ID A0A1W6ZDG7_9BORD Unreviewed; 777 AA.
AC A0A1W6ZDG7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:ARP95401.1};
GN ORFNames=CAL15_13995 {ECO:0000313|EMBL:ARP95401.1};
OS Bordetella genomosp. 13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463040 {ECO:0000313|EMBL:ARP95401.1, ECO:0000313|Proteomes:UP000194161};
RN [1] {ECO:0000313|EMBL:ARP95401.1, ECO:0000313|Proteomes:UP000194161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU7206 {ECO:0000313|EMBL:ARP95401.1,
RC ECO:0000313|Proteomes:UP000194161};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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; CP021111; ARP95401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6ZDG7; -.
DR STRING; 463040.CAL15_13995; -.
DR KEGG; bgm:CAL15_13995; -.
DR OrthoDB; 8552908at2; -.
DR Proteomes; UP000194161; 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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02094; P-type_ATPase_Cu-like; 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; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
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; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
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 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 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 101..119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 139..163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 175..197
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 203..222
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 356..378
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 384..407
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 703..725
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 731..752
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 9..75
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 777 AA; 80794 MW; 98A76DE8A06713C6 CRC64;
MTAATPTLAQ LDLSVEGMTC ASCVRRVEKA LSNVPGVHVA NVNLATERAQ VSYDPDAAAP
EALLAAVGKA GYAAHAIAPH DDHADRQAEA RDAEARRLER ALAVAVALTL PVFLLEMVGH
LVPAWHHWID ATLGQRNSWV LQFVLTTAVL AWPGRHFFTI GLAALWRRAP EMNSLVALGA
GAAWGYSTVA TFVPQWLPAG ARAVYFEAAA VIVTLILLGR MLEARAKGRT GAAIRRLVAL
QPRSARVLRG GQPMDLPIAD VRVGDRVLVR PGEQVPLDGE IIEGSSYVDE SMLTGEPVPV
EKQAGDNVAG GTLNTTGGFT LRVTHVGADT QLARIIRMVE DAQGARLPVQ ALVDRITGWF
VPAVMAAALL TFVAWLVWGP PPALTHALVH AVAVLIIACP CAMGLATPTS IMVGTGRAAE
LGVLFRHGDA LQALRDVDVV AFDKTGTLTQ GRPALAALRL ATGAAAATED ELLRWLASLQ
ARSEHPIAQA IVAAAAERGL ALLPAEDFRA VSGAGVQGRV AGHALSAGAA RLMADHGVDV
SGFGPQAADW ARQGWTPIYV AIDGRAAAMA AVADPVKPSA AQAIAALHAQ GIRTAMITGD
HRDTAQAVAR GLDIDDVRAE VLPDAKVRAV EALRSGGRKV AFVGDGINDA PALAAADVGV
AIGTGTDVAI EAASVVLMTG DLRGVPTAIA LSRATLANIR QNLFWAFAYN AALIPLAAGA
LYPAYGMVLS PMLAAGAMAL SSVFVVGNAL RLKTFAMAGR RRGDPRSAGP RSADPRG
//
