ID   HDA_YERPS               Reviewed;         235 AA.
AC   Q668E8;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=DnaA regulatory inactivator Hda {ECO:0000255|HAMAP-Rule:MF_01158};
GN   Name=hda {ECO:0000255|HAMAP-Rule:MF_01158}; OrderedLocusNames=YPTB2792;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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}.
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DR   EMBL; BX936398; CAH22030.1; -; Genomic_DNA.
DR   RefSeq; WP_002228401.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q668E8; -.
DR   SMR; Q668E8; -.
DR   EnsemblBacteria; CAH22030; CAH22030; YPTB2792.
DR   GeneID; 66844784; -.
DR   KEGG; ypo:BZ17_3839; -.
DR   KEGG; yps:YPTB2792; -.
DR   PATRIC; fig|273123.14.peg.4029; -.
DR   OMA; DWGQIYR; -.
DR   Proteomes; UP000001011; 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..235
FT                   /note="DnaA regulatory inactivator Hda"
FT                   /id="PRO_0000114323"
SQ   SEQUENCE   235 AA;  26703 MW;  4D4CB860F7C0D573 CRC64;
     MLLNTPAQLS LPLYLPDDET FASFYPGENP SLLAAIQSAV HQPHGSYIYF WSREGGGRSH
     LLHAACAELS QQGEAVGYVP LDKRAYFIPE VLEGMEQLAL VCIDNIECIA GDEQWEMAMF
     NLYNRIVETG RTRLLITGDR PPRQLNLGLP DLASRLDWGQ IYKLQPLSDD EKLQALQLRA
     KLRGFELPED VGRFLLKRLD REMRTLFMTL DQLDRASITA QRKLTIPFVK EILSL