ID A0A558C9N2_9PSEU Unreviewed; 556 AA.
AC A0A558C9N2;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 08-NOV-2023, entry version 15.
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 ECO:0000313|EMBL:TVT45506.1};
GN ORFNames=FNH05_20580 {ECO:0000313|EMBL:TVT45506.1};
OS Amycolatopsis rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=2053003 {ECO:0000313|EMBL:TVT45506.1, ECO:0000313|Proteomes:UP000320011};
RN [1] {ECO:0000313|EMBL:TVT45506.1, ECO:0000313|Proteomes:UP000320011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBRC 6029 {ECO:0000313|EMBL:TVT45506.1,
RC ECO:0000313|Proteomes:UP000320011};
RA Duangmal K., Teo W.F.A.;
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TVT45506.1, ECO:0000313|Proteomes:UP000320011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBRC 6029 {ECO:0000313|EMBL:TVT45506.1,
RC ECO:0000313|Proteomes:UP000320011};
RA Srisuk N.;
RT "Amycolatopsis acidicola sp. nov., isolated from peat swamp forest soil.";
RL Submitted (AUG-2019) 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:TVT45506.1}.
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DR EMBL; VJWX01000212; TVT45506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A558C9N2; -.
DR OrthoDB; 9807019at2; -.
DR Proteomes; UP000320011; 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:UP000320011}.
FT DOMAIN 248..376
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 460..529
FT /note="Chromosomal replication initiator DnaA C-terminal"
FT /evidence="ECO:0000259|SMART:SM00760"
FT REGION 85..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..147
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 256..263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ SEQUENCE 556 AA; 61948 MW; 1C3EA7A3D5B92B6D CRC64;
MSEHQINLGV VWEQVVRELS DGTLSPQQRA WMRVTRPIGL LDGTALLAAP SDFAKEAIER
ALREPITHAL SRRLGRPVSL AVKVDTAEVA PPPPSTAQYA PSPARGENPL DPPTLPSMQP
ALPPALQPSL NPSLNPSLPP SLPPLEETLL PPLRRRGVPA EPAPKHLAED DAEEEVDEEG
EALAAAHEIW PMFSGQPIAG QPYTAPAQPQ TSKTRLNEKY TFDTFVIGAS NRFAHAAAFA
VAEAPSRAYN PLFIWGESGL GKTHLLHAVG HYAQRLFPGM RVRYVSTEEF TNDFINSLRD
DRKVAFQRRY RDIDILLVDD IQFLEGKEGT QEEFFHTFNT LHNSNKQIVV SSDRPPKRLE
TLEDRLRTRF EWGLITDIQP PELETRIAIL RKKAAQDRLA VPGDVLEFIA SRVEANIREL
EGALIRVTAF ASLNQAPVDV GLAEIVLRDL IPDSQAPEIN APTIMAATSE FFDVTIDDLC
GPGKTKALAT ARQIAMYLCR ELTDMSLPKI GQTFGGRDHT TVMHADKKIR KEMAERRRIY
DQVQELTFRI KQRARQ
//
