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Database: UniProt
Entry: A5UP91
LinkDB: A5UP91
Original site: A5UP91 
ID   DNAA_ROSS1              Reviewed;         481 AA.
AC   A5UP91;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=RoseRS_0001;
OS   Roseiflexus sp. (strain RS-1).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=357808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Roseiflexus sp. RS-1.";
RL   Submitted (APR-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; CP000686; ABQ88444.1; -; Genomic_DNA.
DR   RefSeq; WP_011954804.1; NC_009523.1.
DR   AlphaFoldDB; A5UP91; -.
DR   SMR; A5UP91; -.
DR   STRING; 357808.RoseRS_0001; -.
DR   KEGG; rrs:RoseRS_0001; -.
DR   eggNOG; COG0593; Bacteria.
DR   HOGENOM; CLU_026910_3_1_0; -.
DR   OrthoDB; 9807019at2; -.
DR   Proteomes; UP000006554; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; cd00009; AAA; 1.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.300.180; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00362; DnaA; 1.
DR   PANTHER; PTHR30050; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1.
DR   PANTHER; PTHR30050:SF2; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48295; TrpR-like; 1.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA replication; DNA-binding; Nucleotide-binding.
FT   CHAIN           1..481
FT                   /note="Chromosomal replication initiator protein DnaA"
FT                   /id="PRO_1000048714"
FT   REGION          87..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         182..189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   481 AA;  54281 MW;  24C9964245F9F713 CRC64;
     MNLTKVWNTT LGSLQVQLPR HEYNTWVRGA TLLEIDNGVA IVRAPNAFIK EGLESRYLAT
     LREQLGSVVG FPVDVRVVLA SPDFERFDGA PHNGRSTENE TRRTAQSLPL QPGSSSNGVN
     HPLERTPPQQ LELHRAVRSS MLNPRYTFDR FIIGPSNRLA NAACMAVAEH PAQAYNPLFL
     YGGVGLGKTH LLHAIGNFVL DRDPEVNVLY VSSETFTNDL INSIRRQQTE EFRIRYRNID
     ILLIDDIQFI AGKEQTQEEF FHTFNTLHSA GKQIVISSDR SPKAILTLEE RLRSRFEWGL
     IVDVQMPDLE TRTAILRAKA EQSPVPVPQP VIDFLAQRIQ SHIRELEGCL NRVTAFAQMY
     NVPVTIEVAT AALSELLDTN RRKRVTPDAI LREVAAFYSV DLRALQGRSR SRNIVIPRQV
     AMYLLREETD SSLMEIGQLL GGRDHTTVMY GCEKITEELN SDARLRQEVA TIRERLLHSA
     G
//
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