DNAB_BUCAP
ID DNAB_BUCAP Reviewed; 465 AA.
AC Q8K932;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Replicative DNA helicase;
DE EC=3.6.4.12;
GN Name=dnaB; OrderedLocusNames=BUsg_528;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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; AE013218; AAM68069.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8K932; -.
DR SMR; Q8K932; -.
DR STRING; 198804.BUsg_528; -.
DR PRIDE; Q8K932; -.
DR EnsemblBacteria; AAM68069; AAM68069; BUsg_528.
DR KEGG; bas:BUsg_528; -.
DR eggNOG; COG0305; Bacteria.
DR HOGENOM; CLU_005373_0_0_6; -.
DR OMA; IEFHARI; -.
DR Proteomes; UP000000416; 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; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 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.
FT CHAIN 1..465
FT /note="Replicative DNA helicase"
FT /id="PRO_0000102017"
FT DOMAIN 196..463
FT /note="SF4 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT BINDING 227..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
SQ SEQUENCE 465 AA; 52721 MW; 2FAB98B336E2EF2D CRC64;
MVYPIYMAKN KSYLHQINRL KIPPHSLEAE QSVLGGLMLD NEQWDSVSEH VVADDFFSKP
HRLIFQEMQQ LLDLGHPIDL ITLSESLEQK GKLESVGRFS YLAELSKNTP STANIIAYAD
IIRERAIVRE MILVANKIAN AGYDTQGRKS EELLDYAESS VFKIAEKRFK KDSGPKNIEQ
ILDETVTSIE KLFLSPNDGV TGINTGYQDL NKKTSGLQPS ELIIIAARPS MGKTTFAMNL
CENAAMLYDK PVLIFSLEMP GEQIMMRMLA SLSRVNQARI RTGQLNDEDW SRMSGTINVL
LKKKNIYIDD SSALTPSEVR SRARRIYREN KGLTLIMVDY LQLMRVPSLS DNRTLEIAEI
SRTLKALAKE LQVPVIALSQ LNRSLEQRSD KRPVNSDLRE SGSLEQDADL IMFIYRDEIY
HENSDFKGVA EIIIGKQRNG PIGTICLTFN GHWSRFDNYC GPKYD
