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Database: UniProt
Entry: A0A0R2BH85_9LACO
LinkDB: A0A0R2BH85_9LACO
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ID   A0A0R2BH85_9LACO        Unreviewed;       464 AA.
AC   A0A0R2BH85;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=FC84_GL000080 {ECO:0000313|EMBL:KRM78925.1};
OS   Lapidilactobacillus dextrinicus DSM 20335.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lapidilactobacillus.
OX   NCBI_TaxID=1423738 {ECO:0000313|EMBL:KRM78925.1, ECO:0000313|Proteomes:UP000051813};
RN   [1] {ECO:0000313|EMBL:KRM78925.1, ECO:0000313|Proteomes:UP000051813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20335 {ECO:0000313|EMBL:KRM78925.1,
RC   ECO:0000313|Proteomes:UP000051813};
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:KRM78925.1}.
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DR   EMBL; AYYK01000008; KRM78925.1; -; Genomic_DNA.
DR   RefSeq; WP_057756318.1; NZ_AYYK01000008.1.
DR   AlphaFoldDB; A0A0R2BH85; -.
DR   STRING; 1423738.FC84_GL000080; -.
DR   PATRIC; fig|1423738.3.peg.81; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000051813; 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:KRM78925.1};
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:UP000051813}.
FT   DOMAIN          178..460
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   REGION          403..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   464 AA;  51924 MW;  AD0F91894700F67E CRC64;
     MDNLQNQLPP HSEEAEQAVL GSIFLRPDAI VDAMEYLVPE DFYRRAHQII FQAMINISDR
     QDAIDVVTIR SELESHHQFE DVGGAAYIAE LASNTPSYRN VGYYAKIVEE KSMLRRLIGT
     ATHIVNESYQ QDEDATTILD NAEKQIMDVS QNRNRNGFKQ ISDVLLESMA NIDELTKQDS
     TITGLSTGYA DLDRITAGLH EDELIILAAR PGVGKTAFAL NIAQNIGTKN EDVSIAIFSL
     EMGAEQLVNR MICAEGNIES NHLRTGQLTD EEWDHLMVAM ASLSKAKIYI DDTPGVKMAE
     IRAKCRRLQQ EQKNLGLIVI DYLQLIEGSG QENRQQEVSA ISRQLKMLAK ELHVPVIALS
     QLSRGVEQRQ DKRPVLSDIR ESGSIEQDAD IVAFLYREDY YRSEDEDDDT GSAPAQSSDD
     DQNVGPVEVI IEKNRAGARG TVQLLFVKSY NKFASVSNRD MMPQ
//
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