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Database: UniProt
Entry: A0A1E3TLK8_MYCSH
LinkDB: A0A1E3TLK8_MYCSH
Original site: A0A1E3TLK8_MYCSH 
ID   A0A1E3TLK8_MYCSH        Unreviewed;       457 AA.
AC   A0A1E3TLK8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=MSP7336_01036 {ECO:0000313|EMBL:SRX92810.1};
OS   Mycobacterium shimoidei.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=29313 {ECO:0000313|EMBL:SRX92810.1, ECO:0000313|Proteomes:UP000252015};
RN   [1] {ECO:0000313|EMBL:SRX92810.1, ECO:0000313|Proteomes:UP000252015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P7336 {ECO:0000313|EMBL:SRX92810.1,
RC   ECO:0000313|Proteomes:UP000252015};
RG   IHU Genomes;
RL   Submitted (MAY-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}.
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DR   EMBL; UEGW01000001; SRX92810.1; -; Genomic_DNA.
DR   RefSeq; WP_069394116.1; NZ_UEGW01000001.1.
DR   AlphaFoldDB; A0A1E3TLK8; -.
DR   STRING; 29313.BHQ16_00950; -.
DR   OMA; IEFHARI; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000252015; 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}.
FT   DOMAIN          194..457
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   457 AA;  50373 MW;  B91B46F46206C08B CRC64;
     MAVVDDLGQP GMDVPSEDFG RQPPQDVAAE QSVLGGMLLS KDAIADVLER LRPGDFYRPA
     HQNIYDAILD LYGRGEPADA VTVAAELDRR GLLRRIGGAP YLHTLISTVP TAANAGYYAG
     IVAEKALLRR LVEAGTRVVQ YGYAGAEGSD VAEVVDRAQA EIYDVTDRRL SEDFVALEDL
     LQPTMDEIDA IASTGGLARG VPTGFTELDE VTNGLHPGQM IVIAARPGMG KSTLGLDFMR
     SCSIKHRMSS VIFSLEMSKS EIVMRLLSAE AKIKLSDMRS GRMSDDDWTR LARRMSEISE
     APLYIDDSPN LTMMEIRAKT RRLSQKANLK LVVVDYLQLM SSGKRFESRQ QEVSEFSRSL
     KLLAKELEVP VIAISQLNRG PEQRTDKKPM LADLRESGAI EQDSDLVILL HRPDAFERDD
     PRGGEADLIL AKHRNGPTKT VTVAHQLHLS RFTNMAR
//
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