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Database: UniProt
Entry: A0A076H475_9SYNE
LinkDB: A0A076H475_9SYNE
Original site: A0A076H475_9SYNE 
ID   A0A076H475_9SYNE        Unreviewed;       766 AA.
AC   A0A076H475;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=P-type ATPase transporter for copper {ECO:0000313|EMBL:AII44600.1};
GN   ORFNames=KR100_14740 {ECO:0000313|EMBL:AII44600.1};
OS   Synechococcus sp. KORDI-100.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1280380 {ECO:0000313|EMBL:AII44600.1, ECO:0000313|Proteomes:UP000028591};
RN   [1] {ECO:0000313|EMBL:AII44600.1, ECO:0000313|Proteomes:UP000028591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KORDI-100 {ECO:0000313|EMBL:AII44600.1,
RC   ECO:0000313|Proteomes:UP000028591};
RA   Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT   "Genome sequence of Synechococcus sp. KORDI-100.";
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
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; CP006269; AII44600.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A076H475; -.
DR   STRING; 1280380.KR100_14740; -.
DR   KEGG; synk:KR100_14740; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_11_2_3; -.
DR   Proteomes; UP000028591; 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   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   InterPro; IPR044492; P_typ_ATPase_HD_dom.
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   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
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   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 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:UP000028591};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
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        97..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        128..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        161..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        188..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        344..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        402..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        714..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        745..763
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          3..69
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   766 AA;  81233 MW;  D0F068C19F79C572 CRC64;
     MLQTVVLDVE GMKCGGCVRS VERTLLEQPG VERADVNLVS RAAWLDLADS EGSVEAVLKA
     LADRGFPARE RSLEPVSGPS AAEDVRGLNW WRQWRQLMVA LVLLLLSVLG HLSEAGHLSL
     PLIGRLPFHA TLATVALLGP GRPILVGGFK AARAGAPSMD TLVGLGVSSA YLASLAALIW
     PSVGWPCFFN EPVMLLGFVL LGRFLEERAR FRTGQALQQL AQLQPDTARL LMADGVMREV
     RVGALRPGER VQLLAGDRVP VDGVVVEGCS AVDVSSLTGE PLPLDASPGT ELASGSLNLE
     SSLVIEVTRV GSETALARII RLVEQAQARR APIQGLADRV AGRFCYGVIA FAIAVFLFWW
     LIGAELWPQV LHASSPGMVH GHGHQAGLGS GAETSIGLAL KLAIAVLVVA CPCALGLATP
     TVITVATGLA ARRGWLYRGG DVIETAAAVK QVVFDKTGTL TLGRPLVTAV HAENPNHLLQ
     LAASLESDSR HPLAYALLQE AQRRELDLLP VSDVRTVAGE GLKGVVGRDL EVCVGRPEWL
     TGQGLAWSDP FSLMQQESGG TPVTGTVVAV AEGTSILGFV EIEDQLRSDV SMALKQLRDQ
     GLELAMFSGD RESAVRRLGQ TLGFSEEELG WQMRPEQKLA RLEQLRREQP VAMVGDGIND
     APALAAADLG VAIGTGTQIA QDTAGMVLLG DRLDNLPDAL RLARRTLAKV RQNLFWAFGY
     NLIALPIAAG VLLPSHGLLL SPPLAALLMA LSSITVVVNA LALRPA
//
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