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Database: UniProt
Entry: A0A1H0BR08_9FIRM
LinkDB: A0A1H0BR08_9FIRM
Original site: A0A1H0BR08_9FIRM 
ID   A0A1H0BR08_9FIRM        Unreviewed;       452 AA.
AC   A0A1H0BR08;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=SAMN05192585_12034 {ECO:0000313|EMBL:SDN48061.1};
OS   Acetanaerobacterium elongatum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetanaerobacterium.
OX   NCBI_TaxID=258515 {ECO:0000313|EMBL:SDN48061.1, ECO:0000313|Proteomes:UP000199182};
RN   [1] {ECO:0000313|EMBL:SDN48061.1, ECO:0000313|Proteomes:UP000199182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.5012 {ECO:0000313|EMBL:SDN48061.1,
RC   ECO:0000313|Proteomes:UP000199182};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FNID01000020; SDN48061.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0BR08; -.
DR   STRING; 258515.SAMN05192585_12034; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000199182; 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:SDN48061.1};
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:UP000199182}.
FT   DOMAIN          186..449
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   452 AA;  50596 MW;  2584C15BDA92434B CRC64;
     MNSFAFTETT YGQNAPFNIE AEQSVLGAII IDSSCLSTVL EYIKAEAFYR PQHQEIFSSI
     VKMFAAGKTI DFITLLEEIV IEKVFETPED AKVYLAQLAQ IVPTTSNVEA YAAIVQEKYY
     IRQLMEASKE IIETAAEGSY GAKELLDSAE QKIFDIRQGR DSKGMVKIED AIIQAYDRLQ
     KIAGEDRQKY LGLRSGFSAL DNIIYGLNKS DLILLAGRPG MGKTSFGLNI AQNVAATSHK
     KVVIFSLEMS SEQLTTRLMS SLARIPSGEF RTGNMTSAQW QELAKSSQLL ASYPILIDDA
     SGITVPEMKA KLRRIKDLGL VVIDYLQLMT TGRRSENRVQ EVSEMTRGLK IMAKELDVPV
     IVCSQLSRGP DSRTDHRPVL SDLRESGSIE QDADIVLFLY REAYYTDKPD ADRNIAECIV
     AKNRHGETDI IKLHWDGQFT QFTTLENFRD EG
//
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