ID A0A2S9Z138_9CORY Unreviewed; 551 AA.
AC A0A2S9Z138;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:PRQ11058.1};
GN ORFNames=C1Y63_07970 {ECO:0000313|EMBL:PRQ11058.1};
OS Corynebacterium sp. 13CS0277.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=2071994 {ECO:0000313|EMBL:PRQ11058.1, ECO:0000313|Proteomes:UP000238368};
RN [1] {ECO:0000313|EMBL:PRQ11058.1, ECO:0000313|Proteomes:UP000238368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13CS0277 {ECO:0000313|EMBL:PRQ11058.1,
RC ECO:0000313|Proteomes:UP000238368};
RA Busch A., Hotzel H., Tomaso H., Thomas P., Nguyen T.;
RT "Corynebacterium vierzehnheiligense, a novel Corynebacterium species
RT recovered from Common kestrel (Falco tinnunculus).";
RL Submitted (JAN-2018) 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}.
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:PRQ11058.1}.
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DR EMBL; PPDL01000016; PRQ11058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S9Z138; -.
DR OrthoDB; 9773982at2; -.
DR Proteomes; UP000238368; 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:PRQ11058.1};
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:UP000238368}.
FT DOMAIN 287..551
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 59512 MW; 816F98BFC37A5187 CRC64;
MTNPTSPDPS TAADGTSPAA ASPAEGEDFA VAGVASSFDD DSYVPPGDLD APPPEADYSP
DFAPTTAFGG GGSSDWNGGG GRRRGGRDSF SGKDFVSSRR GFEPPGPEGR DFGRQPPHDN
EAEQGVLGAM LLSSSTIADI VEELSPEDFY KPAHQIIYRA ILDLYTENKE VDPVIVSARL
DRANDLTRVG GAPYLHTLVQ AVPTAANARY YAEIVAEKAI LRRLVDAGTR VVQLGYEGTE
GAEVDAVVDM AQQEVFAIAQ KKSAEDYSPL SEIIRPTMDE LDQIAAHGGL AQGVPTGFVD
LDNLTNGLHG GQMIIVAARP GVGKSTLALD FMRSCSITHH KTSVLFSLEM SKSEVAMRLL
SAEAEVKLSD MRSGRMTDEQ WAKLANRVGE ISEAPLYIDD SPNLTMMEIR SKARRLAQQK
GLDLIVVDYL QLMSSGKKVE SRQQEVSEFS RQLKLLAKEL DVPLIAISQL NRGPESRTDK
RPQLADLRES GSLEQDADMV MLLYRPDSQD KDDARAGEAD IILAKHRGGP IDTVSVAHQL
HYSRFANLAR G
//
