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Database: UniProt
Entry: A0A0U1QP40_9BACL
LinkDB: A0A0U1QP40_9BACL
Original site: A0A0U1QP40_9BACL 
ID   A0A0U1QP40_9BACL        Unreviewed;       456 AA.
AC   A0A0U1QP40;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=SINU_08350 {ECO:0000313|EMBL:KLI02386.1};
OS   Sporolactobacillus inulinus CASD.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC   Sporolactobacillus.
OX   NCBI_TaxID=1069536 {ECO:0000313|EMBL:KLI02386.1, ECO:0000313|Proteomes:UP000035553};
RN   [1] {ECO:0000313|EMBL:KLI02386.1, ECO:0000313|Proteomes:UP000035553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CASD {ECO:0000313|EMBL:KLI02386.1,
RC   ECO:0000313|Proteomes:UP000035553};
RX   PubMed=21952540; DOI=10.1128/JB.05934-11;
RA   Yu B., Su F., Wang L., Xu K., Zhao B., Xu P.;
RT   "Draft genome sequence of Sporolactobacillus inulinus strain CASD, an
RT   efficient D-lactic acid-producing bacterium with high-concentration lactate
RT   tolerance capability.";
RL   J. Bacteriol. 193:5864-5865(2011).
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:KLI02386.1}.
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DR   EMBL; AFVQ02000103; KLI02386.1; -; Genomic_DNA.
DR   RefSeq; WP_010027372.1; NZ_AFVQ02000103.1.
DR   AlphaFoldDB; A0A0U1QP40; -.
DR   STRING; 1069536.SINU_08350; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000035553; 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:KLI02386.1};
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:UP000035553}.
FT   DOMAIN          179..447
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   456 AA;  50894 MW;  91DC6EDEAA0A4668 CRC64;
     MSDLFADRIP PHNMEAEQAV LGAVFLEPSS VITASEVLIP EDFYRTSHQL IFSVMLELSE
     KNEPVDVVTV TNALQSSKRL EEVGGVSYLA ELADSAPTAA NIEYYCSIVA EKATLRRLIR
     TATQIVSEGY TSEDGIETVL DDAERRILEV AERKRSGEFQ AIKDVLMETY DNIEMLQSRQ
     DDVTGTPTGF LELDRMTAGF QKSDLIIVAA RPSVGKTAFA LNIAQNVAIK NEANVAIFSL
     EMGAKQLAMR MLCAEGNINA QKLRTGKLED EDWQKLTMAM GSLSRAGIYI DDSPGVRVND
     IRSKCRRLKQ EKGLDMVVID YLQLIMGSGS SGRQENRQQE VSEISRMLKQ MARELDVPVI
     ALSQLSRGVE ARQDKRPMMS DIRESGSIEQ DADVVAFLYR DDYYNKESEK QNIIEIIIAK
     QRNGPVGTVE LAFVKEYSKF VNIDRKHSDE DVPRGA
//
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