DNAA_HERA2
ID DNAA_HERA2 Reviewed; 472 AA.
AC A9B496;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=Haur_0001;
OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC Herpetosiphon.
OX NCBI_TaxID=316274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in the initiation and regulation of
CC chromosomal replication. Binds to the origin of replication; it binds
CC specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-
CC TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
CC {ECO:0000255|HAMAP-Rule:MF_00377}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00377}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000255|HAMAP-
CC Rule:MF_00377}.
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DR EMBL; CP000875; ABX02653.1; -; Genomic_DNA.
DR AlphaFoldDB; A9B496; -.
DR SMR; A9B496; -.
DR STRING; 316274.Haur_0001; -.
DR PRIDE; A9B496; -.
DR EnsemblBacteria; ABX02653; ABX02653; Haur_0001.
DR KEGG; hau:Haur_0001; -.
DR eggNOG; COG0593; Bacteria.
DR HOGENOM; CLU_026910_3_1_0; -.
DR OMA; FPAFKIV; -.
DR Proteomes; UP000000787; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd06571; Bac_DnaA_C; 1.
DR Gene3D; 1.10.1750.10; -; 1.
DR Gene3D; 3.30.300.180; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00377; DnaA_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR001957; Chromosome_initiator_DnaA.
DR InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR InterPro; IPR018312; Chromosome_initiator_DnaA_CS.
DR InterPro; IPR013317; DnaA.
DR InterPro; IPR013159; DnaA_C.
DR InterPro; IPR024633; DnaA_N_dom.
DR InterPro; IPR038454; DnaA_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010921; Trp_repressor/repl_initiator.
DR PANTHER; PTHR30050:SF2; PTHR30050:SF2; 1.
DR Pfam; PF00308; Bac_DnaA; 1.
DR Pfam; PF08299; Bac_DnaA_C; 1.
DR Pfam; PF11638; DnaA_N; 1.
DR PRINTS; PR00051; DNAA.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00760; Bac_DnaA_C; 1.
DR SUPFAM; SSF48295; SSF48295; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00362; DnaA; 1.
DR PROSITE; PS01008; DNAA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA replication; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..472
FT /note="Chromosomal replication initiator protein DnaA"
FT /id="PRO_1000121988"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ SEQUENCE 472 AA; 52821 MW; 1257B0E47CD4EFC5 CRC64;
MDTKQIWFTT LGTLQNQILR YDYDTWLKTT ALVSVANDLA VIGAPNVTTK QVIEDRFMSV
LRRALGEVLG YQVNVRVIIS SATPAPSEPV AVTPSEPSPT TEVAEPSFAS FNQAAPMLNQ
LPLGDPNRSS VLNPRYTFSS FIVGTSNRLA HAACMAVAEH PAQAYNPLFL YGGVGLGKTH
LLQAIGNYAL DRNPEVNVLY VSSEKFTNDL INAIRRQQTE EFRIRYRNID ILLIDDIQFI
AGKEGTQEEF FHTFNTLHGA GKQIVLSSDR PPKAILTLEE RLRSRFEWGL IVDVQNPDLE
TRTAILRAKG ETLQVPVSSE VIDFLAQRIQ SNIRELEGCL NRVIAYANLN RTPVTVEVAS
AALADLLDTS RRKRVTADDI FREVSQHYGI DQRAIRGRGR SRNVVLPRQV VMYLLREETD
ASLVEIGELL GGRDHTTVMH GYNKITDDLT SDARLRNDIT SLRQRLYGEN AR