ID A0A0F4LWJ7_9LACO Unreviewed; 461 AA.
AC A0A0F4LWJ7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, 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 Name=dnaB {ECO:0000313|EMBL:KJY62679.1};
GN ORFNames=JF72_00180 {ECO:0000313|EMBL:KJY62679.1};
OS Lactobacillus apis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=303541 {ECO:0000313|EMBL:KJY62679.1, ECO:0000313|Proteomes:UP000033682};
RN [1] {ECO:0000313|EMBL:KJY62679.1, ECO:0000313|Proteomes:UP000033682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hma11 {ECO:0000313|EMBL:KJY62679.1,
RC ECO:0000313|Proteomes:UP000033682};
RA Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA Vasquez A.;
RT "Comparative genomics of the lactic acid bacteria isolated from the honey
RT bee gut.";
RL Submitted (JAN-2015) 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|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:KJY62679.1}.
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DR EMBL; JXLG01000001; KJY62679.1; -; Genomic_DNA.
DR RefSeq; WP_046305721.1; NZ_KQ033999.1.
DR AlphaFoldDB; A0A0F4LWJ7; -.
DR STRING; 303541.JF72_00180; -.
DR PATRIC; fig|303541.3.peg.157; -.
DR HOGENOM; CLU_005373_0_0_9; -.
DR Proteomes; UP000033682; 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: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:KJY62679.1};
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:UP000033682}.
FT DOMAIN 178..457
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT REGION 402..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..422
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 50993 MW; 0D2C697A4080116D CRC64;
MDNIVSQQIP HDGEAEKAVL GAIFIDPDAI ADASSEVQPN DFYKKANQLI FQAMLDLSDR
GDAIDPLTLQ DELTKKNQLD DIGGIAYVSE LAIATPTAAH VSYYAKIVHR KALLRRLISA
SQKIISNAMQ DSDDVTDILD DAESEIMNVS SENNANGFRE IKDIVNAAIE EINNIPEDGS
MVTGLPTGFI ELDKMTTGFH ADELIILAAR PGVGKTAFAM NVAQYVGLHT DKTVAVFSLE
MSGEQLVQRM LASEGLINSQ HLRTGQLDEE EWRKLIVASG SLANASIYID DTPGIKMSEI
RAQARRLAKE KGNLGLIVID YLQLIEGPRS ESRQQEVSAI SRQLKKLAKE LHVPVIALSQ
LSRSVEQRQD KRPVLSDIRE SGSIEQDADI VSFLYRDDYY REENEEGSSE DHEEVGAEDD
NGEVEVIIEK NRSGSRGTIK LMFSKPYNRF SNLDYSHDQP G
//
