UniProt: A0A1C3K7W1

Database: UniProt
Entry: A0A1C3K7W1_9BURK

LinkDB:  A0A1C3K7W1_9BURK 
Original site:  A0A1C3K7W1_9BURK

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (11)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (22)   

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ID   A0A1C3K7W1_9BURK        Unreviewed;       459 AA.
AC   A0A1C3K7W1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=ODI_00589 {ECO:0000313|EMBL:SBT27600.1}, ODI_R1593
GN   {ECO:0000313|EMBL:SOE48695.1};
OS   Orrella dioscoreae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Orrella.
OX   NCBI_TaxID=1851544 {ECO:0000313|EMBL:SBT27600.1, ECO:0000313|Proteomes:UP000078558};
RN   [1] {ECO:0000313|EMBL:SBT27600.1, ECO:0000313|Proteomes:UP000078558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Orrdi1 {ECO:0000313|EMBL:SBT27600.1};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SOE48695.1, ECO:0000313|Proteomes:UP000078558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Orrdi1 {ECO:0000313|EMBL:SOE48695.1};
RA   de Groot N.N.;
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FLRC01000055; SBT27600.1; -; Genomic_DNA.
DR   EMBL; LT907988; SOE48695.1; -; Genomic_DNA.
DR   RefSeq; WP_067759494.1; NZ_LT907988.1.
DR   AlphaFoldDB; A0A1C3K7W1; -.
DR   STRING; 1851544.ODI_00589; -.
DR   KEGG; odi:ODI_R1593; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000078558; Chromosome i.
DR   Proteomes; UP000078558; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078558}.
FT   DOMAIN          190..458
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   459 AA;  50267 MW;  D6CE0DEBEA6F6933 CRC64;
     MNSPTSDKEL EYLRVPPHSV EAEQSVLGGL LLDNGAWDRI GDVLSENDFY RHDHRLIWQH
     IARLISLSRP ADVVTVNESL DTAGKSAEAG GIAYLNALAH NTPSAANIRR YGEIVRERSV
     LRKLVTIADE IAAAAFNPNG KDARQLLDDA ESKVFKIAEE SASNTSGFKE IQPLLTQVVE
     RIDELYHRES DSDVTGVPTG FADLDKMTSG LQGGDLIIVA GRPSMGKTSF SMNIGEHIAI
     EQGLPVAVFS MEMGAVQLAQ RMLGSVGLLD QHRMRTGKLT AEDWPRVTHA VQKMQDAQVY
     IDETPALSPM EVRARARRLA RQCGQLGLII IDYMQLMSGN GGASSENRAA EVSEISRSLK
     GLAKELNCPL IALSQLNRSL EQRPNKRPVM SDLRESGAIE QDADVILFIY RDEVYNPDSP
     DKGSAEIIIG KQRNGPIGTV RLTFQGSSTR FLNFSAAGY
//

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