ID A9BXS6_DELAS Unreviewed; 839 AA.
AC A9BXS6;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:ABX38352.1};
GN OrderedLocusNames=Daci_5724 {ECO:0000313|EMBL:ABX38352.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX38352.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX38352.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000884; ABX38352.1; -; Genomic_DNA.
DR RefSeq; WP_012207521.1; NC_010002.1.
DR AlphaFoldDB; A9BXS6; -.
DR STRING; 398578.Daci_5724; -.
DR GeneID; 24118475; -.
DR KEGG; dac:Daci_5724; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_4; -.
DR Proteomes; UP000000784; 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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 2.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 2.
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; IPR006122; HMA_Cu_ion-bd.
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; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR00003; copper ion binding protein; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Ion transport {ECO:0000256|ARBA:ARBA00022796};
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:UP000000784};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT TRANSMEM 178..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 216..232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 252..274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 280..299
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 433..455
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 461..484
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 779..798
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 804..822
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 9..74
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 76..141
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 144..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 87255 MW; 26CE2022A7F2A0F3 CRC64;
MNASTKAGMA IDLPVQGMTC ASCVGRVERA LKKLPGVQEA VVNLATEKAS IRFEGAADLP
AAISAIEKAG YEVPQSSVEL EVEGMTCASC VGRVERALKK VEGVQSASVN LATERALVTL
AGSADVAALV AAVHKAGYEA RPLGASANPA SEGGAAQSPA EDGTEQRQAR ERASLKRSLI
VATVFALPVF VLEMGGHMVP AFHHWVGQAI GTQNSWYLQC LLSAIVLFGP GLRFFQKGIP
ALLRGAPDMN SLVAVGTSAA FAYSLVATFV PQWLPAGTVN VYYEAAAVIV ALILLGRFME
ARAKGNTSEA IRRLVRLQAK TARVRKDGAV QEVDIAAVRA GDTIEVRPGE RIPVDGEVIE
GSSFVDESMI SGEPVPVEKT PGAELVGGTV NQNGALAFRA TKVGADTLLA QIIRMVEQAQ
GSKLPIQALV DQVTMWFVPA VMAVALLTFG AWLAWGPSPA LSFALVNAVA VLIIACPCAM
GLATPTSIMV GTGRAAQMGV LLRKGEALQT LKDARVVAVD KTGTLTRGRP ELTDLVLAPG
FEGERSRVLA LVAAVEDRSE HPIARAIVDA AKAEDLPLGA VDRFESVTGF GVRAQVEGVR
VEIGADRFMR ELGLQVDTLA DEAARLGDEG KTPLYAAVDG RLAAMIAVAD PIKDSTPAAI
AALHALGLKV AMITGDNRRT AEAIARQLGI DEVVAEVLPG GKVDAVKRLK AEHGTLAYVG
DGINDAPALA EADVGLAIGT GTDIAIEAAD VVLMSGDLGG VPNAIALSKA TMANIRQNLF
WAFAYNVALI PVAAGLLYPV NGTLLSPVFA AGAMALSSVF VLSNALRLRR FSPPLAAGR
//
