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Database: UniProt
Entry: A0A0R1WP99_9LACO
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ID   A0A0R1WP99_9LACO        Unreviewed;       464 AA.
AC   A0A0R1WP99;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-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=FC40_GL001414 {ECO:0000313|EMBL:KRM19722.1};
OS   Ligilactobacillus hayakitensis DSM 18933 = JCM 14209.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1423755 {ECO:0000313|EMBL:KRM19722.1, ECO:0000313|Proteomes:UP000051054};
RN   [1] {ECO:0000313|EMBL:KRM19722.1, ECO:0000313|Proteomes:UP000051054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18933 {ECO:0000313|EMBL:KRM19722.1,
RC   ECO:0000313|Proteomes:UP000051054};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRM19722.1}.
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DR   EMBL; AZGD01000034; KRM19722.1; -; Genomic_DNA.
DR   RefSeq; WP_025022147.1; NZ_BAML01000007.1.
DR   AlphaFoldDB; A0A0R1WP99; -.
DR   STRING; 1423755.FC40_GL001414; -.
DR   PATRIC; fig|1423755.3.peg.1501; -.
DR   eggNOG; COG0305; Bacteria.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000051054; 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:RHEA.
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; 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   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:KRM19722.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362085}; Primosome {ECO:0000256|RuleBase:RU362085};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051054}.
FT   DOMAIN          180..459
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   464 AA;  51669 MW;  5C8B2A916D9E8AE9 CRC64;
     MDNELLNENL PPQNIEAEQA VLGAIFLNQD ALADAMEYLE PNDFYRRAHQ LLFQAMIDLN
     DDSEAIDVLT IQDRLTKNNQ LEDVGGVIYI AELAGSVPTA ANIVHYAKIV EEKSMLRRLI
     LAANNIISKA NDNEQDVPAL LDDAERQIMN VSERNSRSGF RAIKDVLDDA LVEIDRLSKQ
     DSDITGISTG YREIDKMTAG LQPDNLIILA ARPAVGKTAF ALNIAQNVAR DNDVSVAIFS
     LEMSAESLVN RLLCAEGSIN ANDLRTGQLD ENEWSNLVVA MGSLSRSQIF IDDTPGIKMA
     EIRAKCRRLA KERGNLGLVV VDYLQLIEGS NKESRQQEVS EISRQLKKLS KELSIPIIAL
     SQLSRGVEQR QDKRPVLSDI RESGSIEQDA DIVAFLYRDD YYERGEKNDD DSQEEVNPQN
     QDVGEVELII EKNRAGARGT VKLLFIKSYN KFTGIAYGQQ EPAM
//
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