ID   HDA_ECOL5               Reviewed;         233 AA.
AC   Q0TEZ2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=DnaA regulatory inactivator Hda {ECO:0000255|HAMAP-Rule:MF_01158};
GN   Name=hda {ECO:0000255|HAMAP-Rule:MF_01158}; OrderedLocusNames=ECP_2498;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- FUNCTION: Mediates the interaction of DNA replication initiator protein
CC       DnaA with DNA polymerase subunit beta sliding clamp (dnaN). Stimulates
CC       hydrolysis of ATP-DnaA to ADP-DnaA, rendering DnaA inactive for
CC       reinitiation, a process called regulatory inhibition of DnaA or RIDA
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The active form seems to be an ADP-bound monomer. Forms the
CC       RIDA complex (regulatory inactivation of DnaA) of ATP-DnaA, ADP-Hda and
CC       the DNA-loaded beta sliding clamp (dnaN). {ECO:0000255|HAMAP-
CC       Rule:MF_01158}.
CC   -!- SIMILARITY: Belongs to the DnaA family. HdA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01158}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABG70487.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000247; ABG70487.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001307333.1; NC_008253.1.
DR   AlphaFoldDB; Q0TEZ2; -.
DR   SMR; Q0TEZ2; -.
DR   STRING; 362663.ECP_2498; -.
DR   EnsemblBacteria; ABG70487; ABG70487; ECP_2498.
DR   GeneID; 66673639; -.
DR   KEGG; ecp:ECP_2498; -.
DR   HOGENOM; CLU_072265_1_1_6; -.
DR   OMA; DWGQIYR; -.
DR   Proteomes; UP000009182; Chromosome.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0032297; P:negative regulation of DNA-templated DNA replication initiation; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01158; Hda; 1.
DR   InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR   InterPro; IPR013317; DnaA.
DR   InterPro; IPR017788; Hda.
DR   InterPro; IPR022864; Hda_Enterobact.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   PRINTS; PR00051; DNAA.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03420; DnaA_homol_Hda; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA replication inhibitor.
FT   CHAIN           1..233
FT                   /note="DnaA regulatory inactivator Hda"
FT                   /id="PRO_1000065562"
SQ   SEQUENCE   233 AA;  26633 MW;  D25C7CDF31DAF7DC CRC64;
     MNTPAQLSLP LYLPDDETFA SFWPGDNSSL LAALQNVLRQ EHSGYIYLWA REGAGRSHLL
     HAACAELSQR GDAVGYVPLD KRTWFVPEVL DGMEHLSLVC IDNIECIAGD ELWEMAIFDL
     YNRILESGKT RLLITGDRPP RQLNLGLPDL ASRLDWGQIY KLQPLSDEDK LQALQLRARL
     RGFELPEDVG RFLLKRLDRE MRTLFMTLDQ LDRASITAQR KLTIPFVKEI LKL