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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//