ID A0A3P3VRX2_9GAMM Unreviewed; 949 AA.
AC A0A3P3VRX2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=D0544_06395 {ECO:0000313|EMBL:RRJ84728.1};
OS Aestuariirhabdus litorea.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Aestuariirhabdaceae; Aestuariirhabdus.
OX NCBI_TaxID=2528527 {ECO:0000313|EMBL:RRJ84728.1, ECO:0000313|Proteomes:UP000280792};
RN [1] {ECO:0000313|EMBL:RRJ84728.1, ECO:0000313|Proteomes:UP000280792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GTF-13 {ECO:0000313|EMBL:RRJ84728.1,
RC ECO:0000313|Proteomes:UP000280792};
RA Khan S.A.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RRJ84728.1, ECO:0000313|Proteomes:UP000280792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GTF-13 {ECO:0000313|EMBL:RRJ84728.1,
RC ECO:0000313|Proteomes:UP000280792};
RA Shieh W.Y.;
RT "Simiduia agarivorans gen. nov., sp. nov., a marine, agarolytic bacterium
RT isolated from shallow coastal water from Keelung, Taiwan.";
RL Submitted (DEC-2018) 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:RRJ84728.1}.
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DR EMBL; QWEZ01000001; RRJ84728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P3VRX2; -.
DR Proteomes; UP000280792; 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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 3.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 3.
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; 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; 3.
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; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 3.
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:UP000280792};
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 286..305
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 317..334
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 355..377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 383..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 539..558
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 564..587
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 879..898
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 904..922
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 10..73
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 199..262
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 152..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 100960 MW; 6E6FE7406F067E67 CRC64;
MNTEHTTAVP ETELSLEGVK CNGCVNKIRR ALVESDPDAS IEVDLEQRLA RVHSVLSADQ
LINLVEELGY GASLSEPVAP PHHRFRVEGV KCNGCLNKIR SALLDRDEGA EASADFDAKV
LEIQSQLPPT EVIELVSGLG YGIQPLETAE PTETLAETDA AQQTAEPETR EPVNAAEPEP
EPEPEPEPEP EPEPETVGQG LQLALEGMTC AGCVKSIETA IQGVSGVDRV EVNFGSRSAL
VSGSASAEDL IHAVEQAGYG ASLVEDPEQA EQQKEAFEAA EYRRKLINTG IGLGLGVPLM
IAGFTHGMEL SSPAERGFWG LIGLLTLAVL LSAGRHFYVG AWKAFTHHNA NMDTLIATGT
GAAWLYSMVV VVAPGIVPEA ARGLYFEAAA MIIGLINLGQ ALELKARGRT SQAIKRLLNL
RTKSARVWRE GRYQELPIEQ VQQDDLLQVR PGEQIPVDGV VTEGSSNLDE SMLTGEPMPV
KKTLGDELSA GTLNRTGALC FRATRVGKAT RLAQIIEMVR RAQNSKPPIS RLADQVSSIF
VPAVMLIAVA TALAWYNLGP DPRVVHMLVA ATTVLIIACP CALGLATPIS TMIGVGKAAE
FGILIRNGEA LQKASTLSYV VVDKTGTLTL GQPRVTNFEL YGDGAKEPTL ALVHALESRS
EHPLGEALVS YCQDQSGEQE VEAFEALSGK GLQARVAGQQ VLIGNPRLMA DHRIDLSIAQ
SHVESWEAEA RTLVYVAIDG HLSALFGIAD PIKPDAAEAI QRLKQDGVRV LMLTGDNPAT
AAAVARQTGI DEYQAELMPD DKLAEIRRLQ SLGERVGMAG DGINDAPALS QADVGFAIGS
GTDVAIESAD ITLMRGSLHG IADAVELSRA TLRNIKQNLW GAFTYNALGI PVAAGVLYPF
TGLLLSPVIA GVAMSLSSVT VVSNANRLRF FAPSHLPHTD NGPVAKESV
//
