ID   DNAA_STRAQ              Reviewed;         624 AA.
AC   Q9ZH75;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Chromosomal replication initiator protein DnaA;
GN   Name=dnaA;
OS   Streptomyces anulatus (Streptomyces chrysomallus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11523 / DSM 40128 / JCM 4296 / LMG 20459 / NBRC 15393;
RX   PubMed=9611803; DOI=10.1099/00221287-144-5-1281;
RA   Jakimowicz D., Majka J., Messer W., Speck C., Fernandez M., Martin M.C.,
RA   Sanchez J., Schauwecker F., Keller U., Schrempf H.,
RA   Zakrzewska-Czerwinska J.;
RT   "Structural elements of the Streptomyces oriC region and their interactions
RT   with the DnaA protein.";
RL   Microbiology 144:1281-1290(1998).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=11073953; DOI=10.1074/jbc.m007876200;
RA   Majka J., Zakrzewska-Czerwinska J., Messer W.;
RT   "Sequence recognition, cooperative interaction, and dimerization of the
RT   initiator protein DnaA of Streptomyces.";
RL   J. Biol. Chem. 276:6243-6252(2001).
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       TTGTCCACA-3'. DnaA binds to ATP and to acidic phospholipids.
CC   -!- SUBUNIT: Can form a dimer when binding to a single dnaA box.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000305}.
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DR   EMBL; AF071024; AAD08807.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZH75; -.
DR   SMR; Q9ZH75; -.
DR   PRIDE; Q9ZH75; -.
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; 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   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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; DNA replication; DNA-binding; Nucleotide-binding.
FT   CHAIN           1..624
FT                   /note="Chromosomal replication initiator protein DnaA"
FT                   /id="PRO_0000114270"
FT   REGION          88..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         325..332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   624 AA;  69922 MW;  580CE90014A2F833 CRC64;
     MADVPADLAA VWPRVLEQLL GEGQQGIEPK DKQWIERCQP LALVADTALL AVPNEWGKRV
     LEGRLAPLIS ETLTRECGRP IRIAITVDDS AGEPPSPPAP PMHQSHQSQQ GHRYPAQQRD
     DAPRGDAYDG YGHRPSDDGM PTRRPAYPDY QQQRPEPGAW PRTQEDLSWQ QPRHGGYQDR
     EQPSGEPYRE SESYRERENE QYREQAPEQW RQPYGTGRPQ QPQHDYRSGP PEHQGYEQQR
     PDRQDQGQGP RQGGHGPGRT GGSVPGPMGA QPAPAPGPGE PHARLNPKYL FDTFVIGASN
     RFAHAAAVAV AEAPAKAYNP LFIYGESGLG KTHLLHAIGH YARSLYPGTR VRYVSSEEFT
     NEFINSIRDG KGDTFRKRYR DVDILLVDDI QFLASKESTQ EEFFHTFNTL HNANKQIVLS
     SDRPPKQLVT LEDRLRNRFE WGLTTDVQPP ELETRIAILR KKAVQEQLNA PPEVLEFIAS
     RISRNIRELE GALIRVTAFA SLNRQPVDLG LTEIVLKDLI PGGEESAPEI TAPAIMAATA
     DYFGLTVDDL CGSSRTRVLV TARQIAMYLC RELTDLSLPK IGAQFGGRDH TTVMHADRKI
     RALMAERRSI YNQVTELTNR IKNG