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Database: UniProt
Entry: K7A607_9ALTE
LinkDB: K7A607_9ALTE
Original site: K7A607_9ALTE 
ID   K7A607_9ALTE            Unreviewed;       430 AA.
AC   K7A607;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
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:GAC30900.1};
GN   ORFNames=GPAL_4061 {ECO:0000313|EMBL:GAC30900.1};
OS   Glaciecola pallidula DSM 14239 = ACAM 615.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Glaciecola.
OX   NCBI_TaxID=1121922 {ECO:0000313|EMBL:GAC30900.1, ECO:0000313|Proteomes:UP000006251};
RN   [1] {ECO:0000313|EMBL:GAC30900.1, ECO:0000313|Proteomes:UP000006251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACAM 615 {ECO:0000313|EMBL:GAC30900.1,
RC   ECO:0000313|Proteomes:UP000006251};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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}.
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:GAC30900.1}.
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DR   EMBL; BAEQ01000068; GAC30900.1; -; Genomic_DNA.
DR   AlphaFoldDB; K7A607; -.
DR   STRING; 1121922.GCA_000428905_03213; -.
DR   Proteomes; UP000006251; 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|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          158..425
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   430 AA;  47861 MW;  1DB1CFBD6BE954BD CRC64;
     MIAPDSWDKV AEIVVESDFY NRSHRTIFGA IIKLLSNNQS VDTVTVKDTL AQSGKLDEAG
     GFSYLIELAK NTPSAANVSA YASVIRERAI VRELIGVAHD IADVGYNPEG RNSADILDFA
     ESKVFEIAEK RTGENEGPKD ITTVLTKTVN RLDELVKQGL EITGVSTGYT DLDSKTSGLQ
     RSDLIIVAAR PSMGKTTFAM NLCENAMMLQ DKPVLVFSLE MPAEQIMMRM LASLSRVNQT
     HIRTAQLDDE EWARMSGTIK TLKKKDNLYI DDSSGLTPME LRTRARKIAR DKGGLSLIMI
     DYLQLMRVPS LSENRTLEIA EISRSLKALA KELEVPVVAL SQLNRTLEQR ADKRPINSDL
     RESGSIEQDA DLIMFIYRDE VYNEASEMKG IAEIIIGKQR NGPIGTSRLT FQGQFSRFDN
     YAGPAFEDEY
//
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