ID A0A1G2CIB3_9BACT Unreviewed; 673 AA.
AC A0A1G2CIB3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE SubName: Full=ATPase P {ECO:0000313|EMBL:OGZ01143.1};
GN ORFNames=A3B13_00210 {ECO:0000313|EMBL:OGZ01143.1};
OS Candidatus Liptonbacteria bacterium RIFCSPLOWO2_01_FULL_45_15.
OC Bacteria; Candidatus Liptonbacteria.
OX NCBI_TaxID=1798649 {ECO:0000313|EMBL:OGZ01143.1, ECO:0000313|Proteomes:UP000176287};
RN [1] {ECO:0000313|EMBL:OGZ01143.1, ECO:0000313|Proteomes:UP000176287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGZ01143.1}.
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DR EMBL; MHKZ01000006; OGZ01143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2CIB3; -.
DR STRING; 1798649.A3B13_00210; -.
DR Proteomes; UP000176287; 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 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; 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; TIGR01512; ATPase-IB2_Cd; 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; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
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 PROSITE; PS00154; ATPASE_E1_E2; 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 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 39..60
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 72..90
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 97..119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 131..148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 282..303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 620..639
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 645..668
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 71372 MW; 56A65E41744BB314 CRC64;
MTLIPLKSKK SNREAEHGDH AASFNKHEGH NSNIFKIKFW ASFALSIPIV LYSGLVSSVF
NWTAPVFPGS AYIQFVLGST VFFYGGWIFL TSARRELGAR LPGMMTLIAI AITTAYAWSV
YATLAGRADN LFWELATLIT IMLLGHWVEM SAVSSAQSAL KEISKLLPDT AEVVRDSVAK
IIPLAELREG DIVLVRPGGK IAADGEVVEG DSSVDESIAT GESKPVSKSI GSEVIAGTIN
GDGILRLKVT KIGERTFLAG VMRLVAEAQS SKSRLQILSD RAAFYLTIVA VAAGTITFIS
WILAGGGTAF AVERLVAVLV IACPHALGLA VPLVASISTT KAARNGFLIK QRLALEAARN
VDVVLFDKTG TLTKGEYGVT DVWAVTGDEK EIMRLAASAD AYSEHPIAKA IVAHALERNI
PLTEIKDFSR IPGKGSQAKI GGALVTIGGA AVVEGKNISL PAGVAEEHKK GKTIIYVLRD
DAFIGVIALA DIIREESREA IKTLKAMGIK VAMVTGDSED VAAWVADELG IDEYFARTMP
DKKSEKIKLL QSGGRRVAMV GDGINDAPAL TQADIGIAIG AGTNVAIESA GIILVKNDPR
DIPKIVALSR FTYAKMIQNL FWAAGYNVVA IPLAAGILAS RGILLSPAIG AVFMSLSTVI
VAINAMLLKG RKL
//