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DABA2_HALNC
ID   DABA2_HALNC             Reviewed;         827 AA.
AC   D0KWS7;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Probable inorganic carbon transporter subunit DabA2 {ECO:0000255|HAMAP-Rule:MF_01871, ECO:0000303|PubMed:31406332};
GN   Name=dabA2 {ECO:0000255|HAMAP-Rule:MF_01871, ECO:0000303|PubMed:31406332};
GN   OrderedLocusNames=Hneap_0211 {ECO:0000312|EMBL:ACX95074.1};
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, COFACTOR, SUBUNIT,
RP   SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-351;
RP   ASP-353; HIS-524 AND CYS-539.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01871,
CC         ECO:0000269|PubMed:31406332};
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 CCCP, suggesting
CC       uptake is coupled to a cation gradient (PubMed:31406332).
CC       {ECO:0000269|PubMed:31406332, ECO:0000269|Ref.2}.
CC   -!- SUBUNIT: Forms a complex with DabB2, possibly a heterodimer.
CC       {ECO:0000269|PubMed:31406332}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01871, ECO:0000305|PubMed:31406332}; Peripheral membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_01871, ECO:0000305|PubMed:31406332};
CC       Cytoplasmic side {ECO:0000305|PubMed:31406332}.
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) DabA
CC       family. {ECO:0000255|HAMAP-Rule:MF_01871, ECO:0000305}.
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DR   EMBL; CP001801; ACX95074.1; -; Genomic_DNA.
DR   RefSeq; WP_012823110.1; NC_013422.1.
DR   STRING; 555778.Hneap_0211; -.
DR   TCDB; 9.A.2.1.2; the putative dissolved inorganic carbon concentrating transporter (dic-ct) family.
DR   EnsemblBacteria; ACX95074; ACX95074; Hneap_0211.
DR   KEGG; hna:Hneap_0211; -.
DR   eggNOG; COG3002; Bacteria.
DR   HOGENOM; CLU_009885_1_0_6; -.
DR   OMA; DCDLEGR; -.
DR   OrthoDB; 179501at2; -.
DR   Proteomes; UP000009102; 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; 2.
DR   Pfam; PF10070; MpsB; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Metal-binding;
KW   Reference proteome; Transport; Zinc.
FT   CHAIN           1..827
FT                   /note="Probable inorganic carbon transporter subunit DabA2"
FT                   /id="PRO_0000453154"
FT   BINDING         351
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01871,
FT                   ECO:0000305|PubMed:31406332"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01871,
FT                   ECO:0000305|PubMed:31406332"
FT   BINDING         524
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01871,
FT                   ECO:0000305|PubMed:31406332"
FT   BINDING         539
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01871,
FT                   ECO:0000305|PubMed:31406332"
FT   MUTAGEN         351
FT                   /note="C->A: DAB2 no longer restores CAfree growth, still
FT                   binds Zn(2+)."
FT                   /evidence="ECO:0000269|PubMed:31406332"
FT   MUTAGEN         353
FT                   /note="D->A: DAB2 no longer restores CAfree growth, still
FT                   binds Zn(2+)."
FT                   /evidence="ECO:0000269|PubMed:31406332"
FT   MUTAGEN         524
FT                   /note="H->A: DAB2 no longer restores CAfree growth, still
FT                   binds Zn(2+)."
FT                   /evidence="ECO:0000269|PubMed:31406332"
FT   MUTAGEN         539
FT                   /note="C->A: DAB2 no longer restores CAfree growth."
FT                   /evidence="ECO:0000269|PubMed:31406332"
SQ   SEQUENCE   827 AA;  91617 MW;  1A8EA0E787EDC2EA CRC64;
     MTTLTSLQRS EAQRNHIVDL IDKACLRIAP IWPLDSFVAV NPYLGLIDQP FDTVGRYLEQ
     TVGESLFMDH GWFADKIAQG EITDDDLAQA AQQLDPSISL DTIKQQLAVH RQPAPALPLV
     TNELDRRDAP PVSEFVIEQV SQFMANYYDR GQALWHLPKE ASASLFAQWR RYTLINRSAS
     AVGLKQVRQH LLAVPSDAID ALFWALDQIN LPESRLPDYL FTLLKTIGGW ASWCRYLHFQ
     AGLHGESQHD LRDLLIIRLV WVALVIKETS SAGRQQWRAK LNDWFDPAKL VASPSATATA
     STKAQSSRID EILLAAAEQA FRRRINAGLN RQPADAPDQQ AERPTVQAAF CIDVRSEVFR
     RHLEASSPGL ETIGFAGFFG LPIDYCRMGE SEARLQNPVL INPAYRAQET GDPAIAQHRH
     ARQSRGAIWK QFKLSAASCF TFVESAGLSY VPRLLADSLG WHRSSLPPDA PGLTPEERAR
     LHPQLVKLDG GALSTQEKVD LAEKVLRGLG LTHTFAPIVL LAGHGSSTTN NPHRAGLDCG
     ACAGQAGDVN ARVAVQLLNE AAVRLGLIER GIAIPRDTRF VAALHDTTTD HIELLDLDQS
     GIESDQLSSL TQALKQAGEL TRLERLVTLE AQVDTVDAEK QATFRGRDWS QVRPEWGLAG
     NAAFIAAPRW RTRGLDLGGR AFLHDYDWRH DKEFGVLNVI MTAPLIVANW INLQYYGSTV
     DNLHQGAGNK VLHNVVGGTV GVIEGNGGDL RVGLAMQSLH DGEQWRHEPL RLSAYIEAPI
     AEIDKIIAGH DMLNALINNR WMHILHIDDN GIPHRRHAHG DWRPEPI
 
 
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