ID T5CPF8_HELPX Unreviewed; 741 AA.
AC T5CPF8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Copper-transporting ATPase {ECO:0000256|ARBA:ARBA00040690};
DE EC=7.2.2.9 {ECO:0000256|ARBA:ARBA00038904};
GN ORFNames=N411_01675 {ECO:0000313|EMBL:EQL56473.1};
OS Helicobacter pylori FD535.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1191464 {ECO:0000313|EMBL:EQL56473.1, ECO:0000313|Proteomes:UP000015966};
RN [1] {ECO:0000313|EMBL:EQL56473.1, ECO:0000313|Proteomes:UP000015966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD535 {ECO:0000313|EMBL:EQL56473.1,
RC ECO:0000313|Proteomes:UP000015966};
RX PubMed=23012278; DOI=10.1128/JB.01278-12;
RA Gunaletchumy S.P., Teh X., Khosravi Y., Ramli N.S., Chua E.G., Kavitha T.,
RA Mason J.N., Lee H.T., Alias H., Zaidan N.Z., Yassin N.B., Tay L.C.,
RA Rudd S., Mitchell H.M., Kaakoush N.O., Loke M.F., Goh K.L., Vadivelu J.;
RT "Draft genome sequences of Helicobacter pylori isolates from Malaysia,
RT cultured from patients with functional dyspepsia and gastric cancer.";
RL J. Bacteriol. 194:5695-5696(2012).
RN [2] {ECO:0000313|EMBL:EQL56473.1, ECO:0000313|Proteomes:UP000015966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD535 {ECO:0000313|EMBL:EQL56473.1,
RC ECO:0000313|Proteomes:UP000015966};
RX PubMed=24051312;
RA Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA Loke M.F., Vadivelu J.;
RT "Multiple genome sequences of Helicobacter pylori strains of diverse
RT disease and antibiotic resistance backgrounds from malaysia.";
RL Genome Announc. 1:E00687-E00713(2013).
CC -!- FUNCTION: Probably involved in copper export.
CC {ECO:0000256|ARBA:ARBA00037143}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:10376, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29036, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.9;
CC Evidence={ECO:0000256|ARBA:ARBA00036474};
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:EQL56473.1}.
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DR EMBL; AKHP02000067; EQL56473.1; -; Genomic_DNA.
DR RefSeq; WP_000665023.1; NZ_AKHP02000067.1.
DR AlphaFoldDB; T5CPF8; -.
DR PATRIC; fig|1191464.11.peg.224; -.
DR Proteomes; UP000015966; 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 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 84..108
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 120..138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 185..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 343..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 368..394
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 685..704
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 710..729
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..67
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 741 AA; 81316 MW; 1B0832A3594BD6ED CRC64;
MKESFYIEGM TCTACSSGIE RSLGRKSFVK KIEVSLLNKS ANIEFNENET NLDEIFKLIE
KLGYSPKKTL TKEKKEFFSP NVKLALAVIF TLFVVYLSMG AMLSPSLLPE SLLTINNHSN
FLNACLQLIG TLIVMHLGRD FYIQGFKALW HRQPNMSSLI AIGTSAALIS SLWQLYFVYT
NQWSYGHYYF ESVCVILMFV MVGKRIENVS KDKALDAMQA LMKNAPKTAL KMQNNQQIEV
LVDSIVVGDI LKVLPGSAIA VDGEIIEGEG ELDESMLSGE ALPVYKKVGD KVFSGTLNSH
TSFLMKATQN NKNSTLSQII EMIHNAQSSK AEISRLADKV SSVFVPSVIA IAVLAFVVWL
IIAPKPDFWW NFGIALEVFV SVLVISCPCA LGLATPMSIL VANQKASSLG LFFKDAKSLE
KARLVNTIVF DKTGTLTNGK PVVKSVHSNI ELLELLSLAG SIEKSSEHVI AKGIVEYAKE
HNAPLKEMSG VKVKTGFGIS AKVDYQGAKK IIKVGNSEFF NPINTLEIKE NGILVFVGRM
ISEKEDELLG VFVLEDLPKK GVKEHIAQIK NLGINTLLLS GDNRENVKKC TLELGIDGYI
SNAKPQDKLN KIKELKEKGQ IVMMVGDGLN DAPSLAMSDV AVVMAKGSDV SVQAADIVSF
NNDIKSVYSA IKLSQATIKN IKENLFWAFC YNSVFIPLAC GVLYKANIML SPAIAGLAMS
LSSVSVVLNS QRLRNFKIKD H
//
