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Database: UniProt
Entry: HDA_PROMH
LinkDB: HDA_PROMH
Original site: HDA_PROMH 
ID   HDA_PROMH               Reviewed;         248 AA.
AC   B4EY85;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   07-JUN-2017, entry version 56.
DE   RecName: Full=DnaA regulatory inactivator Hda {ECO:0000255|HAMAP-Rule:MF_01158};
GN   Name=hda {ECO:0000255|HAMAP-Rule:MF_01158}; OrderedLocusNames=PMI1571;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/JB.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master
RT   of both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
CC   -!- FUNCTION: Mediates the interaction of DNA replication initiator
CC       protein DnaA with DNA polymerase subunit beta sliding clamp
CC       (dnaN). Stimulates hydrolysis of ATP-DnaA to ADP-DnaA, rendering
CC       DnaA inactive for reinitiation, a process called regulatory
CC       inhibition of DnaA or RIDA (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The active form seems to be an ADP-bound monomer. Forms
CC       the RIDA complex (regulatory inactivation of DnaA) of ATP-DnaA,
CC       ADP-Hda and the DNA-loaded beta sliding clamp (dnaN).
CC       {ECO:0000255|HAMAP-Rule:MF_01158}.
CC   -!- SIMILARITY: Belongs to the DnaA family. HdA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01158}.
DR   EMBL; AM942759; CAR43293.1; -; Genomic_DNA.
DR   SMR; B4EY85; -.
DR   STRING; 529507.PMI1571; -.
DR   PRIDE; B4EY85; -.
DR   EnsemblBacteria; CAR43293; CAR43293; PMI1571.
DR   KEGG; pmr:PMI1571; -.
DR   eggNOG; ENOG4108KZ1; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000256538; -.
DR   KO; K10763; -.
DR   OMA; DWGQIYR; -.
DR   OrthoDB; POG091H0GIW; -.
DR   Proteomes; UP000008319; Chromosome.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0032297; P:negative regulation of DNA-dependent DNA replication initiation; IEA:InterPro.
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   Complete proteome; DNA replication; DNA replication inhibitor;
KW   Reference proteome.
FT   CHAIN         1    248       DnaA regulatory inactivator Hda.
FT                                /FTId=PRO_0000389450.
SQ   SEQUENCE   248 AA;  28068 MW;  476FE281B8D235B9 CRC64;
     MLESRRLLNY SGEVLLNTPS QLSLPLSLPD DETFDSFYAG ENASLVAAIQ TAIHQSHGSY
     IYFWSRDGGG KSHLLHAACA ELSLAGDAVG YVPLDKRAYF VPDVLEGMEH LSLVCIDNVQ
     CIAGDEEWEL ALFNLYNRVL ELGRTCLLIT GDRPPRQIDL QLPDLASRLD WGQIYRLQPL
     SDEEKIQALQ LRAKLRGFEL PEDVGRFVLK RLDRKMRTLF EMLDELDHAS IVAQRKLTIP
     FVKDILKL
//
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