ID A0A1B1BBN5_9ACTN Unreviewed; 655 AA.
AC A0A1B1BBN5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:ANP56201.1};
GN ORFNames=AVL59_00005 {ECO:0000313|EMBL:ANP56201.1};
OS Streptomyces griseochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68214 {ECO:0000313|EMBL:ANP56201.1, ECO:0000313|Proteomes:UP000092659};
RN [1] {ECO:0000313|EMBL:ANP56201.1, ECO:0000313|Proteomes:UP000092659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14511 {ECO:0000313|EMBL:ANP56201.1,
RC ECO:0000313|Proteomes:UP000092659};
RA Wu L.;
RT "Complete genome sequence of Streptomyces griseochromogenes ATCC 14511, the
RT Blasticidin S producer.";
RL Submitted (JUN-2016) 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; CP016279; ANP56201.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B1BBN5; -.
DR STRING; 68214.AVL59_00005; -.
DR KEGG; sgs:AVL59_00005; -.
DR Proteomes; UP000092659; Chromosome.
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 348..476
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 562..631
FT /note="Chromosomal replication initiator DnaA C-terminal"
FT /evidence="ECO:0000259|SMART:SM00760"
FT REGION 77..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ SEQUENCE 655 AA; 72509 MW; 2EF01F73DC38BEEE CRC64;
MWPRVLEQLL GEGRGQGVEA KDEHWIRRCQ PLALVADTAL LAVPNEFAKG VLEGRLAPIV
SDTLSRECGR PIRIAITVDD SAGEPPAPSA PVQQPQPRYE EPELPSGPYE GYGRHRAGDH
HPGGEPPARG DQLHTTRGDQ HPPSRADQLP TARPAYPSEY QRPEPGAWPR PSQDEYGWQQ
PRLGFPERDP YASPPQDAYG SSGPDAYGSP AQDYRPQGME RPPYDQPRSE YDAPRPDYDR
PDYDSPRSEY EPSRAEYDQR DPVRRERPEP PSGVGPVHRG GPGRPDLPPA AGGGAPGPQA
APPAPASGPG EPTARLNPKY LFDTFVIGAS NRFAHAAAVA VAEAPAKAYN PLFIYGESGL
GKTHLLHAIG HYARSLYPGT RVRYVSSEEF TNEFINSIRD GKGDSFRKRY REMDILLVDD
IQFLADKEST QEEFFHTFNT LHNANKQIVL SSDRPPKQLV TLEDRLRNRF EWGLITDVQP
PELETRIAIL RKKAVQEQLN APPEVLEFIA SRISRNIREL EGALIRVTAF ASLNRQPVDL
GLTEIVLKDL IPGGEDSAPE ITATAIMAAT ADYFGLTVED LCGTSRGRAL VTARQIAMYL
CRELTDLSLP KIGAQFGGRD HTTVMHADRK IRALMAERRS IYNQVTELTN RIKNG
//
