ID A0A3G6J8N3_9CORY Unreviewed; 468 AA.
AC A0A3G6J8N3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:AZA12374.1};
GN ORFNames=CGERO_10475 {ECO:0000313|EMBL:AZA12374.1};
OS Corynebacterium gerontici.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=2079234 {ECO:0000313|EMBL:AZA12374.1, ECO:0000313|Proteomes:UP000271587};
RN [1] {ECO:0000313|EMBL:AZA12374.1, ECO:0000313|Proteomes:UP000271587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W8 {ECO:0000313|EMBL:AZA12374.1,
RC ECO:0000313|Proteomes:UP000271587};
RA Kleinhagauer T., Glaeser S.P., Spergser J., Ruckert C., Kaempfer P.,
RA Busse H.-J.;
RL Submitted (NOV-2018) 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}.
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DR EMBL; CP033897; AZA12374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G6J8N3; -.
DR KEGG; cgk:CGERO_10475; -.
DR OrthoDB; 9773982at2; -.
DR Proteomes; UP000271587; Chromosome.
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:InterPro.
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; 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 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 SMART; SM00382; AAA; 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|RuleBase:RU362085, ECO:0000313|EMBL:AZA12374.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000271587}.
FT DOMAIN 204..468
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 468 AA; 51986 MW; D0163E9C6869ED54 CRC64;
MTNPSFDDDY FPPEPPADDA PTPRGPAREA RREPQDIEAE QSVLGAIMLS PHLVADIIEL
LRPEDFYRPA HQMIYEAIID LYSDNKEIDA VIVTGQLDRR NQLERVGGAP YVHTLISSVP
TSSNARYYAE LVAEKALLRQ LVHAGTRVAQ MGYEGTEGAE VEQVIDLAQQ EVFKIAKKNK
ATDYKSLSEI SEPTMRMIEE IDAQGGLAKG VPTGFADLDQ LTNGLHGGQM IIVAARPGVG
KSTLALDFVR SCTIDQGKAA VIFSLEMSSE EIAMRLFSAE SEVKLSDMRG GHLNQEQWTR
LVDRVGRIDQ APLFIDDSAN LTMMEIRAKA RKLKQDHDIQ LIILDYLQLM SSGKRVESRQ
QEVSEFSRQL KLLAKELDVP LVAISQLNRG PESRTDKKPQ VADLRESGSL EQDADMVMLL
YRPDSQNTDD ERAGEADIIL AKHRGGPIGT VSVAHQLHFS RFVNMPRG
//
