ID G7SGM6_STRSU Unreviewed; 816 AA.
AC G7SGM6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 70.
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 Name=copA {ECO:0000313|EMBL:AER18891.1};
GN ORFNames=SSUD12_0568 {ECO:0000313|EMBL:AER18891.1};
OS Streptococcus suis D12.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1004952 {ECO:0000313|EMBL:AER18891.1, ECO:0000313|Proteomes:UP000008845};
RN [1] {ECO:0000313|EMBL:AER18891.1, ECO:0000313|Proteomes:UP000008845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D12 {ECO:0000313|EMBL:AER18891.1};
RX PubMed=22026465; DOI=10.1186/1471-2164-12-523;
RA Zhang A., Yang M., Hu P., Wu J., Chen B., Hua Y., Yu J., Chen H., Xiao J.,
RA Jin M.;
RT "Comparative Genomic Analysis of Streptococcus suis reveals significant
RT genomic diversity among different serotypes.";
RL BMC Genomics 12:523-523(2011).
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 Evidence={ECO:0000256|ARBA:ARBA00001390};
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}.
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DR EMBL; CP002644; AER18891.1; -; Genomic_DNA.
DR RefSeq; WP_014637658.1; NC_017621.1.
DR AlphaFoldDB; G7SGM6; -.
DR KEGG; ssk:SSUD12_0568; -.
DR PATRIC; fig|1004952.3.peg.550; -.
DR HOGENOM; CLU_001771_0_3_9; -.
DR Proteomes; UP000008845; Chromosome.
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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
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; 2.
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; PR00941; CDATPASE.
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 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 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 194..212
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 233..255
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 267..285
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 419..440
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 446..469
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 762..784
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 790..809
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 72..138
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 816 AA; 87602 MW; C37AC8FA6D29988B CRC64;
MKHVTYAVTG MTCASCAMTV EKAVGKLAGV EEASVNLATE KLSVSYDERL LGLEDFRQAV
EKAGYQLVDN LVTESYDISG MTCASCAMTV EKALDKLEGV EEVSVNLATE KATIRYSRDR
QNPASLEKAV ERAGYQLIRP EEVEETVDKG PSKEDSLWKR FVWSAVFTLP LLYIAMGPML
PWGGLPLPAL LHQPLVYAVS QVILLLPVLY LGRSFFQKGF KTLLQGHPNM DSLIAVGTGA
ALVQGLLMIA FLLMGKEVAM HGHHPELYFE SAAVILTLIT LGKYFEARAK GQTSEAIKKL
MDLAPKTAQV LRNGQEMQVP IEEVVVGDQV LVRPGQQIPV DGQVLEGQTR VDESMLTGES
LPVKKALGDT VFGGTLNQQG AITMQATKVG RDTTLAQIIR LVEEAQGSKA PIAKLADQVS
AVFVPVVMGL AFLSGLAWYF LGQESWIFSL SIIIAVLVIA CPCALGLATP TAIMVGTGKG
AENGLLFKSG QAIETLQGVN TIVFDKTGTI TEGKPQVTDV HLLATKNREQ VLQLAASSEQ
FSEHPLAQAL LQAAQTEKID LLPATDFQAL SGRGLSVTIA EQTIYLGNER LMRERGIDVS
QGRAVAEAFA HQAKTPVFLA SQRELLAVIA IADKVKETSR QAVQALQAMG LEVVMLTGDN
EKTAQAIAKE VGIEQVVSQV LPDDKANQVK HLQEQDKTVA MVGDGINDAP ALAQAHVGLA
IGSGTDIAIE SADIVLMHSD ILDVVKAVKL SQATMRTIKQ NLFWAFAYNV IGIPIAMGLL
HVFGGPLLNP MFAGAAMALS SVSVVLNALR LKTYKL
//
