HELS_METTH
ID HELS_METTH Reviewed; 690 AA.
AC O26901;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=ATP-dependent DNA helicase Hel308 {ECO:0000255|HAMAP-Rule:MF_00442};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00442};
GN Name=hel308 {ECO:0000255|HAMAP-Rule:MF_00442}; OrderedLocusNames=MTH_810;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP FUNCTION AS A HELICASE, FUNCTION AS AN ATPASE, SUBSTRATE, DNA-BINDING, AND
RP MUTAGENESIS OF LYS-51.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=15994460; DOI=10.1093/nar/gki685;
RA Guy C.P., Bolt E.L.;
RT "Archaeal Hel308 helicase targets replication forks in vivo and in vitro
RT and unwinds lagging strands.";
RL Nucleic Acids Res. 33:3678-3690(2005).
RN [3]
RP FUNCTION AS A HELICASE, FUNCTION AS AN ATPASE, DNA-BINDING, DOMAIN, AND
RP MUTAGENESIS OF ARG-647; ARG-649 AND ARG-651.
RX PubMed=17991488; DOI=10.1016/j.jmb.2007.10.004;
RA Woodman I.L., Briggs G.S., Bolt E.L.;
RT "Archaeal Hel308 domain V couples DNA binding to ATP hydrolysis and
RT positions DNA for unwinding over the helicase ratchet.";
RL J. Mol. Biol. 374:1139-1144(2007).
RN [4]
RP FUNCTION, AND REVIEW.
RX PubMed=19143605; DOI=10.1042/bst0370074;
RA Woodman I.L., Bolt E.L.;
RT "Molecular biology of Hel308 helicase in archaea.";
RL Biochem. Soc. Trans. 37:74-78(2009).
RN [5]
RP INTERACTION WITH RPA, SUBUNIT, DNA-BINDING, AND MUTAGENESIS OF LYS-51;
RP ARG-647; ARG-649 AND ARG-651.
RX PubMed=21195035; DOI=10.1016/j.dnarep.2010.12.001;
RA Woodman I.L., Brammer K., Bolt E.L.;
RT "Physical interaction between archaeal DNA repair helicase Hel308 and
RT replication protein A (RPA).";
RL DNA Repair 10:306-313(2011).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF LYS-51; PHE-434; PHE-439; 459-GLN--ASN-464 AND
RP TYR-460.
RX PubMed=28738244; DOI=10.1016/j.dnarep.2017.07.005;
RA Northall S.J., Buckley R., Jones N., Penedo J.C., Soultanas P., Bolt E.L.;
RT "DNA binding and unwinding by Hel308 helicase requires dual functions of a
RT winged helix domain.";
RL DNA Repair 57:125-132(2017).
CC -!- FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be
CC involved in repair of stalled replication forks. Helicase with 3'-to
CC 5'- polarity; able to unwind over 100 bp of DNA at 50 degrees Celsius.
CC Unwinds forked DNA, preferentially on lagging strand forks; has weaker
CC activity on Holliday junctions. Displaces the invading strand in DNA D-
CC loops. Unwinds short oligonucleotides from dsDNA with 3'- but not blunt
CC ends or 5'-ssDNA tails in an ATP-dependent manner. ATPase activity is
CC stimulated by ssDNA but not dsDNA, protein binds ssDNA, dsDNA with
CC 5'- or 3'-overhangs but not blunt ended dsDNA and replication forks.
CC Replication forks bind both this protein and RPA. RPA does not
CC stimulate the helicase activity of this protein. {ECO:0000255|HAMAP-
CC Rule:MF_00442, ECO:0000269|PubMed:15994460,
CC ECO:0000269|PubMed:17991488, ECO:0000269|PubMed:19143605,
CC ECO:0000269|PubMed:28738244}.
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:0000255|HAMAP-Rule:MF_00442};
CC -!- SUBUNIT: Monomer (By similarity). Binds replication protein A (RPA), in
CC presence and absence of DNA. {ECO:0000255|HAMAP-Rule:MF_00442,
CC ECO:0000269|PubMed:21195035}.
CC -!- DOMAIN: The C-terminal region (about 633-690) acts as a brake for ATP
CC hydrolysis (PubMed:17991488) and interacts with RPA (PubMed:21195035).
CC {ECO:0000269|PubMed:17991488, ECO:0000269|PubMed:21195035}.
CC -!- SIMILARITY: Belongs to the helicase family. Hel308 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00442}.
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DR EMBL; AE000666; AAB85310.1; -; Genomic_DNA.
DR PIR; C69208; C69208.
DR RefSeq; WP_010876445.1; NC_000916.1.
DR AlphaFoldDB; O26901; -.
