ID A0A0H4C008_9ACTN Unreviewed; 625 AA.
AC A0A0H4C008;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 47.
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:AKN69132.1};
GN ORFNames=QR97_04270 {ECO:0000313|EMBL:AKN69132.1};
OS Streptomyces sp. PBH53.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1577075 {ECO:0000313|EMBL:AKN69132.1, ECO:0000313|Proteomes:UP000036399};
RN [1] {ECO:0000313|EMBL:AKN69132.1, ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|EMBL:AKN69132.1,
RC ECO:0000313|Proteomes:UP000036399};
RX PubMed=26227608;
RA Gosse J.T., Hill P., Dowd S.E., Boddy C.N.;
RT "Draft Genome Sequence of Streptomyces sp. Strain PBH53, Isolated from an
RT Urban Environment.";
RL Genome Announc. 3:e00859-e00815(2015).
RN [2] {ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|Proteomes:UP000036399};
RA Gosse J.T., Boddy C.N., Hill P.B.;
RT "Draft Genome Sequence of Streptomyces sp. strain PBH53, isolated from
RT urban environment.";
RL Submitted (JUN-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}.
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DR EMBL; CP011799; AKN69132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4C008; -.
DR STRING; 1577075.QR97_04270; -.
DR PATRIC; fig|1577075.3.peg.877; -.
DR Proteomes; UP000036399; 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}; Reference proteome {ECO:0000313|Proteomes:UP000036399}.
FT DOMAIN 318..446
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 532..601
FT /note="Chromosomal replication initiator DnaA C-terminal"
FT /evidence="ECO:0000259|SMART:SM00760"
FT REGION 62..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 326..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ SEQUENCE 625 AA; 69444 MW; A18B66D031B0A21E CRC64;
MEAKDEHWIR RCQPLALVAD TALLAVPNEF AKGVLEGRLA PIVSETLSRE CGRPIRIAIT
VDDSAGEPPA PAAPPAQQTP KPRYEEPELP SGPYEGYGRH RGGADQLPGT EPRPEQLPSA
RPDQLPTVRP AYPSEYHRPE PGAWPRPAQD EYGWQQPRLG FPERDPYASP SSQDAYGSGA
DAYGSPSQDY RPQGMDRPPY EQQRGDYDTP RAEYEPARSD YESARPEYDP SRTEYDQRDP
VRRELPEPPA HRGGPGRPDM PSAGAPGPLA AQPAPASGPG EPTARLNPKY LFDTFVIGAS
NRFAHAAAVA VAEAPAKAYN PLFIYGESGL GKTHLLHAIG HYARSLYPGT RVRYVSSEEF
TNEFINSIRD GKGDSFRKRY REMDILLVDD IQFLADKEST QEEFFHTFNT LHNANKQIVL
SSDRPPKQLV TLEDRLRNRF EWGLITDVQP PELETRIAIL RKKAVQEQLN APPEVLEFIA
SRISRNIREL EGALIRVTAF ASLNRQPVDL GLTEIVLKDL IPGGEDSTPE ITATAIMAAT
ADYFGLTVDD LCGSSRGRQL VTARQIAMYL CRELTDLSLP KIGAQFGGRD HTTVMHADRK
IRALMAERRS IYNQVTELTN RIKNG
//
