ID A0A3N5BG72_9STAP Unreviewed; 464 AA.
AC A0A3N5BG72;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=EDD62_1385 {ECO:0000313|EMBL:RPF56726.1};
OS Abyssicoccus albus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae.
OX NCBI_TaxID=1817405 {ECO:0000313|EMBL:RPF56726.1, ECO:0000313|Proteomes:UP000277108};
RN [1] {ECO:0000313|EMBL:RPF56726.1, ECO:0000313|Proteomes:UP000277108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29158 {ECO:0000313|EMBL:RPF56726.1,
RC ECO:0000313|Proteomes:UP000277108};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
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|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:RPF56726.1}.
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DR EMBL; RKRK01000003; RPF56726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N5BG72; -.
DR OrthoDB; 9773982at2; -.
DR Proteomes; UP000277108; 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:RPF56726.1};
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:UP000277108}.
FT DOMAIN 177..458
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
SQ SEQUENCE 464 AA; 52395 MW; A1EF9695F95A53F9 CRC64;
MFEQNQHIPF SIDAEKSVLG AILIDPEHGL QRAQNLLPQD FYYQNHQHIF ESMLKLYDKN
EQVDTTTLVN ALTKEGVLQD IGGPLYIAEL AQFVPTSRNI DYYIEIVENY SLKRQLIYAA
QDIARDGMNE EIDLDDLLSE AEKMISSIGQ GRGSEGFKDI NSVMHEVYEM IEQRTRSNGE
TTGIPSGYAS LDRMTSGFGK NDLIILAARP SVGKTAFALN IAQNIALNKQ DDYSVAVFSL
EMGADQLATR MVCSVANLDS NKLRTGQFDQ SDWDRFIFAI GELGKSKMFI DDTPGIKIND
IRAKSRALKQ EHGLDMIIID YLQLIQGSGL RKGENRQQEV SEISRTLKEI ARELEVPVIA
LSQLSRGVEQ RQDKRPMLSD IRESGSIEQD ADIVAFLYRD DYYQREAEDE DGNVSQNDQE
DNGIVEVILA KHRNGPTGTV PLIFVKKHNK FNSIDERYAE QYMG
//
