ID A0A1A1X490_9MYCO Unreviewed; 792 AA.
AC A0A1A1X490;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 ORFNames=A5730_02650 {ECO:0000313|EMBL:OBF13541.1};
OS Mycobacterium sp. ACS4054.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834119 {ECO:0000313|EMBL:OBF13541.1, ECO:0000313|Proteomes:UP000091876};
RN [1] {ECO:0000313|EMBL:OBF13541.1, ECO:0000313|Proteomes:UP000091876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS4054 {ECO:0000313|EMBL:OBF13541.1,
RC ECO:0000313|Proteomes:UP000091876};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in initiation and elongation during chromosome
CC replication; it exhibits DNA-dependent ATPase activity.
CC {ECO:0000256|ARBA:ARBA00002835, 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBF13541.1}.
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DR EMBL; LZHV01000006; OBF13541.1; -; Genomic_DNA.
DR RefSeq; WP_067894335.1; NZ_LZHV01000006.1.
DR AlphaFoldDB; A0A1A1X490; -.
DR STRING; 1834119.A5730_02650; -.
DR OrthoDB; 9773982at2; -.
DR Proteomes; UP000091876; 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: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:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00984; DnaB_C; 1.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR004860; LAGLIDADG_2.
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; 2.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
DR SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS51199; SF4_HELICASE; 2.
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|RuleBase:RU362085, ECO:0000313|EMBL:OBF13541.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362085}; Primosome {ECO:0000256|RuleBase:RU362085};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 195..232
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT DOMAIN 371..475
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 567..792
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 86571 MW; D2BC059E8DB3DF2A CRC64;
MAVVDDLAPG MDSPAPSEDF GRQPPQDMAA EQAVLGGMLL SKDAIADVLE RLRPGDFYRP
AHQNVYDAIL DLYGRGEPAD AVTVAAELDR RGMLRRIGGA PYLHTLISTV PTAANAGYYA
TIVAEKALLR RLVEAGTRVV QYGYAGAEGA DVAEVVDRAQ AEIYEVADRR TTEDFVPLED
LLQPTMDEID AIASNGGVAR GVPTGFTELD EVTNGLHAGQ MIIVAARPGV GKALALDTLL
PTPSGWTTMG EVAVGDELLG DDGRPTRVVA ATEVMLGRPC FEVEFSDGTV IVADAAHQWL
TETRASRKSA QAAAVGYHRY KNQRTFAAVR TTAEIAGSLR CATLDRRLNH SVVNARALDL
PDREFLVPPY TLGAWLGDGT SAAAQITVAD PEIIMRIEAD GLVTTLQARL RTLGVLGNKH
IPVDYLRGSE TQRRALFAGL LDTDGTVTAG GAVQFSVTNQ RLACDVAELI VSLGYRCQTS
TKRVRGRRES SSVAYTLTFS TDDAVFALQR KALLHKERRA ATGTARSGSR FIVDVRPIET
VPVRCVEVDN HSHMYLASQA MVPTHNSTLG LDFLRSCSIK HRMASVIFSL EMSKSEIVMR
LLSAEAKIKL ADMRSGRMND DDWTRLARRM SEISEAPLYI DDSPNLTMME IRAKARRLKQ
KADLRLVVVD YLQLMSSGKK VESRQLEVSE FSRQLKLLAK ELEVPVVAIS QLNRGPEQRT
DKKPMLSDLR ESGSLEQDAD MVILLNRPDA FERDDPRGGE ADFILAKHRN GPTKTVTVAH
QLHLSRFANM AR
//
