COPA_HELFC
ID COPA_HELFC Reviewed; 732 AA.
AC O32619; E7A9G6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Copper-transporting ATPase;
DE EC=7.2.2.8;
GN Name=copA; OrderedLocusNames=Hfelis_12590;
OS Helicobacter felis (strain ATCC 49179 / NCTC 12436 / CS1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=936155;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49179 / NCTC 12436 / CS1;
RX PubMed=9440521; DOI=10.1128/jb.180.2.317-329.1998;
RA Bayle D., Waengler S., Weitzenegger T., Steinhilber W., Volz J.,
RA Przybylski M., Schaefer K.P., Sachs G., Melchers K.;
RT "Properties of the P-type ATPases encoded by the copAP operons of
RT Helicobacter pylori and Helicobacter felis.";
RL J. Bacteriol. 180:317-329(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49179 / NCTC 12436 / CS1;
RA Arnold A., Zigova Z., Lawley T., Falkow S., Bentley S., Aslett M.,
RA Muller A.;
RT "Comparative whole genome analysis of the carcinogenic bacterial pathogen
RT Helicobacter felis.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably involved in copper export.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
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DR EMBL; AJ001932; CAA05104.1; -; Genomic_DNA.
DR EMBL; FQ670179; CBY83343.1; -; Genomic_DNA.
DR PIR; T47269; T47269.
DR RefSeq; WP_013469707.1; NC_014810.2.
DR AlphaFoldDB; O32619; -.
DR SMR; O32619; -.
DR STRING; 936155.HFELIS_12590; -.
DR EnsemblBacteria; CBY83343; CBY83343; HFELIS_12590.
DR GeneID; 36134482; -.
DR KEGG; hfe:HFELIS_12590; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_7; -.
DR OMA; ITFFGWM; -.
DR OrthoDB; 237367at2; -.
DR Proteomes; UP000007934; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00403; HMA; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 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; Cell membrane; Copper; Copper transport; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..732
FT /note="Copper-transporting ATPase"
FT /id="PRO_0000046169"
FT TOPO_DOM 1..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..365
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..683
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 684..694
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 695..713
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..732
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 2..68
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 421
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 16
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 609
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 613
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
SQ SEQUENCE 732 AA; 78853 MW; 7105107EA5949EFD CRC64;
MTKAQFYIEG MTCSACSSGI ERALGRKKFV QEVGVDLISK KAFVVYDENQ ASLEDVFKQI
EKLGYQPRVA TDTPNTFLNP SFLTPNVKLA LVLLGTLGVL ALSMFAPLLP LPSFLKNPFI
NGIVQLVLSL MVMHMGRNFY VHGFKALWAR QPNMDSLIAL GTSAALLYSL VLLFRAYTHA
PIEGYYFESV CVILLFVMAG KRVEENSKDK ALEAMQSLMR HQSLNALKIE NGQSVEVPLE
SLQKGDILQI LPGSYIPVDG VLFKGEAEVD ESMLSGESLP VYKKEGMDLF AGTLNTTTTF
QMRATHTKAQ STLAKILTLI AKAQGSKAPI ARLADKVAGV FVPIVIGIAS IAFLVWLVLG
DFTRALEVFI AILVISCPCA LGLATPMALL VAQKEASLLG LFFKDAVSLE KAKNVNHVIF
DKTGTLTLGT PLVQEVRVAE GVDRLELLTL CASLEAQSEH VIAKGIVAHA KEQGIALQEV
QEVQAKPGFG IKGVVGDQII KAGNLEFFNL PNPFGTLEGI QVFVGTETQI LGVVVLADSL
KEGSKEAISE LKALGVKTTL LSGDNLENVR ALATQLGIQD YHAQAKPEDK LKVIQELKAQ
GKVVMMVGDG VNDAPSLALS DVGVVMAKGS DASLEVADVV SFNNDIQSVV SAMKLSALTI
ANIKQNLFWA FCYNSIAIPL ACGVAYKLGI MFNPMLASLA MSLSSVSVVL NAQRLRGAHF
KIRGSHENRH SS
