ID A0A101JGU0_9ACTN Unreviewed; 615 AA.
AC A0A101JGU0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=ADL15_38110 {ECO:0000313|EMBL:KUL26505.1};
OS Actinoplanes awajinensis subsp. mycoplanecinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL26505.1, ECO:0000313|Proteomes:UP000053244};
RN [1] {ECO:0000313|EMBL:KUL26505.1, ECO:0000313|Proteomes:UP000053244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL26505.1,
RC ECO:0000313|Proteomes:UP000053244};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL26505.1}.
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DR EMBL; LLZH01000306; KUL26505.1; -; Genomic_DNA.
DR RefSeq; WP_067702007.1; NZ_LLZH01000306.1.
DR AlphaFoldDB; A0A101JGU0; -.
DR OrthoDB; 9807019at2; -.
DR Proteomes; UP000053244; 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:UP000053244}.
FT DOMAIN 309..437
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 521..590
FT /note="Chromosomal replication initiator DnaA C-terminal"
FT /evidence="ECO:0000259|SMART:SM00760"
FT REGION 80..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 317..324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ SEQUENCE 615 AA; 68956 MW; E468D3819910CAE1 CRC64;
MADQVDLGLL WQDTLSELSE EIASRQQRAY LRFTRLRAIV EDTALLSVPD AYTRDVIELR
LRPAITEALT RRLNRPIQVA VTVRPPEDGS GMPGTVYGTP VESDSAPHAE PQPLHYAEPP
RNPDPRPYQP ELPAYQPEQQ QYQQPAFGPP DRAPEPYPTG SAQHSGPPPS YIRDGSASRA
GQEALFADPM PPQANRSAAN RTDKGPERDA PSAPNEAAVH RMPADQSQMR DNQRRQDDRR
DDSMPMRPGD NGPGRPQVDL RGPGSSPRPG GNDGNRLNPK YMFETFVIGS SNRFAHAASV
AVAESPAKAY NPLFIYGSSG LGKTHLLHAI GHYATTLGHA RSVRYVSTEE FTNDFINSLR
DDKTQAFQRR YRDVDILLID DIQFLENRER TQEEFFHTFN TLHNANKQIV ISSDRSPRQL
ATLEDRMRTR FEWGLLADIQ PPDLETRIAI LQKKAAQERM YAPADVLEFI ASRVSNSIRE
LEGALIRVTA FASLTRATVQ LSLAEEVLRD FMPDGAGPEI TADQIMVSTA DYFGVSLEDL
RGHSRSRVLV NARQVAMYLC RELTDLSLPR IGQAFGGRDH TTVMHADRKI RQHMAERRSL
YNQIAELTNR IKQNT
//
