ID A0A370DQ44_9GAMM Unreviewed; 983 AA.
AC A0A370DQ44;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=DIZ78_05775 {ECO:0000313|EMBL:RDH87003.1};
OS endosymbiont of Escarpia spicata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2200908 {ECO:0000313|EMBL:RDH87003.1, ECO:0000313|Proteomes:UP000254771};
RN [1] {ECO:0000313|EMBL:RDH87003.1, ECO:0000313|Proteomes:UP000254771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1462 {ECO:0000313|EMBL:RDH87003.1};
RX PubMed=30022157;
RA Li Y., Liles M.R., Halanych K.M.;
RT "Endosymbiont genomes yield clues of tubeworm success.";
RL ISME J. 0:0-0(2018).
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:RDH87003.1}.
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DR EMBL; QFXE01000007; RDH87003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370DQ44; -.
DR Proteomes; UP000254771; 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; 2.
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; 3.
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:UP000254771};
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 259..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 331..349
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 361..378
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 512..534
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 540..569
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 857..876
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 882..904
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 11..73
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 100..162
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 918..981
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 983 AA; 102608 MW; A94D6D98504412FE CRC64;
MISPAADTGG DSYLIAIEGM SCGHCVAAVE KAVFAVADVV SIEVDLEKQF AQVSGGLPHN
VIAAIVEAGY TARPLPQIPA DCPVPDPTVP SSAAEKQITG DYEIAIGDMT CSSCVAAVER
AIRSVPGVSE ASVNLVEKRA QVVGGDPGAV VNAVMGQGYS ARLLERPKVS DSLLFSVPGL
GKTASPAALE TVIHSLDVTA KVAIEGETLS VTTTTHPADL LIALHSAGYE SKLLEQFVDP
YVEQGLEAQQ EIRRSRQRAL LAALVGGGLM AANLAGWLPA LTDADGPIGL SGQAFWGLVA
GVCLFVMWFS GRNYYSGAWK QARHFAANMD TLVALGTGAA WLSSVILIIR PDFIPGGGHL
YLDASVLILA FLQFGHVLET SAKRTTSEAI GSLVGLAPKS AVVEREFGEV EIPVSLLRLG
DHIRVRPGER MPIDGEVIDG RSSVDESMLT GESMPVSKQP GDQVIGGTMN RSGTLLFGIT
RLGEETTLAH IITMVKRAQM SKPPIGRLVD RVAAVFVPIV IVIALLTFVV WYQIGPDPRA
AYALTAGIAV LVIACPCALG LATPIAIMVG TGRAAQLNIL IRNSDALQSA SRLTHLVVDK
TGTLTEGRPT VTAIHPAGTT PESEVIRLAA MVETGSEHPL AEAVVEAARS RGLDIAGVTD
FQALEGRGVS GQAEGRRLLL GNHHLMEEQG ATLPPALLKE ASRQAANAAT PVWLAVDSQI
AGLLAVNDPV RPDSFAAVEA LQREGVRVVM CTGDNRATAE AVAADLKIDE VHSERLPGEK
LDVVKSLQRQ GYRVGMVGDG INDAPALAQA DTGFAVGSGA DVAIDNADIT LAGDSLADVS
TAIAISSATI RNIKQNLFGA FIYNVIGIPM AAGVLFPVTG WLLPPMFASA AMALSSVTVV
FNANRLRFFQ PLRMERPVSI KLNVTGMTCP HCVNHVTKAL QGVGGVESVE VSLDAGEALV
TGSAAVDLLI AAVKDAGYNA ETV
//
