ID A0A329ZJT4_9HELI Unreviewed; 719 AA.
AC A0A329ZJT4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Copper-transporting ATPase {ECO:0000256|ARBA:ARBA00040690};
DE EC=7.2.2.9 {ECO:0000256|ARBA:ARBA00038904};
GN ORFNames=CCY99_00460 {ECO:0000313|EMBL:RAX55204.1};
OS Helicobacter sp. 16-1353.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=2004996 {ECO:0000313|EMBL:RAX55204.1, ECO:0000313|Proteomes:UP000251728};
RN [1] {ECO:0000313|EMBL:RAX55204.1, ECO:0000313|Proteomes:UP000251728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-1353 {ECO:0000313|EMBL:RAX55204.1,
RC ECO:0000313|Proteomes:UP000251728};
RX PubMed=29225701; DOI=10.1186/s13099-017-0220-y;
RA Feng Y., Mannion A., Madden C.M., Swennes A.G., Townes C., Byrd C.,
RA Marini R.P., Fox J.G.;
RT "Cytotoxic Escherichia coli strains encoding colibactin and cytotoxic
RT necrotizing factor (CNF) colonize laboratory macaques.";
RL Gut Pathog. 9:71-71(2017).
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:RAX55204.1}.
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DR EMBL; NHYM01000001; RAX55204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329ZJT4; -.
DR OrthoDB; 2490525at2; -.
DR Proteomes; UP000251728; 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 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; 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: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 PRINTS; PR00942; CUATPASEI.
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; 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|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..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 109..127
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 148..169
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 175..194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 328..351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 357..385
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 665..686
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 692..713
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 719 AA; 78952 MW; B8CA9FCAB39E47FF CRC64;
MKQLRLKITG MTCAACSGSI ERSFRRKSYI DKIEVDLING SAFIIYDEKT ANIDDIIKHI
QKLGYGAEIL KNSQKKDSSY NNDYLIAIIF AIPLFLISMG SMFLHLHNEI LICLIEIILL
LPILYAGRNI YKKGFLSLLN LVPNMDSLVM LGSGSAILYS LYMIILYILN INQELLHSIY
FESAGVIIAV IMLGKRLEHK ATDNAKTGLK DLINLLPKTT LVLQNNNIVE KNIKDICIND
IIVIPKGAMV SLDGILINNE CKVDESLITG ESKHKRKQKG DIILSGSINQ NEQFMLKVVA
LEEDSMIGKI INLMQGIKKA PIARIADIVS AYFVPIVIFI SIIGALAWFI YRGDFHFSFI
VLTSTLLISC PCALGLATPL SILVATNKAS QNAIYFKSGE SLEKTSKINI VVFDKTGTLT
KGELEVIDFV LKENNSFSKE QILSLSNALE KASEHLIAKA IIKYISKIPN INNELKSNDV
KTSVGLGISG MVENHLIKIG NAEFIGLDKD SLIVSKHTLA YISIDGIYCG AFIIADSLRE
NAKILISNLK SLGIKSIILS GDSKDSVSSV ASLCGIDEFY YSQLPNDKLN YITNLQKENN
KVAFIGDGIN DALAISKADI GISLSLANDI AIKQADIILL STDLNSLYRA IVLSKKTLKN
IKENLAFAFI YNICAIPIAL GIPYLFNINL ALNPMIAGIA MGLSSISVVL NSLRLNRAI
//
