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Database: UniProt
Entry: C4III0_CLOBU
LinkDB: C4III0_CLOBU
Original site: C4III0_CLOBU 
ID   C4III0_CLOBU            Unreviewed;       493 AA.
AC   C4III0;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 62.
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   Name=dnaB {ECO:0000313|EMBL:EEP53150.1};
GN   ORFNames=CLP_2216 {ECO:0000313|EMBL:EEP53150.1};
OS   Clostridium butyricum E4 str. BoNT E BL5262.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP53150.1, ECO:0000313|Proteomes:UP000003081};
RN   [1] {ECO:0000313|EMBL:EEP53150.1, ECO:0000313|Proteomes:UP000003081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E4 str. BoNT E BL5262 {ECO:0000313|Proteomes:UP000003081};
RA   Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C.,
RA   Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.;
RL   Submitted (AUG-2009) 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}.
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:EEP53150.1}.
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DR   EMBL; ACOM01000005; EEP53150.1; -; Genomic_DNA.
DR   RefSeq; WP_003412462.1; NZ_ACOM01000005.1.
DR   AlphaFoldDB; C4III0; -.
DR   STRING; 1492.ATN24_09030; -.
DR   eggNOG; COG0305; Bacteria.
DR   HOGENOM; CLU_005373_0_0_9; -.
DR   Proteomes; UP000003081; 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:UP000003081}.
FT   DOMAIN          174..492
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   REGION          420..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  55437 MW;  FB96287AF94C6224 CRC64;
     MNNRVMPSSL EAEQTLIGCI LNSTDRFIEA DTILNYEDFY VDKHKKIYET IKKLCDNSVS
     VDTVTVVDNL KKKGILEECG GITYLSNLET GAVNYSSIEN YARIVKEKSD RRALVKTGSK
     LMEDAFEKED VKEAIEDAEK CIFNVSASKN ITGPERIDTI LEKAFVKLEK RCKNGGGLVG
     ISTGFKGIDD ITGGLKPGEF VIVAARPSMG KTAFALNIAQ SASRTSSVII FSLEMETESL
     LNRMISSSCM IKMNDIQSGT LTDDQFVRIM KRTSELGKRN LYIDDKSTML SDIKALCRKQ
     KLQKGLDVIV IDYLQLIRTT MKANQREQEV SYISKELKSL AKELNITVIA LSQLSRAPET
     RNDHRPMLSD LRESGSIEQD ADIIHFIYRD AYYNNNKKKK GKKKDSEGIQ GEFKINNSLS
     TSVNKSTADN SGNLNINKNH ENNMRKDVEY NKKPDDIIAE IITAKNRNGQ TKTNKLNWIG
     EYQRFTSADV IKQ
//
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