ATCS_SYNY3
ID ATCS_SYNY3 Reviewed; 745 AA.
AC P73241;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Probable copper-transporting ATPase PacS;
DE EC=7.2.2.8;
GN Name=pacS; OrderedLocusNames=sll1920;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: May play a role in the osmotic adaptation. {ECO:0000250}.
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 -!- INTERACTION:
CC P73241; P73213: ssr2857; NbExp=3; IntAct=EBI-904982, EBI-904975;
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; BA000022; BAA17268.1; -; Genomic_DNA.
DR PIR; S75354; S75354.
DR PDB; 2GCF; NMR; -; A=1-73.
DR PDB; 2XMW; X-ray; 1.80 A; A=1-71.
DR PDB; 4A48; X-ray; 1.40 A; A/B=2-70.
DR PDB; 4A4J; X-ray; 1.25 A; A=2-70.
DR PDBsum; 2GCF; -.
DR PDBsum; 2XMW; -.
DR PDBsum; 4A48; -.
DR PDBsum; 4A4J; -.
DR AlphaFoldDB; P73241; -.
DR SMR; P73241; -.
DR DIP; DIP-35107N; -.
DR IntAct; P73241; 11.
DR STRING; 1148.1652345; -.
DR PaxDb; P73241; -.
DR EnsemblBacteria; BAA17268; BAA17268; BAA17268.
DR KEGG; syn:sll1920; -.
DR eggNOG; COG2217; Bacteria.
DR InParanoid; P73241; -.
DR OMA; ITFFGWM; -.
DR PhylomeDB; P73241; -.
DR EvolutionaryTrace; P73241; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0015677; P:copper ion import; TAS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Copper; Copper transport;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..745
FT /note="Probable copper-transporting ATPase PacS"
FT /id="PRO_0000046161"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..372
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..687
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 708..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 720..738
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 739..745
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 3..68
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 428
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
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 633
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 637
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:4A4J"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:4A4J"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:4A4J"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:4A4J"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:4A4J"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2GCF"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:4A4J"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4A4J"
SQ SEQUENCE 745 AA; 79950 MW; 40831F66621735FB CRC64;
MAQTINLQLE GMRCAACASS IERAIAKVPG VQSCQVNFAL EQAVVSYHGE TTPQILTDAV
ERAGYHARVL KQQVLSSQQT EDRKPVFSAK LVTGLVISAV LFFGSLPMML GVNIPHFPHI
FHDPWLQWLL ATPVQFWSGA EFYRGAWKSV RTRSATMDTL VALGTSAAYF YSVAITLFPQ
WLTSQGLAAH VYFEAAAVVI TLILLGRSLE QRARRETSAA IRKLMGLQPQ TALVKRGEHW
ETVAIAELAI NDVVRVRPGE KIPVDGVVVA GNSTVDESLV TGESFPVDKT VGTEVIGATL
NKSGSLDIQV SKLGQDSVLA QIIQLVQQAQ ASKAPIQHFV DRITHWFVPT VIVVAIAAFC
IWWLTTGNIT LAVLTLVEVL IIACPCALGL ATPTSVMVGT GKGAEYGVLI KEASSLEMAE
KLTAIVLDKT GTLTQGKPSV TNFFTLSPTS TEESLQLIQW AASVEQYSEH PLAEAVVNYG
QSQQVSLLEI DNFQAIAGCG VAGQWQGQWI RLGTSNWLTD LGVTGTEHQP WQSQAQQWEK
EQKTVIWLAV DTEVKALLAI ADAIKPSSPQ VVQALKKLGL SVYMLTGDNQ ATAQAIADTV
GIRHVLAQVR PGDKAQQVEQ LQQKGNIVAM VGDGINDAPA LAQADVGIAI GTGTDVAIAA
SDITLIAGDL QGILTAIKLS RATMGNIRQN LFFAFIYNVI GIPVAAGLFY PLFGLLLNPI
LAGAAMAFSS VSVVTNALRL KKFCP
