DNAA_MYCBO
ID DNAA_MYCBO Reviewed; 507 AA.
AC P49991; A0A1R3XTY8; X2BDR0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Chromosomal replication initiator protein DnaA;
GN Name=dnaA; OrderedLocusNames=BQ2027_MB0001;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-471.
RX PubMed=7557482; DOI=10.1016/0378-1119(95)00403-s;
RA Rajagopalan M., Qin M.H., Steingrube V.A., Nash D.R., Wallace R.J. Jr.,
RA Madiraju M.V.V.S.;
RT "Amplification and cloning of the Mycobacterium tuberculosis dnaA gene.";
RL Gene 163:75-79(1995).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000305}.
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DR EMBL; LT708304; SIT98333.1; -; Genomic_DNA.
DR EMBL; U19186; AAA85542.1; -; Genomic_DNA.
DR PIR; PC4084; PC4084.
DR RefSeq; NP_853671.1; NC_002945.3.
DR RefSeq; WP_010950320.1; NC_002945.4.
DR AlphaFoldDB; P49991; -.
DR SMR; P49991; -.
DR EnsemblBacteria; SIT98333; SIT98333; BQ2027_MB0001.
DR PATRIC; fig|233413.5.peg.1; -.
DR OMA; REFNPLF; -.
DR Proteomes; UP000001419; 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; 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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA replication; DNA-binding; Nucleotide-binding.
FT CHAIN 1..507
FT /note="Chromosomal replication initiator protein DnaA"
FT /id="PRO_0000114210"
FT REGION 99..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 288
FT /note="H -> R (in Ref. 3; AAA85542)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="R -> D (in Ref. 3; AAA85542)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="I -> V (in Ref. 3; AAA85542)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="D -> G (in Ref. 3; AAA85542)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="E -> V (in Ref. 3; AAA85542)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="A -> P (in Ref. 3; AAA85542)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="N -> S (in Ref. 3; AAA85542)"
FT /evidence="ECO:0000305"
FT CONFLICT 429..430
FT /note="EE -> GR (in Ref. 3; AAA85542)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="T -> P (in Ref. 3; AAA85542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 56600 MW; 3935A335D413AADE CRC64;
MTDDPGSGFT TVWNAVVSEL NGDPKVDDGP SSDANLSAPL TPQQRAWLNL VQPLTIVEGF
ALLSVPSSFV QNEIERHLRA PITDALSRRL GHQIQLGVRI APPATDEADD TTVPPSENPA
TTSPDTTTDN DEIDDSAAAR GDNQHSWPSY FTERPRNTDS ATAGVTSLNR RYTFDTFVIG
ASNRFAHAAA LAIAEAPARA YNPLFIWGES GLGKTHLLHA AGNYAQRLFP GMRVKYVSTE
EFTNDFINSL RDDRKVAFKR SYRDVDVLLV DDIQFIEGKE GIQEEFFHTF NTLHNANKQI
VISSDRPPKQ LATLEDRLRT RFEWGLITDV QPPELETRIA ILRKKAQMER LAIPDDVLEL
IASSIERNIR ELEGALIRVT AFASLNKTPI DKALAEIVLR DLIADANTMQ ISAATIMAAT
AEYFDTTVEE LRGPGKTRAL AQSRQIAMYL CRELTDLSLP KIGQAFGRDH TTVMYAQRKI
LSEMAERREV FDHVKELTTR IRQRSKR
