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heavy metal translocating P-type ATPase [Pseudomonas aeruginosa].


LOCUS       WP_010895660             740 aa            linear   BCT 17-NOV-2023
ACCESSION   WP_010895660
VERSION     WP_010895660.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..740
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=78598
     Region          45..105
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(51..53,56)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          141..737
                     /region_name="P-type_ATPase_Cd-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux
                     ATPase; cd07545"
                     /db_xref="CDD:319845"
     Site            order(391,393,699..700,721,725)
                     /site_type="other"
                     /note="putative HM ion binding site [ion binding]"
                     /db_xref="CDD:319845"
     Site            order(435..437,500,516..518,547,587..589,609,612,615,634,
                     637)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319845"
ORIGIN      
        1 mshehadtcc hghghghdhg hrhaprpava aigtlagnae lrwsdlriea mdcpteerli
       61 rdalgrqpav eslefnlmqr llrvqhrfds veplqkliag lgmqavplda gentdgpsqa
      121 pakpwwplal agamalasei vewfglapdw vvaglallai lgaglptyrk gwialknrnl
      181 ninalmsiav tgavligqwp eaamvsvlfa iaelieaksl drarnairgl lqlapeqatv
      241 lvggewkelp akqveleatv rvkpgerial dgevtsgrss vnqapitges lpvekevgep
      301 vfagsingeg aleyrvtrra ddstlariih aveeaqgsra ptqrfvdsfa rvytpvvfli
      361 alatavlppl lfggawldwi yralvllvia cpcalvistp vtivsglsaa arlgilikgg
      421 vflelgrkls wvaldktgti thgkpqqtdy lpiaeadgtd arllaaslaa rsdhpvsrav
      481 anaaeedgla lgvvedlaal pgrgvsgrid gvlyhlgnhr lveelglcsp aleerldale
      541 rqgktvialc dpqrvralfa vadgvkdssr eaihelhald vktlmltgdn phtaaaiaaq
      601 vgidaargnl lpedklreve arqadgsrvg mvgdgindap alaradigfa mgaagtdtai
      661 etagvalmdd dlrklpqfvr lsrtthailv qnitlalgik avflaltlag egtlwmavfa
      721 dmgasllvvf nglrllrkrf