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DNAA_SYNP2
ID   DNAA_SYNP2              Reviewed;         449 AA.
AC   B1XKQ0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   OrderedLocusNames=SYNPCC7002_A0001;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) 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; CP000951; ACA98019.1; -; Genomic_DNA.
DR   RefSeq; WP_012305643.1; NC_010475.1.
DR   AlphaFoldDB; B1XKQ0; -.
DR   SMR; B1XKQ0; -.
DR   STRING; 32049.SYNPCC7002_A0001; -.
DR   EnsemblBacteria; ACA98019; ACA98019; SYNPCC7002_A0001.
DR   KEGG; syp:SYNPCC7002_A0001; -.
DR   eggNOG; COG0593; Bacteria.
DR   HOGENOM; CLU_026910_3_1_3; -.
DR   OMA; REFNPLF; -.
DR   Proteomes; UP000001688; 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..449
FT                   /note="Chromosomal replication initiator protein DnaA"
FT                   /id="PRO_1000122027"
FT   REGION          90..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         151..158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   449 AA;  50517 MW;  51FA0B32046B8D62 CRC64;
     MTQNPQWLWQ EVLTKLEQQL SRPTYETWIQ PTAIQQWRED EIVLCAPNAF VLNHIQKYYG
     ALITETIAEL LQQPVKVRLT SPEGNTLAAT QSFYSSRSGQ STRPGKKTPE LNSKYTFSRF
     VVGPTNRMAH AAALAVAESP GRDFNPLVLC GGVGLGKTHL MQAIGHYRLD TQPDAKIFYV
     STEQFTNDLI VAIRKDSLQT FREHYRTADI LLVDDIQFIE GKEYTQEEFF YTFNTLHEAG
     KQIVLASDRP PHQIPGLQQR LSSRFSMGLI ADIQPPDLET RMAILQKKAE AENLNLSRSV
     IEYIATHYTA NIRELEGALL RAVTHIAISG LPMTVENLAP ILNPTVEYAP AAPDVILQIA
     AEATGVSIED LKGASRRREI STARQIAMYL MRQHTDLSLP RIGELFGGKD HTTVMYSCDK
     IGQLLTKNQK ISQLVSQISD RINHHHQNL
 
 
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