ID A0A2A3Y576_9MICC Unreviewed; 478 AA.
AC A0A2A3Y576;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=CIK74_15830 {ECO:0000313|EMBL:PCC32100.1};
OS Glutamicibacter sp. BW77.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Glutamicibacter.
OX NCBI_TaxID=2024402 {ECO:0000313|EMBL:PCC32100.1, ECO:0000313|Proteomes:UP000218926};
RN [1] {ECO:0000313|EMBL:PCC32100.1, ECO:0000313|Proteomes:UP000218926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BW77 {ECO:0000313|EMBL:PCC32100.1,
RC ECO:0000313|Proteomes:UP000218926};
RX PubMed=28644126;
RA Bonham K.S., Wolfe B.E., Dutton R.J.;
RT "Extensive horizontal gene transfer in cheese-associated bacteria.";
RL Elife 6:e22144-e22144(2017).
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:PCC32100.1}.
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DR EMBL; NRGT01000077; PCC32100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3Y576; -.
DR OrthoDB; 9807019at2; -.
DR Proteomes; UP000218926; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000218926}.
FT DOMAIN 169..300
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 381..450
FT /note="Chromosomal replication initiator DnaA C-terminal"
FT /evidence="ECO:0000259|SMART:SM00760"
FT REGION 93..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 450..477
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 101..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ SEQUENCE 478 AA; 53711 MW; 7518BC823AD6AB3F CRC64;
MSSDETNSIG SSWRQVIRKI EDDDRVKARH RPFVSLAKPQ GLIGSTLLVA VPNDLTRDIL
QTQLREPLDQ ALREVFQDDI RCAVSVDLSL AEEVEQPPEK KTSPAPVPVP VPETPGPRPQ
PAPQPTPPSN SQEFGRLNPK YIFDTFVIGS SNRFAHAAAV AVAEAPAKAY NPLFIYGDSG
LGKTHLLHAI GHYARHLYKG IRVRYVNSEE FTNDFINSIR DDEGASFKQT YRNVDILLID
DIQFLANKDA TQEEFFHTFN ALHNHNKQVV ITSDLPPKQL QGFEDRMRSR FEWGLLTDIQ
PPELETRIAI LRKKADAENL SAPGDVMEYI ASRISTNIRE LEGALIRVTA FASLNNQHVD
LALAETVLKD LISADGAQEI TPSTIIKQTA EYFGLTIDEL NSKSRTRTLV TARQIAMYLL
RELTDMSLPK IGAELGGRDH TTVIHADRKI RELMAERRAI FNQVTELTNR IKQSQREH
//