ATSY_SYNP6
ID ATSY_SYNP6 Reviewed; 790 AA.
AC P07893; Q5N145;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Probable copper-transporting ATPase SynA;
DE EC=7.2.2.9;
GN Name=synA; Synonyms=ctaA; OrderedLocusNames=syc1785_d;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 498-790.
RX PubMed=3041005; DOI=10.1016/0022-2836(87)90667-x;
RA Cozens A.L., Walker J.E.;
RT "The organization and sequence of the genes for ATP synthase subunits in
RT the cyanobacterium Synechococcus 6301. Support for an endosymbiotic origin
RT of chloroplasts.";
RL J. Mol. Biol. 194:359-383(1987).
CC -!- FUNCTION: Involved in copper transport.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:10376, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29036, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.9;
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; AP008231; BAD79975.1; -; Genomic_DNA.
DR EMBL; X05925; CAA29364.1; -; Genomic_DNA.
DR RefSeq; WP_011244095.1; NC_006576.1.
DR AlphaFoldDB; P07893; -.
DR SMR; P07893; -.
DR STRING; 269084.syc1785_d; -.
DR EnsemblBacteria; BAD79975; BAD79975; syc1785_d.
DR KEGG; syc:syc1785_d; -.
DR eggNOG; COG2217; Bacteria.
DR OMA; HWMLPAW; -.
DR Proteomes; UP000001175; Chromosome.
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:0043682; F:P-type divalent 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_0000046157"
FT TOPO_DOM 1..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..134
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..416
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..726
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 727..749
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 750..753
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 754..776
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 777..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 cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 28
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
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; 83657 MW; 822B3A9A3F139CDF CRC64;
MPAAIVHSAD PSSTSILVEV EGMKCAGCVA AVERRLQQTA GVEAVSVNLI TRLAKVDYDA
ALIEDPTVLT TEITGLGFRA QLRQDDNPLT LPIAEIPPLQ QQRLQLAIAA FLLIVSSWGH
LGHWLDHPLP GTDQLWFHAL LAIWALLGPG RSILQAGWQG LRCGAPNMNS LVLLGTGSAY
LASLVALLWP QLGWVCFLDE PVMLLGFILL GRTLEEQARF RSQAALQNLL ALQPETTQLL
TAPSSIAPQD LLEAPAQIWP VAQLRAGDYV QVLPGVRIPV 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
