ID   DABA_HALWD              Reviewed;         931 AA.
AC   Q18H12;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Probable inorganic carbon transporter subunit DabA {ECO:0000255|HAMAP-Rule:MF_01871};
GN   Name=dabA {ECO:0000255|HAMAP-Rule:MF_01871}; OrderedLocusNames=HQ_2622A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
CC   -!- FUNCTION: Part of an energy-coupled inorganic carbon pump.
CC       {ECO:0000255|HAMAP-Rule:MF_01871}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01871};
CC   -!- SUBUNIT: Forms a complex with DabB. {ECO:0000255|HAMAP-Rule:MF_01871}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01871};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01871}.
CC   -!- SIMILARITY: Belongs to the inorganic carbon transporter (TC 9.A.2) DabA
CC       family. {ECO:0000255|HAMAP-Rule:MF_01871}.
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DR   EMBL; AM180088; CAJ52733.1; -; Genomic_DNA.
DR   RefSeq; WP_011571849.1; NC_008212.1.
DR   AlphaFoldDB; Q18H12; -.
DR   STRING; 362976.HQ_2622A; -.
DR   EnsemblBacteria; CAJ52733; CAJ52733; HQ_2622A.
DR   GeneID; 4193044; -.
DR   KEGG; hwa:HQ_2622A; -.
DR   eggNOG; arCOG04520; Archaea.
DR   HOGENOM; CLU_009885_0_0_2; -.
DR   OMA; DCDLEGR; -.
DR   Proteomes; UP000001975; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01871; DabA; 1.
DR   InterPro; IPR018752; DabA.
DR   PANTHER; PTHR38344; PTHR38344; 3.
DR   Pfam; PF10070; MpsB; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Metal-binding; Reference proteome; Transport;
KW   Zinc.
FT   CHAIN           1..931
FT                   /note="Probable inorganic carbon transporter subunit DabA"
FT                   /id="PRO_0000387331"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..380
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         399
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01871"
FT   BINDING         401
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01871"
FT   BINDING         604
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01871"
FT   BINDING         619
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01871"
SQ   SEQUENCE   931 AA;  102008 MW;  65C31C36E1572B4A CRC64;
     MTTESTSESK TKTETETETE TEQRNDLSNS SNSSEDASCP GSSPVSTESD PDNDDTSVSA
     NTIVRQYIES AAESVGALWP IHSFVTANPL SGFEDQPFHK AVAAGATRFG GDGYPDSDVF
     EHAWKTGQIN QEILKKTLDE YETDHTPASA IAAIDSGTQA TSGRDTGVRM GTGVDDEINN
     WDEIDKRVIK WLSAFLDAGS AEWEMPNRGS GFYTAFQSVA TYDTMIPDTD LIEDPPADPI
     DAVSTVLASY PRSQWSEIIE AQITALPGWT GLICYRTENE TAWQTAYPIT LVGYLAARMM
     LADALSIPLD SISRPAHSVT STEESTADIE TYPLQEIILI AWERTYREEL IEQIADTADN
     HKHEHDHDHD ADKTIGDDVE PQADSRSSSV RPDAQLVFCI DTRSEIIRRH IESTGQYETY
     GYAGFFGIPM RYRGYDDAVS IDACPPIVDA QHRISESAKH ADENKTPNGQ YNSRYERIRD
     IYDAGIDIVD SLASNVTTAF NFVETTGSGY GVGLALRTLF PQRVYDILTR IENRLPRIDV
     ISQPQLNTAT GEVNQYSHNE TDGSHSEDVL PYGLTHQERV EYAASAFELM GLKTFGRVVG
     FIGHASQTAN NPFGSSLDCG ACAGNAGGPS ARVLAQICND DAVKTSLRDR GIDIPVDTVF
     IAGEHTTTTD KITLYTEAIP DSHQDDIRSL QADLSIAQED AAAERLESLS GDTTVDAIQD
     IERRAADWAE TRPEWGLAGN AGFVIGPRRL TDDVDLEGRV FLHSYDWQQD ETGSALESIL
     TGPLIVTQWI NAQYYFATVD TAVYGSGSKV TQNPVGNVGI YQGNGGDLMR GLPVQSVRKS
     TDNLYHQPIR LSTVVHAPVS KVTHALADLE SVTELLDNNW ISLTVIDPTR ENDAFHYVKG
     LKWLPHGEGY KHDATECISP QINQTVSSSS D