ID A0A239FQ13_9ACTN Unreviewed; 587 AA.
AC A0A239FQ13;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|ARBA:ARBA00018893, ECO:0000256|HAMAP-Rule:MF_00377};
GN Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN ORFNames=SAMN06893096_105167 {ECO:0000313|EMBL:SNS58004.1};
OS Geodermatophilus pulveris.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1564159 {ECO:0000313|EMBL:SNS58004.1, ECO:0000313|Proteomes:UP000198373};
RN [1] {ECO:0000313|EMBL:SNS58004.1, ECO:0000313|Proteomes:UP000198373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46839 {ECO:0000313|EMBL:SNS58004.1,
RC ECO:0000313|Proteomes:UP000198373};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00377}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|ARBA:ARBA00006583,
CC ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU004227}.
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DR EMBL; FZOO01000005; SNS58004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239FQ13; -.
DR OrthoDB; 9807019at2; -.
DR Proteomes; UP000198373; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; cd00009; AAA; 1.
DR CDD; cd06571; Bac_DnaA_C; 1.
DR Gene3D; 1.10.1750.10; -; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.300.180; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00362; DnaA; 1.
DR PANTHER; PTHR30050; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1.
DR PANTHER; PTHR30050:SF2; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48295; TrpR-like; 1.
DR PROSITE; PS01008; DNAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00377};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00377};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00377};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00377};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00377}.
FT DOMAIN 279..407
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 491..560
FT /note="Chromosomal replication initiator DnaA C-terminal"
FT /evidence="ECO:0000259|SMART:SM00760"
FT REGION 84..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 287..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ SEQUENCE 587 AA; 65127 MW; 84FD4497DEB2988E CRC64;
MADATVDLAA VWDQIRERLA TSLSPQQNAM LNLTRPVGVF EDTAVLAAPN EFTQTVLESR
MRRVLAEALS EHLGREIRVA VQVEDSPAAP PAPPRPEVPT RRPWSVVEAQ RAEEDRETRD
RADDGRSAFG VRADVRPAWE DGAADAPDPR PAERDVEEWA PTDWSPAARR PAGRGTRAAE
RDWGGTDLDE DGVAVLPFDL DGGDGAGGPQ EPPGPSRGRR GGSRGGDAVP LFGGDRRTPA
GGQDPGLNPK YVFDSFVIGN SNRFAHAAAV AVAEAPARAY NPLFVYGDSG LGKTHLLHAI
GHYAARMFPN VRVRYVSTEE FTNEFINLVH SGRAEEFRRR FRDIDFLLID DIQFLERAER
TQEEFFHTFN TLHNASKQIV ITSDRAPKKL TTLEDRLRTR FEWGLITDVQ APDLETRIAI
LRKKAYGERL QVPDQVLEFI ASKVQTNIRE LEGALIRVTA FASLNRQQVD LPLAELVLKD
LISDEQGPQI TAAIIMAATA EYFSVTMEEL QGANRSRTLV NARQIAMYLC RELTELSLPR
IGASFGGKDH TTVMHAVKKI TNLMSERRAT YTQVTELTAR IKSRARQ
//
