ID A0A0B5DEY8_9CORY Unreviewed; 497 AA.
AC A0A0B5DEY8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=B842_12370 {ECO:0000313|EMBL:AJE34319.1};
OS Corynebacterium humireducens NBRC 106098 = DSM 45392.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1223515 {ECO:0000313|EMBL:AJE34319.1, ECO:0000313|Proteomes:UP000031524};
RN [1] {ECO:0000313|EMBL:AJE34319.1, ECO:0000313|Proteomes:UP000031524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFC-5 {ECO:0000313|Proteomes:UP000031524};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium humireducens DSM 45392(T),
RT isolated from a wastewater-fed microbial fuel cell.";
RL Submitted (APR-2013) 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|ARBA:ARBA00002835, 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; CP005286; AJE34319.1; -; Genomic_DNA.
DR RefSeq; WP_040087035.1; NZ_CP005286.1.
DR AlphaFoldDB; A0A0B5DEY8; -.
DR STRING; 1223515.B842_12370; -.
DR KEGG; chm:B842_12370; -.
DR HOGENOM; CLU_005373_0_0_11; -.
DR OrthoDB; 9773982at2; -.
DR Proteomes; UP000031524; Chromosome.
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:AJE34319.1};
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}.
FT DOMAIN 233..497
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 54752 MW; 253BE38B1A9B5530 CRC64;
MTSGIGDASF DDDYVPPSEP DLPEDPGALV PAFQAPERQG GRPERRRNRG NTGAAFGEYR
QPPHDREAEQ GVLGAMLLSP NTVVEIIGEL SPEDFYHPAH QLIYSAMIDL FGESKDIDPV
IVAGRLDRHN DLERVGGAPY LHTLISSVPT AANARYYAEI VAEKAILRRL VDAGTRVVQL
GYEGNEGAEV ETVLDLAQQE VFAIAQKTET EDYAVLADII EPTMEELDQI ANLGGLAQGV
PTGFVDLDNL TNGLHGGQMI IVAARPGVGK STIALDFMRS CSIKHNKASV IFSLEMSKSE
IVMRLMSAET SIKLSDMRSG RMTDESWTTL ANRVGQISEA PLFIDDSPNL TMMEIRSKAR
RLKQKHDLQL IVIDYLQLMS SGKKVESRQQ EVSEFSRQLK LLAKELDVPL VAISQLNRGP
EARTDKRPQL ADLRESGSLE QDADMVMLLY RPDSQDREDV RAGEADIILA KHRGGPIDTV
TVAHQLHFSR FVDMARG
//
