ID A0A101WAJ1_9FLAO Unreviewed; 794 AA.
AC A0A101WAJ1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=ATPase {ECO:0000313|EMBL:KUO69687.1};
GN ORFNames=APF83_09860 {ECO:0000313|EMBL:KUO69687.1};
OS Lutibacter sp. BRH_c52.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=1734397 {ECO:0000313|EMBL:KUO69687.1, ECO:0000313|Proteomes:UP000054346};
RN [1] {ECO:0000313|EMBL:KUO69687.1, ECO:0000313|Proteomes:UP000054346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c52 {ECO:0000313|EMBL:KUO69687.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUO69687.1}.
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; LOEY01000004; KUO69687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101WAJ1; -.
DR Proteomes; UP000054346; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 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; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 733..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 760..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..150
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 794 AA; 88918 MW; 6EA05D59F863ACAB CRC64;
MDINSCYHCG ASCGKSTILF DEKQFCCNGC KTVYEILSIN ELGCYYDLQS TPGTIPSDIK
GKYNYLENED IIEKLLEFND TETSVVEFFI PSIHCSSCIW ILENLTKLNS GVTTSMVNFP
KKTVRITFKN KATNLKQLAE LLTSIGYEPY ISLDDADAKK NKVDKTLIYQ VSVAAFCFGN
IMLLSFPEYF DADEFWLEKY KHVFRWSMFA MAIPVVFYAA KNYYISAYKG LSHKILNIDV
PIALGVSVLF IRSTIEIAFD IGTGFFDSLA GLVFFLLLGK FFQQKTYNFL SFERDYKSYF
PIAVTKLSDG IEKNIPVQAI EKGDRLLIRN QELIPVDGIL INGNASIDYS FVTGESMPVS
KQSGDKLFAG GKQTEGALEM EVINTISQSY LTQLWSNDVF NKTSEHTIKN ITDTISKLFT
INILTISFLG GLFWYFHNHS MVFNVVTAVL IIACPCALAL SAPFAIGNIL RIFGYRKFYL
KNAETVENLA KVDTIIFDKT GTITSADKSN LIFRGESLSK EEIRAVKSVL RASNHPLSRL
VYGHIQEEIL TEKPTYFEEQ LGKGIHAVLN TMDIKLGSAS FVGATSSETN ETAIHLAINN
QFKGSYIFKN SYREGTKEVF ETLAKKYKLV ILSGDNDGER EYLEKLLPKN TLFQFNQKPE
NKLEYIKKLQ QNGEKVMMVG DGLNDAGALA QSNVGIVISE NVNVFSPACD GILDAKFFNK
LPKLLTISNK TMTIIKTSFI LAFCYNVIGL YFALTGVLTP IIAAILMPVS SISIVIFVTI
MTNLAAKKYL KEFS
//