ATCS_SYNE7
ID ATCS_SYNE7 Reviewed; 747 AA.
AC P37279; Q8KPV5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Probable copper-transporting ATPase PacS;
DE EC=7.2.2.8;
GN Name=pacS; OrderedLocusNames=Synpcc7942_1570; ORFNames=sed0002;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8370468; DOI=10.1016/0014-5793(93)80928-n;
RA Kanamaru K., Kashiwagi S., Mizuno T.;
RT "The cyanobacterium, Synechococcus sp. PCC7942, possesses two distinct
RT genes encoding cation-transporting P-type ATPases.";
RL FEBS Lett. 330:99-104(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., Gonzalez A.,
RA Salinas I., McMurtry S., Golden S.S., Youderian P.;
RT "Synechococcus elongatus PCC7942 cosmid 6C3.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in the osmotic adaptation.
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; D16437; BAA03907.1; -; Genomic_DNA.
DR EMBL; AY120852; AAM82673.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57600.1; -; Genomic_DNA.
DR RefSeq; WP_011378089.1; NC_007604.1.
DR AlphaFoldDB; P37279; -.
DR SMR; P37279; -.
DR STRING; 1140.Synpcc7942_1570; -.
DR PRIDE; P37279; -.
DR EnsemblBacteria; ABB57600; ABB57600; Synpcc7942_1570.
DR KEGG; syf:Synpcc7942_1570; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_3; -.
DR OMA; ITFFGWM; -.
DR OrthoDB; 237367at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1570-MON; -.
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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00403; HMA; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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; 2.
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..747
FT /note="Probable copper-transporting ATPase PacS"
FT /id="PRO_0000046160"
FT TOPO_DOM 1..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..132
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..378
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..720
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 721..739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 740..747
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 3..69
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 434
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 17
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 634
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 638
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT CONFLICT 366
FT /note="V -> L (in Ref. 1; BAA03907)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="L -> M (in Ref. 1; BAA03907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 747 AA; 79700 MW; 125EFF764BEF17D9 CRC64;
MVNQQTLTLR GMGCAACAGR IEALIQALPG VQECSVNFGA EQAQVCYDPA LTQVAAIQAA
IEAAGYHAFP LQDPWDNEVE AQERHRRARS QRQLAQRVWV SGLIASLLVI GSLPMMLGIS
IPGIPMWLHH PGLQLGLTLP VLWAGRSFFI NAWKAFRQNT ATMDTLVAVG TGAAFLYSLA
VTLFPQWLTR QGLPPDVYYE AIAVIIALLL LGRSLEERAK GQTSAAIRQL IGLQAKTARV
LRQGQELTLP ITEVQVEDWV RVRPGEKVPV DGEVIDGRST VDESMVTGES LPVQKQVGDE
VIGATLNKTG SLTIRATRVG RETFLAQIVQ LVQQAQASKA PIQRLADQVT GWFVPAVIAI
AILTFVLWFN WIGNVTLALI TAVGVLIIAC PCALGLATPT SIMVGTGKGA EYGILIKSAE
SLELAQTIQT VILDKTGTLT QGQPSVTDFL AIGDRDQQQT LLGWAASLEN YSEHPLAEAI
VRYGEAQGIT LSTVTDFEAI PGSGVQGQVE GIWLQIGTQR WLGELGIETS ALQNQWEDWE
AAGKTVVGVA ADGHLQAILS IADQLKPSSV AVVRSLQRLG LQVVMLTGDN RRTADAIAQA
VGITQVLAEV RPDQKAAQVA QLQSRGQVVA MVGDGINDAP ALAQADVGIA IGTGTDVAIA
ASDITLISGD LQGIVTAIQL SRATMTNIRQ NLFFAFIYNV AGIPIAAGIL YPLLGWLLSP
MLAGAAMAFS SVSVVTNALR LRQFQPR
