MULTISPECIES: ATP-binding protein [Enterobacteriaceae].

LOCUS       WP_001302026             362 aa            linear   BCT 23-DEC-2024
ACCESSION   WP_001302026
VERSION     WP_001302026.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 362)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 362)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
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 10543770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..362
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39553
     Region          78..220
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
     Site            83..90
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(84..91,156,203)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            152..157
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Site            219
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
ORIGIN      
        1 mspqnnhlqr ppaavlyade laklkqndna pcppgwqlsl paarafilgd saqnisrkvv
       61 ispsaverml vtlatgrglm lvgepgtaks llsellatsi sgdagltiqg gasttedqik
      121 ygwnyallin hgpstealvp aplyqgmrdg kivrfeeitr tplevqdcll gmlsdrvmtv
      181 peltgeasql yaregfniia tantrdrgvn emsaalkrrf dfetvfpimd faqelelvas
      241 asarllahsg iphkvpdavl ellvrtfrdl rangekktsm dtltaimsta eavnvahavg
      301 vrawflanra gepadlvdci agtivkdnee drarlrryfe qrvathkeah wqayyqarhr
      361 lp