DNAA_YERPG
ID DNAA_YERPG Reviewed; 462 AA.
AC A9R5R5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=YpAngola_A4177;
OS Yersinia pestis bv. Antiqua (strain Angola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Angola;
RX PubMed=20061468; DOI=10.1128/jb.01518-09;
RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA Achtman M., Lindler L.E., Ravel J.;
RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT new insights into the evolution and pangenome of the plague bacterium.";
RL J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX86526.1; -; Genomic_DNA.
DR RefSeq; WP_002220732.1; NZ_CP009935.1.
DR AlphaFoldDB; A9R5R5; -.
DR SMR; A9R5R5; -.
DR GeneID; 66843639; -.
DR KEGG; ypg:YpAngola_A4177; -.
DR PATRIC; fig|349746.12.peg.913; -.
DR OMA; REFNPLF; -.
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.
FT CHAIN 1..462
FT /note="Chromosomal replication initiator protein DnaA"
FT /id="PRO_1000122036"
FT REGION 104..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 167..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ SEQUENCE 462 AA; 52176 MW; BCB55EBFDA8F8C4E CRC64;
MSLSLWQQCL ARLQDELPAT EFSMWIRPLQ AELSDNTLAL YAPNRFVLDW VRDKYLNNIN
GLLNDFCGTE VPLLRFEVGS KPAARAHNNP VTASVSAPVA PVTRSAPMRP SWDNSPAQPE
LSYRSNVNPK HTFDNFVEGK SNQLARAAAR QVADNPGGAY NPLFLYGGTG LGKTHLLHAV
GNGIMARKAN AKVVYMHSER FVQDMVKALQ NNAIEEFKRY YRSVDALLID DIQFFANKER
SQEEFFHTFN ALLEGNQQII LTSDRYPKEI NGVEDRLKSR FGWGLTVAIE PPELETRVAI
LMKKADENDI RLPGEVAFFI AKRLRSNVRE LEGALNRVIA NANFTGRAIT IDFVREALRD
LLALQEKLVT IDNIQKTVAE YYKIKVADLL SKRRSRSVAR PRQMAMALAK ELTNHSLPEI
GDAFGGRDHT TVLHACRKIE QLREESHDIK EDFSNLIRTL SS