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Database: UniProt
Entry: A0A1Y5EIX8_9GAMM
LinkDB: A0A1Y5EIX8_9GAMM
Original site: A0A1Y5EIX8_9GAMM 
ID   A0A1Y5EIX8_9GAMM        Unreviewed;       806 AA.
AC   A0A1Y5EIX8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=ATPase P {ECO:0000313|EMBL:OUR82479.1};
GN   ORFNames=A9Q82_06620 {ECO:0000313|EMBL:OUR82479.1};
OS   Cycloclasticus sp. 46_120_T64.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Cycloclasticus.
OX   NCBI_TaxID=1856281 {ECO:0000313|EMBL:OUR82479.1, ECO:0000313|Proteomes:UP000195872};
RN   [1] {ECO:0000313|Proteomes:UP000195872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hu P., Dubinsky E.A., Probst A.J., Wang J., Sieber C.M.K., Tom L.M.,
RA   Gardinali P., Banfield J.F., Atlas R.M., Andersen G.L.;
RT   "Simulation of Deepwater Horizon oil plume reveals substrate specialization
RT   within a complex community of hydrocarbon-degraders.";
RL   Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2017).
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:OUR82479.1}.
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DR   EMBL; MAAM01000009; OUR82479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5EIX8; -.
DR   Proteomes; UP000195872; 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   GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR   CDD; cd00371; HMA; 1.
DR   CDD; cd02079; P-type_ATPase_HM; 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; IPR017969; Heavy-metal-associated_CS.
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; 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: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   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; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 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|ARBA:ARBA00022723,
KW   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        173..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        209..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        246..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        270..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        455..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        752..769
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        775..793
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          89..155
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   806 AA;  87978 MW;  245892A4D9ABF979 CRC64;
     MVNPLNNSTV CYHCGEAVPR AQNWGIHFDG EWRAMCCPGC ASVAEAIIDN GLADFYQKRT
     AFSESATLIP EPLSHYDSPA ADGMGGEINE VSLIIEGISC SACIWLLERH VRQLNGVASF
     KINYATRRAQ LEFCLDSILL SEVLTAIRAI GYRALPYDAN KQFLVLQAER KDFIGRIGVA
     LLFSMQVMMI TLGVYMAGID TIETQMLSFL RWISAFLSLP VILYSAKPFL VAAYRDMKNA
     MPGMDVPVAL GISLGFIASV WNTWLLAGDT YYESVCMFIL FLLLARYVEF LTRWYAVSSS
     ERLTQAIPVV AKKLLSDGSL ESVAAKTLQL GDEIQINPGD VIPADSLIVS GTSQVDESIL
     TGENEPINKS VGDTVLGGSH NLQHSLVAKV SCVGKASTLS TISRLIDRAH SEKPNWVELA
     DRYASVFVSM VVLLTVGTAW YGFSQGAEDW FSTALSVLVV TCPCALSLAT PTAYTAAMSA
     LFNKGIIITK GQALDKLASI KHVIFDKTGT LTQGVMRITH YQQLAQLEYQ ECLDLAISLE
     AFSEHPIARA FKRERQDKVY QPQQVKHVNG AGLMANINQQ DYYLGSWVYI AGVLALEEEP
     VQMSGSLVYL ATAKQLLAVF EIEDDIRQGA VSTVTWLQQQ GKVLHLVSGD RATPVDWLAA
     KLGIERVKSN ASPVDKLNEI ECLQQRGDPA VMIGDGVNDA PIMAKADVSI SVSGASQLAR
     SSSDILLMGD DMSALRDVFA LSSQTRRVIK QNMCWALVYN IGALPLAMAG QVEPWQAALG
     MSVSSLVVVL NSFRLRMLRP AGQEND
//
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