ID H6LB80_ACEWD Unreviewed; 747 AA.
AC H6LB80;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN OrderedLocusNames=Awo_c08410 {ECO:0000313|EMBL:AFA47632.1};
OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS / WB1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=931626 {ECO:0000313|EMBL:AFA47632.1, ECO:0000313|Proteomes:UP000007177};
RN [1] {ECO:0000313|Proteomes:UP000007177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC {ECO:0000313|Proteomes:UP000007177};
RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT "Complete genome sequence of Acetobacterium woodii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFA47632.1, ECO:0000313|Proteomes:UP000007177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC {ECO:0000313|Proteomes:UP000007177};
RX PubMed=22479398; DOI=10.1371/journal.pone.0033439;
RA Poehlein A., Schmidt S., Kaster A.K., Goenrich M., Vollmers J., Thurmer A.,
RA Bertsch J., Schuchmann K., Voigt B., Hecker M., Daniel R., Thauer R.K.,
RA Gottschalk G., Muller V.;
RT "An ancient pathway combining carbon dioxide fixation with the generation
RT and utilization of a sodium ion gradient for ATP synthesis.";
RL PLoS ONE 7:E33439-E33439(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775,
CC ChEBI:CHEBI:456216; EC=7.2.2.21;
CC Evidence={ECO:0000256|ARBA:ARBA00036510};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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DR EMBL; CP002987; AFA47632.1; -; Genomic_DNA.
DR RefSeq; WP_014355235.1; NC_016894.1.
DR AlphaFoldDB; H6LB80; -.
DR STRING; 931626.Awo_c08410; -.
DR KEGG; awo:Awo_c08410; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_6_2_9; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00941; CDATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cadmium {ECO:0000256|ARBA:ARBA00022539};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000007177};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 119..138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 144..166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 379..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 705..726
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 747 AA; 80910 MW; 6B6F5B70D3502B21 CRC64;
MKVFLEGLNC ANCAGKIEKL VGKMPNVSAA SISLATGSLV IEEADGFARE ETYDAIVKLV
HSLEPHVVVS TTRNQTAAVT GCGCGDHAHG HSHEHAHDHP KTEAVQSHTH GDMDKRQKIE
LSSAIGLFIL GFILQALLPA NLEMVTIGVF LGAYLLAGYR VILLAFRNIG HGQIFDENFL
MAIATFGALF LTEWPEAAGV MIFFGIGEYF QDRAVDNARR SIAETISFNA ITANRVDPEG
EVVIDAKEVK IGDLLIIKPG EKIPADGIII EGVSHLDTSP LTGESYPRKV AKGDEILSGM
INGNAVLKIR VTKDYENSTA MKIMHLIEEA SDKKGKTEKF ITKFSHYYTP IVVFSAIAMA
IIPPLFISGA SWQTWFYQSL IFLVVSCPCA LVLSIPISYF GGIGRASKEG VLIKGGNYLD
VLYQSDVFVF DKTGTLTQGE FKVLKAEPAP GFTEAELLAA AATGEHYSNH PIGKAITTYV
KMAVDENNLT DYLEVPGKGT RVVVGDQVIL AGNRSLFQEH QIELADNQET GTIVYVAVDN
KLAGYLVLGD MLKENAFSAL TLLKKLGIKK TIMLSGDNSS VANEIGTQLM LDEVIGDCLP
QDKVRAFEKI KGGNTAGKTI FVGDGMNDAP VLAMADAGIA MGALGSDAAI EAADIILMKD
DPMDIVKAVN IAKYTRRIMI QNIVMALGIK LTVLTMTFFG MGEMYLAIFA DVGAAILTIL
NTTRILRYRG FWQKQNRSKQ LVERIAD
//
