DNAB_PASMU
ID DNAB_PASMU Reviewed; 467 AA.
AC Q9CNL6;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Replicative DNA helicase;
DE EC=3.6.4.12;
GN Name=dnaB; OrderedLocusNames=PM0412;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02496.1; -; Genomic_DNA.
DR RefSeq; WP_005726119.1; NC_002663.1.
DR AlphaFoldDB; Q9CNL6; -.
DR SMR; Q9CNL6; -.
DR STRING; 747.DR93_1186; -.
DR EnsemblBacteria; AAK02496; AAK02496; PM0412.
DR GeneID; 62224662; -.
DR KEGG; pmu:PM0412; -.
DR HOGENOM; CLU_005373_0_0_6; -.
DR OMA; IEFHARI; -.
DR Proteomes; UP000000809; 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; Reference proteome.
FT CHAIN 1..467
FT /note="Replicative DNA helicase"
FT /id="PRO_0000102027"
FT DOMAIN 193..461
FT /note="SF4 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT BINDING 224..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
SQ SEQUENCE 467 AA; 52011 MW; 7BE33C8CA32AE87C CRC64;
MAKKNAQIPS KPLEQGIVPP HSLEAEQSVL GGILIHPAHW DSISDMLIAD DFYLAAHRVI
FQEMENLLRQ GKPIDLINLY EFLREKNLSE DVGGFAYLAE LSKNTPSVSN IVSYAAIVRD
RAILRDLISV SNDVAQSCYT TKGMEVKDIL DEAERKVFAI SEKRTTSNEG PQNICAILEK
TIDRIELLSK TEGHNGITGV STGFDALDKK TAGLQPSDLI IVAARPSMGK TTFAMNLCEN
AALKSDKPVL VFSLEMPAEQ IMMRSLASLS RVDQTKIRTG QGLDQSDWSK IGSTMGLFAN
KPNLYIDDSS GLTPTELRSR ARRVYRENGG LSLIMVDYLQ LMRAPGFADN RTLEIAEISR
SLKALAKELE VPVIALSQLN RTLENRADKR PVNSDLRESG SIEQDADLIM FIYRDEVYNE
NSEDKGVAEI IIGKQRNGPI GRVRLAFRGQ FSRFDNLAEQ RDIRDDY