ID A0A0S7XLU0_9BACT Unreviewed; 808 AA.
AC A0A0S7XLU0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE SubName: Full=ATPase {ECO:0000313|EMBL:KPJ63366.1};
GN ORFNames=AMS15_00570 {ECO:0000313|EMBL:KPJ63366.1};
OS Planctomycetes bacterium DG_23.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=1703414 {ECO:0000313|EMBL:KPJ63366.1, ECO:0000313|Proteomes:UP000052166};
RN [1] {ECO:0000313|EMBL:KPJ63366.1, ECO:0000313|Proteomes:UP000052166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_23 {ECO:0000313|EMBL:KPJ63366.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
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:KPJ63366.1}.
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; LIZR01000006; KPJ63366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7XLU0; -.
DR STRING; 1703414.AMS15_00570; -.
DR PATRIC; fig|1703414.3.peg.1554; -.
DR Proteomes; UP000052166; 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: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; -; 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; 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 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
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}.
FT TRANSMEM 156..175
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 260..281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 411..432
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 438..459
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 752..771
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 777..800
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..58
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 70..135
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 808 AA; 87115 MW; BD9EB0BC137DC97F CRC64;
MHCASCVLTI ENALKKTPGV SDARVNFSSE KAYVEYDPAK TTLDELHQTI AQAGYKTIEP
KETPEVKGKA TLKLKVIGMD NPHCLGTVDG ALRSLHGIVK KDLFVNQKAT IHYDSSVLSS
DRIKETIKAA GYTPIEEEEV TVDAEKEARQ KEVRSLKIRF TISIILASPL MYFAMATGLK
LPLAPFMIQH MALIQFLLAT PIMLAGYQFF TRGILALIKT KTANMDTLVA LGVGAAYLYS
LYVSAAMWLG STAFTMRNLY YEIAGFLIAF ILLGKLLEAI AKGKTSEAIR KLMGLQAMTA
FVLRNGQEQE IPVEEMTVGD IVIVKPGQKI PVDGILTEGY SSVDESMITG ESIPVEKSEG
SEVIGATINK TGSFKFKATK VGKDTALAQI VKLVEEAQGS KAPIQQFADK VSAYFVPAVV
IIGTVAFVVW LLAGANFLFA LTIFIAVLII ACPCALGLAT PTAVMVGTGI GAENGILIKS
AESLQNAHQI NAIVFDKTGT LTKGQPELTD VIAYGVPEEE VLSLAASVEK NSEHPLGEAI
VKAAQQKNVR LRDVRDFASM TGRGVAAKID GDEILLGNRG LMEDRNIDIS GATQDLERLQ
GEGKTVMLFA TNHRLLGMVA VADTLKEFSK EAVAKLKEMG KQVIMITGDN KRTGEAIARQ
VGIDRVLAEV LPQNKAQEIK KLQEEGLKVA MVGDGINDAP ALTQADIGLA IGTGTDVAIE
SGDVVLIKDD LRDVVMAMDL SRYAMKKIKQ NLFWAFFYNS AGIPIAAGVL YPFTGFLLNP
MIAGAAMAFS SVSVVSNSLL MRRYRKSI
//
