heavy metal translocating P-type ATPase [Listeria monocytogenes].

LOCUS       WP_003723407             737 aa            linear   BCT 24-DEC-2024
ACCESSION   WP_003723407
VERSION     WP_003723407.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 737)
  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 737)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 737)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 737)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
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 11454793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..737
                     /product="heavy metal translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /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=79809
     Region          7..734
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msdkyvrqdl nvfgmtcaac striekslnk adgvekanvn lvtenaavyy dpevtstedl
       61 ikvvkhagyd aaekmskeek davleknfkk evrrfilsal lslpllltmv thipyihema
      121 faetignwin ptiqlvlati vqfyigwrfy dgaykalrgk sanmdvlval gtsaayfysv
      181 veyvrhiidp svmphyyfet savlitlill gkllesyats rttesiagll elqakeatvi
      241 regkewlvpv dslkigdvil vrpgekvpmd aeiisgetsi deamitgepv pvekkpgdsv
      301 igatinfdga fqakitkrme etvlesiirl veeaqgikap iqrladrisg ifvpivlgia
      361 avtfiiwylv tgtvdgslea aiavlviacp calglatpta imagtgkgae sgilfkggeh
      421 lertskvdti vfdktgtlte gklevsdkka andqffpylf lmeqqsehpi akaiikmlep
      481 enmdvsaikq gkirakaghg mtgnlddskv elgayryvss lttipkedde lieswmhagk
      541 tvvamaidgv yagalalsdt prpeakeaiq klkaqgikta icsgdqsvvv enmakdlgid
      601 mffaeqlpnd ksalveklqq dghivafvgd gindapalaa sdigisigtg tdiaietgdv
      661 tlvshrltli petielskat mrnirqnffw alayncagip iaalgllapw vaglamafss
      721 vsvvtnalrl krykfks