ID A0A0T2IGL7_9MICO Unreviewed; 539 AA.
AC A0A0T2IGL7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=ASD62_11555 {ECO:0000313|EMBL:KQZ89840.1};
OS Phycicoccus sp. Root563.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736562 {ECO:0000313|EMBL:KQZ89840.1, ECO:0000313|Proteomes:UP000051641};
RN [1] {ECO:0000313|Proteomes:UP000051641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root563 {ECO:0000313|Proteomes:UP000051641};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ89840.1, ECO:0000313|Proteomes:UP000051641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root563 {ECO:0000313|EMBL:KQZ89840.1,
RC ECO:0000313|Proteomes:UP000051641};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQZ89840.1}.
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DR EMBL; LMGM01000001; KQZ89840.1; -; Genomic_DNA.
DR RefSeq; WP_056916085.1; NZ_LMGM01000001.1.
DR AlphaFoldDB; A0A0T2IGL7; -.
DR STRING; 1736562.ASD62_11555; -.
DR Proteomes; UP000051641; 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}; Reference proteome {ECO:0000313|Proteomes:UP000051641}.
FT DOMAIN 232..362
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 444..513
FT /note="Chromosomal replication initiator DnaA C-terminal"
FT /evidence="ECO:0000259|SMART:SM00760"
FT REGION 96..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ SEQUENCE 539 AA; 60120 MW; 3CA1C399CB652245 CRC64;
MSEADLDFAQ IWQNTIASLD ADGLPVRERA FLALARLSGL LDGTALVKVP NDYTKDVVEQ
RVRDAVTRAL SSQLGTQVQL AVTVDPSLDE DHYVEDTVGL PDQRGEQRGG TASYGGYGEA
PANFRDAGYG ESPREVGHLE NNGWAPSQRE PQHQPAHRVD PDERPDPSGE QAAQAPGPAP
AQRRPRDEVP SITDESATRL NPKYTFDTFV IGASNRFAHA AAVAVAEAPA KAYNPLFVYG
ESGLGKTHLL HAIGHYARNL YPHVKVRYVN SEEFTNDFIN SIRDDKASNF QRRYRDVDVL
LIDDIQFLQG KVQTQEEFFH TFNTLHNANK QVVITSDLPP KLLSGFEERM RSRFEWGLLT
DVQPPDLETR IAILRKKAIQ ERMSAPDEVL EFIASRISTN IRELEGALIR VTAFASLNRQ
SVDMGLAEIV LKDLIPNEQG SQITSATIMA QTAAYFGLTI EDLCGTSRSR VLVTARQIAM
YLCRELTDLS LPKIGQQFGG RDHTTVMHAD KKIRQLMAER RAIYNQVTEL TNRIKQQSR
//