DR SMR; O26901; -.
DR STRING; 187420.MTH_810; -.
DR EnsemblBacteria; AAB85310; AAB85310; MTH_810.
DR GeneID; 1471218; -.
DR KEGG; mth:MTH_810; -.
DR PATRIC; fig|187420.15.peg.795; -.
DR HOGENOM; CLU_006553_3_0_2; -.
DR OMA; DMHDTYL; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00442; Helicase_Hel308; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR041663; DisA/LigA_HHH.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR022965; Helicase_Hel308.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12826; HHH_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00278; HhH1; 2.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..690
FT /note="ATP-dependent DNA helicase Hel308"
FT /id="PRO_0000102108"
FT DOMAIN 32..188
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT DOMAIN 208..417
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT MOTIF 133..136
FT /note="DEAH box"
FT BINDING 26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT MUTAGEN 51
FT /note="K->L: No helicase activity, 6% ATPase activity.
FT Binds fork DNA as well as wild-type; also supershifts with
FT RFA."
FT /evidence="ECO:0000269|PubMed:15994460,
FT ECO:0000269|PubMed:21195035, ECO:0000269|PubMed:28738244"
FT MUTAGEN 434
FT /note="F->A: Strongly reduced ATPase and helicase
FT activity."
FT /evidence="ECO:0000269|PubMed:28738244"
FT MUTAGEN 439
FT /note="F->V: Reduced ATPase and helicase activity."
FT /evidence="ECO:0000269|PubMed:28738244"
FT MUTAGEN 459..464
FT /note="QYEVEN->GAEVEG: Reduced duplex DNA-binding and
FT unwinding activity, without affecting single-stranded DNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:28738244"
FT MUTAGEN 460
FT /note="Y->A: Reduced duplex DNA-binding and unwinding
FT activity, without affecting single-stranded DNA-binding."
FT /evidence="ECO:0000269|PubMed:28738244"
FT MUTAGEN 647
FT /note="R->A: No change in DNA-binding to replication forks.
FT Basal ATPase 4-5 fold higher than wild-type, ssDNA
FT stimulation is less effective than wild-type. Almost no
FT helicase activity. Binds RPA."
FT /evidence="ECO:0000269|PubMed:17991488,
FT ECO:0000269|PubMed:21195035"
FT MUTAGEN 649
FT /note="R->A: Decreased DNA-binding to replication forks,
FT decreased ssDNA-stimulated ATPase. Decreased helicase
FT activity. No binding to RPA."
FT /evidence="ECO:0000269|PubMed:17991488,
FT ECO:0000269|PubMed:21195035"
FT MUTAGEN 651
FT /note="R->A: No change in DNA-binding to replication forks.
FT Decreased ssDNA stimulation of ATPase. Almost no helicase
FT activity. Binds RPA."
FT /evidence="ECO:0000269|PubMed:17991488,
FT ECO:0000269|PubMed:21195035"
SQ SEQUENCE 690 AA; 78510 MW; 90BEE6110C4133F3 CRC64;
MKSLPPEMRQ ILGDCYPHIR ELNPAQRSAI EAGYLESEDN YIIAIPTASG KTLLGIIAAL
KTVMEGGRVI YTVPLLSIQN EKIKEFRKLE EHGIRVGKDP RTSDIAVMVF ESFDSLTRFS
WNILREVDLL IVDEFHMIGE YTRGPVIESA ITRARTLNPS VRIVALSATL SNMDEIAGWL
DARVVEHDYR PVPLHREVLD TEMFGVREKN DVVLKVLERS LEDGSQTLAF VSTRRFTESL
ASHLADKISG KIPDDMVESF REVAGKVLEV PKSRGSPPTS TCLKLAECLE AGIAFHHAGL
FNRQREIIED EFRDGNILMI TATPSLMYGV NLPSRTVVIR DYTRWTSQGP RRIPVFDYEQ
MSGRAGRPQY DDAGYSYLIA RSHDEAMDLE EYYIRGEVER TTSRIIENRD ALYRQIIAQV
ASGLSGTTEE LADFFRNTFY GYQMVEGPFS DSFGMDSIQY EVENATEYLM RNRILYPGPE
GFSATEFGLL IAKSNYSVET AIKLHQFASE MDEMDIYRLI YEITRTPDMP LISFKGRKSR
DPVRDKLMEH GLFLMDVGNE EATAAALIEW INERTEYEIE NAFHVYAAST RRSAYEASKI
VKFFGKICEI MGVYRHSSQL EILSARLYYG VKEDAIPLVV GVRGLGRVRA RKIIKTFGED
LRHVREDELK RIDGIGPKMA GAIRRYCERF
