ID S5R2W7_9STRE Unreviewed; 745 AA.
AC S5R2W7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN ORFNames=KE3_0431 {ECO:0000313|EMBL:AGS04960.1};
OS Streptococcus lutetiensis 033.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1076934 {ECO:0000313|EMBL:AGS04960.1, ECO:0000313|Proteomes:UP000015268};
RN [1] {ECO:0000313|EMBL:AGS04960.1, ECO:0000313|Proteomes:UP000015268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=033 {ECO:0000313|EMBL:AGS04960.1,
RC ECO:0000313|Proteomes:UP000015268};
RX PubMed=23782707; DOI=10.1186/1471-2180-13-141;
RA Jin D., Chen C., Li L., Lu S., Li Z., Zhou Z., Jing H., Xu Y., Du P.,
RA Wang H., Xiong Y., Zheng H., Bai X., Sun H., Wang L., Ye C., Gottschalk M.,
RA Xu J.;
RT "Dynamics of fecal microbial communities in children with diarrhea of
RT unknown etiology and genomic analysis of associated Streptococcus
RT lutetiensis.";
RL BMC Microbiol. 13:141-141(2013).
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; CP003025; AGS04960.1; -; Genomic_DNA.
DR RefSeq; WP_020916266.1; NC_021900.1.
DR AlphaFoldDB; S5R2W7; -.
DR KEGG; slu:KE3_0431; -.
DR PATRIC; fig|1076934.5.peg.379; -.
DR HOGENOM; CLU_001771_11_2_9; -.
DR Proteomes; UP000015268; 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:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006825; P:copper ion transport; 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; 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; 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 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 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 94..116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 128..145
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 192..211
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 348..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 375..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 690..712
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 718..737
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 3..69
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 745 AA; 80310 MW; FF1E02DE28B7CCCF CRC64;
MEKEEVFVID GMTCAACALT VENAVNKIDH VDSAVVNLTT EKMTVRYNPD LVSEAEIEKA
VVDAGYGACV FNPTTAKSQS ERQSEATHNM WHKFLWSAAF AIPLLYLSMG SMMGMWVPKV
VSMSEHPLIF ALVQLALTLP VMYFGRRFYV NGFRALLKVH PNMDSLVALA TTAAFLYSLY
STYHIILGHV HHVHMLYFES VAVILTLITL GKYFETLSKG RTSDAIQKLL TLSAKEAMVI
RDGVEQKIPI DQVQVGDLIM VKPGEKIPVD GYVVSGHSAI DESMLTGESI PVEKVADDKV
FGASINGQGS LTIRAEKVGD ETLLAQIIKL VEDAQQTKAP IAKIADKVAG VFVPAVMTIA
LITFLFWYFA KGESFVFALQ VAIAILVIAC PCALGLATPT AIMVGTGRGA ENGILYKRGD
VLENAHHIDT MVFDKTGTIT QGKPQVVDVI AYHGDEKSLL VQVASVEKYS EHPLSQAIVE
KASADKLTLE EVENFTSLTG RGLQADLAGK TVYVGNRRLM EELQVDLTAS ETAVLAATQK
GQTPIYISAN EQLIGVITVA DLLKADSKDT VAKLQNQGID VVLLTGDNSN TAQAIAKQAG
IKTVISEVLP DQKSQAIKDL QRQGKMVAMV GDGINDAPAL AVADIGIAVG SGTDIAIESA
DIILMKPEIS DVLRALSISC LTIKVVKENL FWAFIYNILA IPVAMGVLYL FGGPLLNPMI
AGLAMGFSSV SVVLNALRLK YMTLK
//
