ID A0A3S5K2A0_CHLFR Unreviewed; 798 AA.
AC A0A3S5K2A0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:RUR83825.1};
GN ORFNames=PCC6912_20680 {ECO:0000313|EMBL:RUR83825.1};
OS Chlorogloeopsis fritschii PCC 6912.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Chlorogloeopsidaceae;
OC Chlorogloeopsis.
OX NCBI_TaxID=211165 {ECO:0000313|EMBL:RUR83825.1, ECO:0000313|Proteomes:UP000268857};
RN [1] {ECO:0000313|EMBL:RUR83825.1, ECO:0000313|Proteomes:UP000268857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6912 {ECO:0000313|EMBL:RUR83825.1,
RC ECO:0000313|Proteomes:UP000268857};
RX PubMed=30590650;
RA Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA Neumann-Schaal M., Petersen J.;
RT "Day and night: Metabolic profiles and evolutionary relationships of six
RT axenic non-marine cyanobacteria.";
RL Genome Biol. Evol. 0:0-0(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUR83825.1}.
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DR EMBL; RSCJ01000006; RUR83825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S5K2A0; -.
DR STRING; 211165.GCA_000317285_00092; -.
DR Proteomes; UP000268857; Unassembled WGS sequence.
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:0005507; F:copper ion binding; IEA:InterPro.
DR CDD; cd00371; HMA; 2.
DR Gene3D; 3.30.70.100; -; 2.
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; IPR006122; HMA_Cu_ion-bd.
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; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR00003; copper ion binding protein; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00022796};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Ion transport {ECO:0000256|ARBA:ARBA00022796};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000268857};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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:ARBA00022796}.
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 149..171
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 177..195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 332..351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 357..376
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 693..711
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 4..70
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 730..796
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 798 AA; 85966 MW; FE2FDD4033F25F07 CRC64;
MATETVQMKV SGMMCSFCTM SIEQALKRHP GINSVMVNLV HGIVLVEADT SQINEEELKT
AVEKLGYSVS ETEMQQYVTD EALFKLLGQR GIIGMALSLI DLLIDPLNLF QLPPQPRAWF
SLAVAAVVLL WVGYPILRKT LMALQQRVIN ANVLLSAGAW GSFIIGTLSL VDPQWPNFLP
VAAWLMSLHL FFGYFKLDTR KKASEAVRKL LSLQPPRARV LRGGQTVDVL TNEVVVGETL
VVRPGERIPL DGEVIEGIAS VDESSFTGES VPSTKGVNAK VIGGTLNLDG VLNIRVTKIG
QDSFLSQIVR LMTQIAERKP PLELLADRLM NYYGPVVFIV AGLAFTGWVM FSGDYTKATL
VLLTTIIMGY PCALGITTPM LSAIAGGKGI SIGLLVKASE VFHELSVVDM VVFDKTGTLT
YGRPTVTNVE TFGSERIETL TLASAIEEPS EHPIGQAIRF FALREGTQPA AVKEFRAAPG
KGVEARLGET EVLAGKPSFV EERGVSLTAQ VRARIDALSN EGKTVVVLAR GKEAIGIFAL
QDTPRRGAQR LFEKLRQRGI KTVMLTGDAQ RVAEAIGNKL GVDEVRAELL PTDKVAAIET
LQNAGRKVAM VGDGINDAPA LAQANIGIAL GAGTDVAIES AGVILIGDRL NDVLSALILG
KASYRTMTGN VIVAVLFNLV GMGLAAMGFI TPTLAITIMV LSIFAILLNT LRIRGIDLQR
EDLPELEPLA EQEFLVPGMV CEGCASKIST VLTSLVGVQE VKPKVPQKRV YVRYEPTQVQ
EEQLKAALDQ VGFTAIEA
//
