ID A0A1Y6HC41_9XANT Unreviewed; 475 AA.
AC A0A1Y6HC41;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Replicative DNA helicase {ECO:0000256|ARBA:ARBA00021957, ECO:0000256|RuleBase:RU362085};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU362085};
GN Name=dnaB {ECO:0000313|EMBL:SMR02707.1};
GN ORFNames=PD5205_01397 {ECO:0000313|EMBL:SMR02707.1};
OS Xanthomonas fragariae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=48664 {ECO:0000313|EMBL:SMR02707.1, ECO:0000313|Proteomes:UP000195953};
RN [1] {ECO:0000313|EMBL:SMR02707.1, ECO:0000313|Proteomes:UP000195953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PD5205 {ECO:0000313|EMBL:SMR02707.1};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003574, ECO:0000256|RuleBase:RU362085}.
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 Evidence={ECO:0000256|ARBA:ARBA00001665,
CC ECO:0000256|RuleBase:RU362085};
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000256|ARBA:ARBA00008428, ECO:0000256|RuleBase:RU362085}.
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DR EMBL; LT853885; SMR02707.1; -; Genomic_DNA.
DR RefSeq; WP_002810659.1; NZ_ORZZ01000155.1.
DR AlphaFoldDB; A0A1Y6HC41; -.
DR STRING; 48664.BER92_06710; -.
DR GeneID; 61894940; -.
DR KEGG; xfr:BER92_06710; -.
DR eggNOG; COG0305; Bacteria.
DR OrthoDB; 9773982at2; -.
DR Proteomes; UP000195953; Chromosome 1.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00665; DnaB; 1.
DR PANTHER; PTHR30153:SF2; REPLICATIVE DNA HELICASE; 1.
DR PANTHER; PTHR30153; REPLICATIVE DNA HELICASE DNAB; 1.
DR Pfam; PF00772; DnaB; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362085};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU362085};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362085};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU362085};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362085};
KW Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|RuleBase:RU362085}.
FT DOMAIN 204..470
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 52847 MW; 329FDFD13E1FD576 CRC64;
MSARPGFRSK RNRDRDDDYD RPEPRLDQLR VPPHSVEAEQ AVLGGLMLAP DAFDRINDQL
TENDFYRRDH RLIYRAIHEL AEKDRPFDAV TLGEWFESQG KLEQVGDGAY LIELASTTPS
AANIVAYAEI VRDKAVLRQL IEVGTTIVND GFQPEGRESV ELLSSAEKAV FKIAEAGARG
RTDFVAMPSA LKDAFEELRI RFENGGNITG LPTGYTDFDA MTAGLQPTDL IILAARPAMG
KTTLALNIAE YVAIKSKKGV AVFSMEMSAS QLAMRLISSN GRINAQRLRT GALEDEDWAR
VTGAIKMLKE TKIFIDDTPG VSPEVLRSKC RRLKREHDLG LIVIDYLQLM SVPGNSENRA
TEISEISRSL KGLAKELNVP VIALSQLNRS LETRTDKRPV MADLRESGAI EQDADMIVFI
YRDDYYNKEN SPDKGLAEII IGKHRGGPTG SCKLKFFGEY TRFDNLAHDS VGSFE
//
