ID K9RR58_SYNP3 Unreviewed; 748 AA.
AC K9RR58;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Copper/silver-translocating P-type ATPase {ECO:0000313|EMBL:AFY59764.1};
GN OrderedLocusNames=Syn6312_0541 {ECO:0000313|EMBL:AFY59764.1};
OS Synechococcus sp. (strain ATCC 27167 / PCC 6312).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=195253 {ECO:0000313|EMBL:AFY59764.1, ECO:0000313|Proteomes:UP000010379};
RN [1] {ECO:0000313|Proteomes:UP000010379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27167 / PCC 6312 {ECO:0000313|Proteomes:UP000010379};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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; CP003558; AFY59764.1; -; Genomic_DNA.
DR RefSeq; WP_015123308.1; NC_019680.1.
DR AlphaFoldDB; K9RR58; -.
DR STRING; 195253.Syn6312_0541; -.
DR KEGG; syne:Syn6312_0541; -.
DR PATRIC; fig|195253.3.peg.563; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_3; -.
DR OrthoDB; 438550at2; -.
DR Proteomes; UP000010379; 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 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 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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000010379};
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:ARBA00022448}.
FT TRANSMEM 96..117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 129..147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 159..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 194..213
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 347..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 375..396
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 688..710
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 716..735
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..66
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 748 AA; 80022 MW; 65AC9A2155FF3D1E CRC64;
MITLQLTGVR CGACVQTITN AIQALPGVRE CHVNFATTQA SVELDPTLTT IADLEQAVQA
VGYGATYIED PLALLMDSTT ENQAWRQSQR QLRQQVYWGS GLSILIVLGA LPMMLGWDPG
IPQFLQSAWV QALLATPIQF WVGGAFYRQA WIAAQHRTAT MDTLVSLGTS AAYGYSLVLT
FFPAWAAQLG LDHHVYFEVA AIVITLVLLG RYLEQRAKRQ TSQSIRQLIG LQPQTARVVR
PEGDLEIATT AIQVGDVVLI RPGEKIPLDG IVLGGQSNVD EALVTGESQP VFKQPGDAVI
GATLNQSGSL QVQVTKVGRE TFLAQMVQLV QQAQNSRAPI QRRADQVMAW FVPVVIGIAL
VTFLAWWLLT GNLTLALFTL IQVLIIACPC ALGLATPTSI MVGTGKGAEY GILIKGADSL
ELAAKIQTIV LDKTGTLTQG KPTVTHWLTR PDLTTPETQT LIAQTAAVER LSEHPLAQAI
VNYAQSQAVP IPDAEMFQAW PGEGVQGNVN QNFVQVGSLT WLESLHIPAS FLPPALAQDH
SWIGIAINGE MQGLVGITDS LKPSSSSVVQ TLQRMGLKVV MLTGDRWDTA QAIAAEVGIK
EVLAEVKPAA KAAMIEKLQA QGQIVAMVGD GINDAPALAQ ANVGIAIGTG TDVAIAASDI
TLISGDLQAI VTAIQLSRAT LRNIHQNLFF ALIYNGIGIP VAAGLFYPIW GWLLNPILAG
GAMAFSSISV VTNALRLQGF QPDQYPSR
//
