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Database: UniProt
Entry: U7NJ63_9GAMM
LinkDB: U7NJ63_9GAMM
Original site: U7NJ63_9GAMM 
ID   U7NJ63_9GAMM            Unreviewed;       712 AA.
AC   U7NJ63;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=ATPase {ECO:0000313|EMBL:ERS82434.1};
GN   ORFNames=Q671_11735 {ECO:0000313|EMBL:ERS82434.1};
OS   Halomonas sp. PBN3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1397528 {ECO:0000313|EMBL:ERS82434.1, ECO:0000313|Proteomes:UP000017115};
RN   [1] {ECO:0000313|EMBL:ERS82434.1, ECO:0000313|Proteomes:UP000017115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBN3 {ECO:0000313|EMBL:ERS82434.1,
RC   ECO:0000313|Proteomes:UP000017115};
RX   PubMed=24356826;
RA   Overholt W.A., Green S.J., Marks K.P., Venkatraman R., Prakash O.,
RA   Kostka J.E.;
RT   "Draft genome sequences for oil-degrading bacterial strains from beach
RT   sands impacted by the deepwater horizon oil spill.";
RL   Genome Announc. 1:e01015-13(2013).
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:ERS82434.1}.
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DR   EMBL; AXCA01000198; ERS82434.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7NJ63; -.
DR   PATRIC; fig|1397528.3.peg.2921; -.
DR   eggNOG; COG2217; Bacteria.
DR   Proteomes; UP000017115; 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   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; 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; TIGR01512; ATPase-IB2_Cd; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR   PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
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; 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|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        82..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        302..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        336..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        646..671
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          1..59
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   712 AA;  73975 MW;  C7B083DE143B852C CRC64;
     MDCGGCERKV EAALGRLEGI EAVSASSVTG SVTVHPQPHS APSHQTIERI LNELGYRLAA
     DTEKDGSDTP PAPWWQTAKG RLVLVTGGLL ALALVLRMTW PVLGGWPFVA ATLVGLVPIA
     QGAWGALKMR NPFTIEMLMS IAALGALAID AAAEAAVVVF LFAVGELLEG VAASRARRSI
     SALADLTPST ARLMEDGDTR EVSAASLTPG QRVLVRPGDR VPCDGRILTG ESDLDESPIN
     GESVPRSRAP GDDVFAGTVN LDAALEVEVT RGAEDNTIAR VIRLVEEAQA AKAPVARFID
     RFAFYYMPAV VGLALLMAVV PPLVSTMAWS ESVYRALALL LIACPCALVI STPAAIAAGL
     SAGARRGLLI KGGAVLEQLG KLRTVALDKT GTLTAGTPRV TDVEDWATGQ GENEILRLAA
     AMERDSSHPI ATAILAHAQQ QGLSLPLASE SRALSGLGVA GRVEGRELGL VTPRHLAERV
     TLDHDLNVRI AELEGAGKSL ALLVESERPL GLIAVRDEPR EDAREGLAAL SRLGVEAVML
     SGDNARTAAA IGGSLGIEAH GELMPEDKAR RVQQWQATGR GPVGKVGDGI NDAPALAAAD
     VGIAMGGGTD VALETADAAL LKNRVTGIAE LIDLSRATLR NVKTNVALAL GLKAIFLVTT
     ALGITGMWIA VMADTGATVL VTLNAMRLLG YRFSPGTAMS GSASPRYQAA TS
//
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