ID A0A518ALZ3_9BACT Unreviewed; 811 AA.
AC A0A518ALZ3;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE SubName: Full=Copper-exporting P-type ATPase A {ECO:0000313|EMBL:QDU55752.1};
GN Name=copA_2 {ECO:0000313|EMBL:QDU55752.1};
GN ORFNames=Pan181_19470 {ECO:0000313|EMBL:QDU55752.1};
OS Aeoliella mucimassa.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Lacipirellulaceae;
OC Aeoliella.
OX NCBI_TaxID=2527972 {ECO:0000313|EMBL:QDU55752.1, ECO:0000313|Proteomes:UP000315750};
RN [1] {ECO:0000313|EMBL:QDU55752.1, ECO:0000313|Proteomes:UP000315750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pan181 {ECO:0000313|EMBL:QDU55752.1,
RC ECO:0000313|Proteomes:UP000315750};
RA Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA Labrenz M., Spormann A.M., Op den Camp H., Overmann J., Amann R.,
RA Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT characterization uncovers novel biology.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
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; CP036278; QDU55752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A518ALZ3; -.
DR KEGG; amuc:Pan181_19470; -.
DR OrthoDB; 211392at2; -.
DR Proteomes; UP000315750; 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; IPR021993; ATPase-cat-bd.
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; 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:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR Pfam; PF12156; ATPase-cat_bd; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
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; 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|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000315750};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 176..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 211..232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 244..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 272..290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 424..445
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 457..484
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 763..782
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 788..808
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 91..157
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 811 AA; 85334 MW; 74F7C4F4F24F8EFB CRC64;
MTAVPEVVCD HCGLPVPRGL VDPDAELQFC CNGCRTVYGM LHEHGLDEFY HVRSVVDAPK
QAVRSTTQKY EAYDDPAFLA KNGRPLAGGY LSIDLRLEGV HCAACMWLVE RLPKLIAGLA
SAKLQMRDAV VRLTWDPAET KLSTIATALD RLGYPAHPAR DTTASDIHRR SEHAQLIRLG
VAGACAGNTM LLAIALYAGQ FAGIEDEFKN LFRYVSALIG ALALVWPGSV FFRGAISSLR
ARSATLDVPI ALALAAGGLA GVVNAIRGTG EIYFDSLSVL VFLLLVGRWF QARQQRWADE
AVGLLNSFTP STCRVVREDL VIEITTDSLV TGDIVEVLSG GVLPADGVLV EGQSSLNRSL
LTGESRPEPV VVGDDVFAGT QNIGSPIRLR VESIGEATRV GQLMDMVAEG VREKPPIIQF
TDRAAGWFVT IVVSVATLTF IVWAATATLA EAVEHTIALL IVACPCALGL ATPLTLAVAI
GLAAKRHILI KNAGVFEILA GGGRMLLDKT GTVTRGRPTL IEWSGAEWLA PIVAHAESHS
THPIATAFVE AFGSQPIEDR QLVPRDIEEQ HGGGLRGMTG GDRLLVGSPR FLAAEGVTID
AAQADRIASQ EQAGRTMIGV AVAGELLATA ALGDRLHDDS VEAFQQLESL GWHPSILSGD
ATGVVASVAE QLSIPSDKAL GGVTPEQKLA LVTAERSEPT VMIGDGVNDS AALAAADVGI
AVEGGAEASL AAADVYIAAP GLSPVVDLVR LARRTRRTVR QNLVLALAYN TLAVSLAAAG
WITPLVAAIL MPISSATVLA SAMSITLGGE R
//
