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Database: UniProt
Entry: A0A1G2CIB3_9BACT
LinkDB: A0A1G2CIB3_9BACT
Original site: A0A1G2CIB3_9BACT 
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
//
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