ID   ATSY_SYNE7              Reviewed;         790 AA.
AC   P37385; Q31KS2;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Probable copper-transporting ATPase SynA;
DE            EC=7.2.2.8;
GN   Name=synA; OrderedLocusNames=Synpcc7942_2317;
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=7937823; DOI=10.1073/pnas.91.20.9651;
RA   Phung L.T., Ajlani G., Haselkorn R.;
RT   "P-type ATPase from the cyanobacterium Synechococcus 7942 related to the
RT   human Menkes and Wilson disease gene products.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:9651-9654(1994).
RN   [2]
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: Involved in copper transport.
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; U04356; AAB82020.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB58347.1; -; Genomic_DNA.
DR   RefSeq; WP_011378404.1; NC_007604.1.
DR   AlphaFoldDB; P37385; -.
DR   SMR; P37385; -.
DR   STRING; 1140.Synpcc7942_2317; -.
DR   PRIDE; P37385; -.
DR   EnsemblBacteria; ABB58347; ABB58347; Synpcc7942_2317.
DR   KEGG; syf:Synpcc7942_2317; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_0_3_3; -.
DR   OMA; HWMLPAW; -.
DR   OrthoDB; 237367at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_2317-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   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..790
FT                   /note="Probable copper-transporting ATPase SynA"
FT                   /id="PRO_0000046158"
FT   TOPO_DOM        1..105
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..136
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..198
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..358
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        359..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        382..420
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        439..723
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        724..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        744..755
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        756..774
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        775..790
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          14..81
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   ACT_SITE        476
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         25
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         28
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         669
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         673
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
SQ   SEQUENCE   790 AA;  83695 MW;  FA5B7BFEDF4C3793 CRC64;
     MPAAIVHSAD PSSTSILVEV EGMKCAGCVA AVERRLQQTA GVEAVSVNLI TRLAKVDYDA
     ALIEDPTVLT TEITGLGFRA QLRQDDNPLT LPIAEIPPLQ QQRLQLAIAA FLLIVSSWGH
     LGHWLDHPLP GTDQLWFHAL LATWALLGPG RSILQAGWQG LRCGAPNMNS LVLLGTGSAY
     LASLVALLWP QLGWVCFFDE PVMLLGFILL GRTLEEQARF RSQAALQNLL ALQPETTQLL
     TAPSSIAPQD LLEAPAQIWP VAQLRAGDYV QVLPGDRIPV DGCIVAGQST LDTAMLTGEP
     LPQPCQVGDR VCAGTLNLSH RLVIRAEQTG SQTRLAAIVR CVAEAQQRKA PVQRFADAIA
     GRFVYGVCAI AALTFGFWAT LGSRWWPQVL QQPLPGLLIH APHHGMEMAH PHSHSPLLLA
     LTLAISVLVV ACPCALGLAT PTAILVATGL AAEQGILVRG GDVLEQLARI KHFVFDKTGT
     LTQGQFELIE IQPLADVDPD RLLQWAAALE ADSRHPLATA LQTAAQAANL APIAASDRQQ
     VPGLGVSGTC DGRSLRLGNP TWVQVATAKL PTGSAAATSI WLADDQQLLA CFWLQDQPRP
     EAAEVVQALR SRGATVQILS GDRQTTAVAL AQQLGLESET VVAEVLPEDK AAAIAALQSQ
     GDAVAMIGDG INDAPALATA AVGISLAAGS DIAQDSAGLL LSRDRLDSVL VAWNLSQMGL
     RTIRQNLTWA LGYNVVMLPL AAGAFLPAYG LALTPAIAGA CMAVSSLAVV SNSLLLRYWF
     RRSLNHSVSV