ID   HDA_ECOUT               Reviewed;         233 AA.
AC   Q1R8P2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=DnaA regulatory inactivator Hda {ECO:0000255|HAMAP-Rule:MF_01158};
GN   Name=hda {ECO:0000255|HAMAP-Rule:MF_01158}; OrderedLocusNames=UTI89_C2812;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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=ABE08272.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000243; ABE08272.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001307333.1; NZ_CP064825.1.
DR   AlphaFoldDB; Q1R8P2; -.
DR   SMR; Q1R8P2; -.
DR   EnsemblBacteria; ABE08272; ABE08272; UTI89_C2812.
DR   GeneID; 66673639; -.
DR   KEGG; eci:UTI89_C2812; -.
DR   HOGENOM; CLU_072265_1_1_6; -.
DR   OMA; DWGQIYR; -.
DR   Proteomes; UP000001952; 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_1000065563"
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