ID   H3RJ85_PANSE            Unreviewed;       468 AA.
AC   H3RJ85;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   07-JUN-2017, entry version 28.
DE   RecName: Full=Replicative DNA helicase {ECO:0000256|RuleBase:RU362085};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU362085};
GN   Name=dnaB {ECO:0000313|EMBL:EHT98342.1};
GN   ORFNames=CKS_4694 {ECO:0000313|EMBL:EHT98342.1}, DSJ_03115
GN   {ECO:0000313|EMBL:ARF48449.1};
OS   Pantoea stewartii subsp. stewartii DC283.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=660596 {ECO:0000313|EMBL:EHT98342.1, ECO:0000313|Proteomes:UP000005050};
RN   [1] {ECO:0000313|EMBL:EHT98342.1, ECO:0000313|Proteomes:UP000005050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DC283 {ECO:0000313|EMBL:EHT98342.1,
RC   ECO:0000313|Proteomes:UP000005050};
RX   PubMed=22111898; DOI=10.1111/j.1365-2958.2011.07926.x;
RA   Wang X., Yang F., von Bodman S.B.;
RT   "The genetic and structural basis of two distinct terminal side branch
RT   residues in stewartan and amylovoran exopolysaccharides and their
RT   potential role in host adaptation.";
RL   Mol. Microbiol. 83:195-207(2012).
RN   [2] {ECO:0000313|EMBL:EHT98342.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DC283 {ECO:0000313|EMBL:EHT98342.1};
RA   Biehl B.S., Ding Y., Dugan-Rocha S.P., Gibbs R.A., Glasner J.D.,
RA   Kovar C., Muzny D.M., Neeno-Eckwall E.C., Perna N.T., Qin X.,
RA   von Bodman S.B., Weinstock G.M.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ARF48449.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DC283 {ECO:0000313|EMBL:ARF48449.1};
RA   Duong D.A., Stevens A.M., Jensen R.V.;
RT   "Complete Genome Assembly of Pantoea stewartii subsp. stewartii DC283,
RT   a Corn Pathogen.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates in initiation and elongation during
CC       chromosome replication; it exhibits DNA-dependent ATPase activity
CC       and contains distinct active sites for ATP binding, DNA binding,
CC       and interaction with DnaC protein, primase, and other prepriming
CC       proteins. {ECO:0000256|RuleBase:RU362085}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC       {ECO:0000256|RuleBase:RU362085}.
CC   -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC       {ECO:0000256|RuleBase:RU362085}.
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DR   EMBL; CP017581; ARF48449.1; -; Genomic_DNA.
DR   EMBL; AHIE01000037; EHT98342.1; -; Genomic_DNA.
DR   RefSeq; WP_006121562.1; NZ_AHIE01000037.1.
DR   EnsemblBacteria; EHT98342; EHT98342; CKS_4694.
DR   PATRIC; fig|660596.6.peg.4366; -.
DR   OrthoDB; POG091H023D; -.
DR   Proteomes; UP000005050; Unassembled WGS sequence.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR   CDD; cd00984; DnaB_C; 1.
DR   Gene3D; 1.10.860.10; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
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; 2.
DR   TIGRFAMs; TIGR00665; DnaB; 1.
DR   PROSITE; PS51199; SF4_HELICASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362085};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005050};
KW   DNA replication {ECO:0000256|RuleBase:RU362085,
KW   ECO:0000256|SAAS:SAAS00740714};
KW   DNA-binding {ECO:0000256|RuleBase:RU362085,
KW   ECO:0000256|SAAS:SAAS00740674};
KW   Helicase {ECO:0000256|RuleBase:RU362085, ECO:0000313|EMBL:EHT98342.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU362085,
KW   ECO:0000313|EMBL:EHT98342.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362085};
KW   Primosome {ECO:0000256|RuleBase:RU362085}.
FT   DOMAIN      197    464       SF4 helicase. {ECO:0000259|PROSITE:
FT                                PS51199}.
SQ   SEQUENCE   468 AA;  52367 MW;  210F0DE0C9BF8D41 CRC64;
     MAGNKPTNKS NETQDRQLEG VKMPPHSLEA EQSVLGGLML DNERWDNVSE RVVANDFFNR
     SHRLIFSEMQ RLLENSKPID LITLSESLET RGELEMAGGF AYLAELAKNT PSAANIGAYA
     DIVRERAVVR EMIAVANQIA DAGYDPQGRS SEDLLDFAES NVFKIAEARA NKDDGPKNIE
     QILEATVSRI ESLFQTPHDG VTGIDTGYQD LNKKTAGLQR SDLIIVAARP SMGKTTFAMN
     LCENAAMLQD KPVLIFSLEM PSEQIMMRML ASLSRVDQTR IRTGQLDDED WARISGTMGI
     LLEKKNMYID DSSGLTPTEV RSRARRIYRE NGGLSLIMID YLQLMRVPAL SDNRTLEIAE
     ISRSLKALAK ELNVPVVALS QLNRSLEQRA DKRPVNSDLR ESGSIEQDAD LIMFIYRDEV
     YHENSDLKGI AEIILGKQRN GPIGTVRLTF NGQWSRFDNY AGPQYDDE
//