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Database: UniProt
Entry: J3VTT9_9ENTR
LinkDB: J3VTT9_9ENTR
Original site: J3VTT9_9ENTR 
ID   J3VTT9_9ENTR            Unreviewed;       233 AA.
AC   J3VTT9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-SEP-2017, entry version 32.
DE   RecName: Full=DnaA regulatory inactivator Hda {ECO:0000256|HAMAP-Rule:MF_01158, ECO:0000256|SAAS:SAAS00634471};
GN   Name=hda {ECO:0000256|HAMAP-Rule:MF_01158};
GN   ORFNames=A35E_00110 {ECO:0000313|EMBL:AFP85426.1};
OS   secondary endosymbiont of Heteropsylla cubana.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts.
OX   NCBI_TaxID=134287 {ECO:0000313|EMBL:AFP85426.1, ECO:0000313|Proteomes:UP000003937};
RN   [1] {ECO:0000313|EMBL:AFP85426.1, ECO:0000313|Proteomes:UP000003937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22821013; DOI=10.1093/molbev/mss180;
RA   Sloan D.B., Moran N.A.;
RT   "Genome reduction and co-evolution between the primary and secondary
RT   bacterial symbionts of psyllids.";
RL   Mol. Biol. Evol. 29:3781-3792(2012).
CC   -!- FUNCTION: Mediates the interaction of DNA replication inititator
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 reinititation, a process called regulatory
CC       inhibition of DnaA or RIDA. {ECO:0000256|HAMAP-Rule:MF_01158}.
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:0000256|HAMAP-Rule:MF_01158}.
CC   -!- SIMILARITY: Belongs to the DnaA family. HdA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01158, ECO:0000256|SAAS:SAAS00548763}.
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DR   EMBL; CP003547; AFP85426.1; -; Genomic_DNA.
DR   RefSeq; WP_014888723.1; NC_018420.1.
DR   EnsemblBacteria; AFP85426; AFP85426; A35E_00110.
DR   KEGG; sehc:A35E_00110; -.
DR   PATRIC; fig|134287.3.peg.101; -.
DR   KO; K10763; -.
DR   OrthoDB; POG091H0GIW; -.
DR   Proteomes; UP000003937; Chromosome.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0032297; P:negative regulation of DNA-dependent DNA replication initiation; IEA:InterPro.
DR   HAMAP; MF_01158; Hda; 1.
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   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03420; DnaA_homol_Hda; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000003937};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_01158,
KW   ECO:0000256|SAAS:SAAS00634466};
KW   DNA replication inhibitor {ECO:0000256|HAMAP-Rule:MF_01158,
KW   ECO:0000256|SAAS:SAAS00634468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003937}.
FT   DOMAIN       16    212       Bac_DnaA. {ECO:0000259|Pfam:PF00308}.
SQ   SEQUENCE   233 AA;  26473 MW;  B1755B107165AE00 CRC64;
     MNTPMQLSLP LYLPDHKTFS SFYPGNNDVL LSALQDILGD KHGSYLYFWS CKGGGRTHLL
     HAACSKLSSQ DKAVGYVPLD KRTWLVPEVL EGMEQLALVT IDNIEYIAGD LPWEIAIFNL
     YNRIQETGYT RFIISGNCPP RQLNLHLPDL ASRLDWGQIY RLNPLSDEGK GYALQMRAKL
     RGFELTEDVS CFLLKRLQRD MRTLSVALEQ LDHASICAKR KLTIPFVKSI LNL
//
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