DNAB_BUCBP
ID DNAB_BUCBP Reviewed; 463 AA.
AC Q89A52;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Replicative DNA helicase;
DE EC=3.6.4.12;
GN Name=dnaB; OrderedLocusNames=bbp_489;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC -!- FUNCTION: Participates in initiation and elongation during chromosome
CC replication; it exhibits DNA-dependent ATPase activity and contains
CC distinct active sites for ATP binding, DNA binding, and interaction
CC with DnaC protein, primase, and other prepriming proteins.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000305}.
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DR EMBL; AE016826; AAO27194.1; -; Genomic_DNA.
DR AlphaFoldDB; Q89A52; -.
DR SMR; Q89A52; -.
DR STRING; 224915.bbp_489; -.
DR EnsemblBacteria; AAO27194; AAO27194; bbp_489.
DR KEGG; bab:bbp_489; -.
DR eggNOG; COG0305; Bacteria.
DR HOGENOM; CLU_005373_0_3_6; -.
DR OMA; IEFHARI; -.
DR Proteomes; UP000000601; Chromosome.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR CDD; cd00984; DnaB_C; 1.
DR Gene3D; 1.10.860.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR InterPro; IPR007692; DNA_helicase_DnaB.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR InterPro; IPR016136; DNA_helicase_N/primase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00772; DnaB; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR SUPFAM; SSF48024; SSF48024; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00665; DnaB; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Primosome; Reference proteome.
FT CHAIN 1..463
FT /note="Replicative DNA helicase"
FT /id="PRO_0000102018"
FT DOMAIN 192..459
FT /note="SF4 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT BINDING 223..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
SQ SEQUENCE 463 AA; 52984 MW; E89C891396126031 CRC64;
MKNVKKKNLD NQVEKLIELP NSLEAEQSIL GGLMLDNEQW DYISEKISEN DFFSLSHQLI
FREMKYLLNK GYPIDLITLS ESLEQKGKLE YIGRFAYLAE LSKNVPSTAN ITTYADIVRE
RSMVRKIIKI ANKIIQAGYD PRGKTSQELL NLAESKILSI SEQNFQKNSG PKNIEELLDI
TLANIEKLFN TPYKGITGIN TGYQDLNNKT SGLQPSDLII IAARPSMGKT TFAMNICENI
AMTYKKPVLI FSLEMSGEQI MMRMLSSLSR VNQEKLRTGQ LNDEDWARIS STINILLKKK
NMYIDDSSTL TPSEMRSRSR KIYRENNGLS LIMVDYLQLI KVPSLIGNRT LEIAEISRML
KSLAKELKIP IIALSQLNRS LEQRRDKRPI NSDLRESGSL EQDADLIMFI YRDELYHEHT
DLKGIAEIII GKQRNGPIGT IKLTFNGHWS RFDNYSESKY SDE