -!- ACTIVITY REGULATION: Intracellular DIC accumulation is sensitive to
CC CCCP (carbonyl cyanide-m-chlorophenylhydrazone) and DCCD (N,N-
CC dicyclohexylcarbodiimide) and therefore likely driven by either proton
CC gradient, ATP, or both. {ECO:0000269|PubMed:26581415}.
CC -!- SUBUNIT: Forms a complex with DabA. {ECO:0000255|HAMAP-Rule:MF_00862}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00862, ECO:0000305|PubMed:28115547}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00862}.
CC -!- INDUCTION: Induced by growth in low levels of dissolved inorganic
CC carbon (DIC) (at protein level). {ECO:0000269|PubMed:28115547}.
CC -!- DISRUPTION PHENOTYPE: Cells do not grow in low DIC levels, increased
CC carboxysome content. Decreased ability to accumulate and fix DIC under
CC DIC-limiting conditions. {ECO:0000269|PubMed:28115547}.
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; CP000109; ABB41449.1; -; Genomic_DNA.
DR RefSeq; WP_011370276.1; NC_007520.2.
DR SMR; Q31HC4; -.
DR STRING; 317025.Tcr_0853; -.
DR TCDB; 9.A.2.1.1; the putative dissolved inorganic carbon concentrating transporter (dic-ct) family.
DR EnsemblBacteria; ABB41449; ABB41449; Tcr_0853.
DR KEGG; tcx:Tcr_0853; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_11_1_6; -.
DR OMA; MTRISIK; -.
DR OrthoDB; 1274678at2; -.
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; IPR046396; Transporter_DabB.
DR PANTHER; PTHR42829; PTHR42829; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..518
FT /note="Probable inorganic carbon transporter subunit DabB"
FT /id="PRO_0000453158"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 37..57
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 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00862"
SQ SEQUENCE 518 AA; 57971 MW; F5F1E23D192C181C CRC64;
MNMQWVGASM MLLIPVLFFL GSLTNERRAN WNLASAISLL GLFLSMFLGI AVYFEWVNLS
ISGQWVGVSK MSLVMLGLVC FIAFVNVRYS SAYMAGNVDE EKRYLRWLMV TLGCVVTVII
SNHMLVLMVA WIAISLSLHR LLVFFPNRQR AVLAAHKKFI FARVAEACLL GAILILYYEH
GTWFISDIYQ NVSLSTSLTT LDQFAAMLLA LAALVKCAQL PLHGWLIQVV EAPTPVSALL
HAGIINLGGY LLIIFAPLIV LSDMAQWILL IVGGITTVLA ALVMMTRTSV KVRLAWSTMS
QMGLMLVECA LGLFELALLH LVAHSCYKAY AFLNAGSEVE SSMKRRLSRA VAPSVKEWWF
AGIMSAAMVV GLIWLADLSG PYSPWLLFAI AVTLLIAERR GRLTSSSVIG MVGLGVVLLV
VYTLQKNGAS LIVSSMETSV GWKGDLWIGF LLVMFMVGYF LLRYHSEHIW MRKVRRAFYA
GFYLDEWVTR LNLRIYPTRL PVRFKPKKLQ VPKEELFQ