ID A0A370DN93_9GAMM Unreviewed; 468 AA.
AC A0A370DN93;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=DIZ78_09980 {ECO:0000313|EMBL:RDH85777.1};
OS endosymbiont of Escarpia spicata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2200908 {ECO:0000313|EMBL:RDH85777.1, ECO:0000313|Proteomes:UP000254771};
RN [1] {ECO:0000313|EMBL:RDH85777.1, ECO:0000313|Proteomes:UP000254771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1462 {ECO:0000313|EMBL:RDH85777.1};
RX PubMed=30022157;
RA Li Y., Liles M.R., Halanych K.M.;
RT "Endosymbiont genomes yield clues of tubeworm success.";
RL ISME J. 0:0-0(2018).
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:RDH85777.1}.
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DR EMBL; QFXE01000012; RDH85777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370DN93; -.
DR Proteomes; UP000254771; 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:UP000254771}.
FT DOMAIN 196..462
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
SQ SEQUENCE 468 AA; 51548 MW; A41E911AC6D66E47 CRC64;
MSEPDYPQEI ADYPDHAAEA LKVPPHSIQG EQSVLGALML DNATWDQVAD LVVQDDYYRK
EHRLIFGAIA SLAENSQPFD VVTLAETLEQ QGALEDAGGL PYLVRLVEDT PSAANIKSYA
GIVREYSVMR HLISVGTEIS DSAFHPQGRD SAELLDNAER KVFEIAEQRS KGGGGFSPIK
SLLTKAVDRI EALFQQDEPI TGESTGFTDF DAMTSGLQPA DLIIVAGRPS MGKTTFAMNV
AENVAIKGKK AVAVFSMEMP GDSLAMRMMS SLGHIDQLRV RTGKLEDDEW PRLTSAVSML
AETKLFIDDT PAMSPTEVRA RARRLKRENP DLGLIVLDYL QLMQAPGEGD NRTNEISAIS
RSLKALAKEL SVPVMALSQL NRSLESRTNK RPIMSDLRES GAIEQDADLI VFIYRDEVYN
EDSTDKGLAE IIIGKQRNGP IGTTRLTFLG KYTKFENYID DGYSDEGY
//
