ID A0A1V3TR24_9PAST Unreviewed; 723 AA.
AC A0A1V3TR24;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Copper-exporting P-type ATPase {ECO:0000256|ARBA:ARBA00015102};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
DE AltName: Full=Copper-exporting P-type ATPase A {ECO:0000256|ARBA:ARBA00029719};
DE AltName: Full=Cu(+)-exporting ATPase {ECO:0000256|ARBA:ARBA00033239};
GN ORFNames=BMT54_08000 {ECO:0000313|EMBL:OOH88935.1};
OS Pasteurellaceae bacterium 15-036681.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae.
OX NCBI_TaxID=1924934 {ECO:0000313|EMBL:OOH88935.1, ECO:0000313|Proteomes:UP000188845};
RN [1] {ECO:0000313|EMBL:OOH88935.1, ECO:0000313|Proteomes:UP000188845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15-036681 {ECO:0000313|EMBL:OOH88935.1,
RC ECO:0000313|Proteomes:UP000188845};
RA Stuber T.P., Hicks J.A., Robbe-Austerman S., Lantz K.;
RT "Draft genome sequence of a Pasteurellaceae bacterium isolated from a pygmy
RT hippo (Hexaprotodon liberiensis).";
RL Submitted (NOV-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOH88935.1}.
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DR EMBL; MQVI01000026; OOH88935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3TR24; -.
DR STRING; 1924934.BMT54_08000; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000188845; Unassembled WGS sequence.
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; TIGR01512; ATPase-IB2_Cd; 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:SF6; COPPER-EXPORTING P-TYPE ATPASE; 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; PS01229; COF_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000188845};
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 91..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 118..135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 156..174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 180..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 333..355
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 361..382
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 670..689
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 695..714
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..64
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 723 AA; 78511 MW; 175AFDE2DFF11035 CRC64;
MQQQFLLNGL HCAACVRRVE TIVKRIPEVE FASVNLADQT AFVQGDVSAE AVIQAITKIG
FGAELLESEQ ERRAKQQAQT HATLKQKKQQ FILALAVGSL LMLYGLIFGM EATADNRWIW
LIWALITAST MYFSGKHFFT GAWTSLKNRA STMDTLIALS TGVAFLYSFY LTLFPQHHSH
LYYEASVMII GFLNLGKFLE LKAKQRSSLA LEKLLDLAPQ QAVIFEENIA KTIPAKAIKI
EMRVQALTGD RLAVDGTLES GSIWVDESML TGEALPVEKK IGDKVRAGTI VQDGAGIYIA
EQVGSQTALA RIITAVRHAQ SSKPPLAQWV DKVAAVFVPM VVNIALTSSL IWLSLGKGLD
FSLSIFTTVL IIACPCALGL AIPLSTIAGV ARSAEFGVLV RNIEALQASS EIDTLVFDKT
GTLTTGEMQV THIETFNNIS QEQLLTFAKS LELHASHPIA KAIVKFADNL PACEITNLQI
VKGMGMSAKC SEDIVKIGNQ SFIENGCRGD PMWSPINDEN VGTQVFVSIN NLMAGIIYLQ
DQLRAESQEM IKNFQAQGYQ CLMLTGDRKI TADYYANQLG LDGVIADVLP EQKAEQIAKL
QQQGRKVAMI GDGINDAPAL AQANVGIAMH NGSEIAVETA DLSLMKTGLE PVSQILPFSK
QVLTNMKQSL VGAFIYNVVS IPIAAGALYS LTGWLLNPMI AAIAMALSSV TVVLNSQRLL
RKS
//
