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Database: UniProt
Entry: A0A438AJY5_9RHOB
LinkDB: A0A438AJY5_9RHOB
Original site: A0A438AJY5_9RHOB 
ID   A0A438AJY5_9RHOB        Unreviewed;       865 AA.
AC   A0A438AJY5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:RVV98964.1};
GN   ORFNames=EKE94_08775 {ECO:0000313|EMBL:RVV98964.1};
OS   Mesobaculum littorinae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Mesobaculum.
OX   NCBI_TaxID=2486419 {ECO:0000313|EMBL:RVV98964.1, ECO:0000313|Proteomes:UP000285908};
RN   [1] {ECO:0000313|EMBL:RVV98964.1, ECO:0000313|Proteomes:UP000285908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M0103 {ECO:0000313|EMBL:RVV98964.1,
RC   ECO:0000313|Proteomes:UP000285908};
RA   Li F.;
RT   "Mesobaculum littorinae gen. nov., sp. nov., isolated from Littorina scabra
RT   that represents a novel genus of the order Rhodobacteraceae.";
RL   Submitted (NOV-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:RVV98964.1}.
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DR   EMBL; RQXX01000002; RVV98964.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A438AJY5; -.
DR   OrthoDB; 9807843at2; -.
DR   Proteomes; UP000285908; 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; 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; 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; 2.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
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:UP000285908};
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        192..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        226..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        264..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        292..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        445..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        473..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        788..807
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        813..835
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          5..70
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          72..138
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          846..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   865 AA;  87867 MW;  5066F8593F598CBE CRC64;
     MDTAQRITFA IGGMSCGGCA GRVERALTAV EGVRDVAVNL ATETATVVYD APATAAGLAG
     PLREAGYPAR SRTATLTVGS MSCASCVGRV DRALAAAPGV IDVAVNLATE TARVTYLEGA
     TTPQELAATA TRAGYPARIA RIAGAAGATA SAAGAAGAGT GPGAAAGSDA PAADDMRTRK
     DREARVLRRD TAVAAALALP VFLLEMGGHA IPAVHAWIGD TIGHQTSWLL QFVLTTAVLA
     GPGRRFYAKG VPALLRGAPD MNSLVALGTA AAWLFSVVAT FCPGLLPAGT RAVYYEAAAM
     IVVLILVGRW MEARAKGRTG AAIARLVGLQ ARTARVERDG EQVELAIEDI VPGDVLVVRP
     GERIAVDGAV IDGTSHVDES MLTGEPVPVA KAAGDPVTGG TVNGAGGFRF RATRVGADTT
     LSQIIRMVEE AQGAKLPIQG LVNRITLWFV PVVLGLAALT TLAWLVFGPA PVLGHALVAG
     VSVLIIACPC AMGLATPTSI MVGTGRAAEM GVLFRKGDAL QALSDVSVVA LDKTGTLTEG
     RPELTDLVPA PGVDRAEVLA LVAAVEGRSE HPVAGAILRA ARREGVPAHE VAAFSSLTGY
     GVRARVAGRE VLVGADRLMT REGVDTAALA ATEAELARKG RTALYAAIDG RVVALLAVAD
     PVKPASRAAI AALHGMGLKV AMVTGDKPET ARAIAAETGI DHVIAGVLPD GKVAALEALR
     QGGRIAFVGD GINDAPALAQ ADVGIAIGTG TDVAIESADV VLMSGDLRGV VNACEVSRRT
     MRNIRENLFW AFGYNTALIP VAAGVLYPAL GVLLSPVLAA GAMALSSVFV LSNALRLRRL
     RPAMDEGAGA PGPAPSTAPT PVPAE
//
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