DNAB_MYCLE
ID DNAB_MYCLE Reviewed; 604 AA.
AC P46394; O53124;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Replicative DNA helicase;
DE EC=3.6.4.12;
DE Contains:
DE RecName: Full=Mle dnaB intein;
GN Name=dnaB; OrderedLocusNames=ML2680; ORFNames=MLCB1913.16c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-257.
RX PubMed=8969512; DOI=10.1099/13500872-142-11-3147;
RA Fsihi H., de Rossi E., Salazar L., Cantoni R., Labo M., Riccardi G.,
RA Takiff H.E., Eiglmeier K., Bergh S., Cole S.T.;
RT "Gene arrangement and organization in an approximately 76 kb fragment
RT encompassing the oriC region of the chromosome of Mycobacterium leprae.";
RL Microbiology 142:3147-3161(1996).
CC -!- FUNCTION: Participates in initiation and elongation during chromosome
CC replication; it exhibits DNA-dependent ATPase activity. {ECO:0000250}.
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 -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the intervening region (intein) followed
CC by peptide ligation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000305}.
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DR EMBL; AL022118; CAA17948.1; -; Genomic_DNA.
DR EMBL; AL022118; CAA17949.1; -; Genomic_DNA.
DR EMBL; AL583926; CAC32212.1; -; Genomic_DNA.
DR EMBL; L39923; AAB53118.1; -; Genomic_DNA.
DR PIR; F87244; F87244.
DR RefSeq; NP_302709.1; NC_002677.1.
DR RefSeq; WP_010909028.1; NC_002677.1.
DR AlphaFoldDB; P46394; -.
DR SMR; P46394; -.
DR STRING; 272631.ML2680; -.
DR EnsemblBacteria; CAC32212; CAC32212; CAC32212.
DR KEGG; mle:ML2680; -.
DR PATRIC; fig|272631.5.peg.5172; -.
DR Leproma; ML2680; -.
DR eggNOG; COG0305; Bacteria.
DR HOGENOM; CLU_005373_4_0_11; -.
DR OMA; VMTGRPC; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR CDD; cd00984; DnaB_C; 1.
DR Gene3D; 1.10.860.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00772; DnaB; 1.
DR Pfam; PF03796; DnaB_C; 2.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF48024; SSF48024; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00665; DnaB; 1.
DR PROSITE; PS51199; SF4_HELICASE; 2.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Primosome; Reference proteome; Repeat.
FT CHAIN 1..233
FT /note="Replicative DNA helicase, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000013279"
FT CHAIN 234..378
FT /note="Mle dnaB intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000013280"
FT CHAIN 379..604
FT /note="Replicative DNA helicase, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000013281"
FT DOMAIN 196..462
FT /note="SF4 helicase; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT DOMAIN 341..604
FT /note="SF4 helicase; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 227..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT CONFLICT 252..257
FT /note="DVAVGD -> ELRPRS (in Ref. 2; AAB53118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 604 AA; 65876 MW; D140BE34CE90C43D CRC64;
MAVVDDLAHS GMDAVPPSED FGRQPPQDLA AEQSVLGGML LSKDAIADVL ERLRSGDFYR
PAHQNVYDAI LDLYGRGEPA DAVTVAAELD RRGLLRRIGG APYLHTLIST VPTAANAGYY
AGIVAEKALL RRLVEAGTRV VQYGYAGAEG ADVAEVVDRA QAEIYDVAEC RLSENYVPLE
DLLQPTMDDL DAIASNGGIS RGAPTGFTEL DEVTNGLHPG QMIIVAARPG VGKALALDTP
LPTPTGWTAM GDVAVGDELL AVDEAPTRVV AATEVMLGRP CYEIEFSDGT VIVADAQHQW
PTSYGIRTSA QLRCGLDIIA AAGSTPRHAG RLTTAAFMAP VLCIDSVRRV RSVPVRCVEV
DNAAHLYLAG RGMVPTHNST LGLDFMRSCS IKHRLASVIF SLEMSKSEIV MRLLSAEAKI
KLADMRSGRM TDDDWTRLAR RMSEISEAPL YIDDSPNLTM MEIRAKARRL RQKTNLKLVV
VDYLQLMTSG KRFESRQVEV SEFSRHLKLL AKELELPVVA ISQLNRSPEQ RTDKKPMLSD
LRESGSLEQD ADVVILLHRP DAFDRDDPRG GEADLILAKH RNGPTKTVTV AHQLHLSRFT
NMAR
