DNAA_ACIBT
ID DNAA_ACIBT Reviewed; 465 AA.
AC A3M0Q4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=A1S_0001;
OS Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS KC755 / 5377).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=400667;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX PubMed=17344419; DOI=10.1101/gad.1510307;
RA Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA Gerstein M., Snyder M.;
RT "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT density pyrosequencing and transposon mutagenesis.";
RL Genes Dev. 21:601-614(2007).
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; CP000521; ABO10498.2; -; Genomic_DNA.
DR RefSeq; WP_000964767.1; NZ_CP053098.1.
DR AlphaFoldDB; A3M0Q4; -.
DR SMR; A3M0Q4; -.
DR KEGG; acb:A1S_0001; -.
DR HOGENOM; CLU_026910_0_1_6; -.
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..465
FT /note="Chromosomal replication initiator protein DnaA"
FT /id="PRO_1000121940"
FT REGION 81..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ SEQUENCE 465 AA; 52277 MW; 1674004A5431A828 CRC64;
MLWTDCLTRL RQELSDNVFA MWIRPLVAEE VEGILRLYAP NPYWTRYIQE NHLELISILA
EQLSEGRVRQ VEILVDSRPG SILSSSEQPA TTTAALQTAP IPQPAKVKRE PEPVANTAVS
SKSSKKKLLN PQFTFSLFVE GRSNQMAAET CRKVLTQLGA SQHNPLFLYG PTGLGKTHLM
QAVGNALLQA KPNARVMYMT SESFVQDFVS SLQKGKVEEF KKNCRSLDLL LVDDIHLLAG
KEASLVEFFY TFNALLDESK QIILTSDRYP KELTELDPRL VSRFSWGLSV GVEPPDIETR
IEILLKKAEN SGVDLPRNCA LFIAQQVVAN VRELEGALNK VVAISRFKGA PIDLDVVRES
LKDVLAIRAR TISVENIQRV VSEYFRIPLK ELIGPKRTRI YARPRQLAMG LARELTGDSF
PEIGMAFGGR DHSTVMHACE KVVSLREEDP IFDEDYKNLL RLLQS