ID   HELS_SACS9              Reviewed;         715 AA.
AC   D0KN27; A7WPA4;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=Ssol_0266;
OS   Saccharolobus solfataricus (strain 98/2) (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=555311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS),
RP   FUNCTION AS A HELICASE, SUBUNIT, DOMAIN, DNA-BINDING, AND MUTAGENESIS OF
RP   LYS-59; ARG-262; ARG-327; ARG-669 AND 653-LYS--HIS-715.
RC   STRAIN=98/2 / PBL 2025;
RX   PubMed=18056710; DOI=10.1074/jbc.m707548200;
RA   Richards J.D., Johnson K.A., Liu H., McRobbie A.M., McMahon S., Oke M.,
RA   Carter L., Naismith J.H., White M.F.;
RT   "Structure of the DNA repair helicase hel308 reveals DNA binding and
RT   autoinhibitory domains.";
RL   J. Biol. Chem. 283:5118-5126(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98/2;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Mead D.;
RT   "Complete sequence of Sulfolobus solfataricus 98/2.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be
CC       involved in repair of stalled replication forks. A low processivity 3'-
CC       5' helicase. Unwinds short dsDNA substrates with 3'-overhangs (25 bp
CC       dsDNA with 25 base overhang), less active on longer dsDNA substrates.
CC       Also unwinds the lagging strand of a stalled replication fork (but the
CC       leading strand was not tested). Binds ssDNA, but dsDNA about 35-fold
CC       less well. Able to displace streptavidin from biotinylated ssDNA, which
CC       is partially inhibited by DNA-binding proteins, suggesting it may play
CC       a role in stripping proteins from stalled replication forks.
CC       {ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:18056710}.
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. {ECO:0000255|HAMAP-Rule:MF_00442,
CC       ECO:0000269|PubMed:18056710}.
CC   -!- DOMAIN: Crystallizes with 5 domains; the first 4 form a ring through
CC       which ssDNA may pass (seen in A. fulgidus crystals). The C-terminal
CC       domain (654-715) lies perpendicular to the ring and is able to bind
CC       ssDNA, which may cause it to may act as a molecular brake, inhibiting
CC       helicase activity (PubMed:18056710). {ECO:0000269|PubMed:18056710}.
CC   -!- SIMILARITY: Belongs to the helicase family. Hel308 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00442}.
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DR   EMBL; AM778123; CAO85626.1; -; Genomic_DNA.
DR   EMBL; CP001800; ACX90562.1; -; Genomic_DNA.
DR   RefSeq; WP_009988512.1; NZ_ACUK01000013.1.
DR   PDB; 2VA8; X-ray; 2.30 A; A/B=1-715.
DR   PDBsum; 2VA8; -.
DR   AlphaFoldDB; D0KN27; -.
DR   SMR; D0KN27; -.
DR   EnsemblBacteria; ACX90562; ACX90562; Ssol_0266.
DR   GeneID; 44128181; -.
DR   KEGG; sol:Ssol_0266; -.
DR   HOGENOM; CLU_006553_3_0_2; -.
DR   OMA; MFLNANI; -.
DR   BRENDA; 3.6.4.12; 6163.
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; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR022965; Helicase_Hel308.
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   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase;
KW   Hydrolase; Nucleotide-binding.
FT   CHAIN           1..715
FT                   /note="ATP-dependent DNA helicase Hel308"
FT                   /id="PRO_0000429031"
FT   DOMAIN          40..203
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT   DOMAIN          236..442
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT   MOTIF           8..36
FT                   /note="Q motif"
FT   MOTIF           152..155
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT   BINDING         35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT   MUTAGEN         59
FT                   /note="K->A: No helicase activity. Wild-type binding to ss
FT                   and dsDNA."
FT                   /evidence="ECO:0000269|PubMed:18056710"
FT   MUTAGEN         262
FT                   /note="R->A: Significantly reduced helicase, 26-fold
FT                   decreased binding to ssDNA."
FT                   /evidence="ECO:0000269|PubMed:18056710"
FT   MUTAGEN         327
FT                   /note="R->A: Significantly reduced helicase, 6-fold
FT                   decreased binding to ssDNA, wild-type binding to dsDNA."
FT                   /evidence="ECO:0000269|PubMed:18056710"
FT   MUTAGEN         653..715
FT                   /note="Missing: Increased helicase on linear substrates and
FT                   stalled replication fork, nearly wild-type binding to ss
FT                   and dsDNA."
FT                   /evidence="ECO:0000269|PubMed:18056710"
FT   MUTAGEN         669
FT                   /note="R->A: Increased helicase, 3-fold decreased binding
FT                   to ssDNA."
FT                   /evidence="ECO:0000269|PubMed:18056710"
FT   CONFLICT        2
FT                   /note="S -> G (in Ref. 1; CAO85626)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   715 AA;  81507 MW;  D39EF80A29494AC0 CRC64;
     MSLELEWMPI EDLKLPSNVI EIIKKRGIKK LNPPQTEAVK KGLLEGNRLL LTSPTGSGKT
     LIAEMGIISF LLKNGGKAIY VTPLRALTNE KYLTFKDWEL IGFKVAMTSG DYDTDDAWLK
     NYDIIITTYE KLDSLWRHRP EWLNEVNYFV LDELHYLNDP ERGPVVESVT IRAKRRNLLA
     LSATISNYKQ IAKWLGAEPV ATNWRPVPLI EGVIYPERKK KEYNVIFKDN TTKKVHGDDA
     IIAYTLDSLS KNGQVLVFRN SRKMAESTAL KIANYMNFVS LDENALSEIL KQLDDIEEGG
     SDEKELLKSL ISKGVAYHHA GLSKALRDLI EEGFRQRKIK VIVATPTLAA GVNLPARTVI
     IGDIYRFNKK IAGYYDEIPI MEYKQMSGRA GRPGFDQIGE SIVVVRDKED VDRVFKKYVL
     SDVEPIESKL GSERAFYTFL LGILSAEGNL SEKQLENFAY ESLLAKQLVD VYFDRAIRWL
     LEHSFIKEEG NTFALTNFGK RVADLYINPF TADIIRKGLE GHKASCELAY LHLLAFTPDG
     PLVSVGRNEE EELIELLEDL DCELLIEEPY EEDEYSLYIN ALKVALIMKD WMDEVDEDTI
     LSKYNIGSGD LRNMVETMDW LTYSAYHLSR ELKLNEHADK LRILNLRVRD GIKEELLELV
     QISGVGRKRA RLLYNNGIKE LGDVVMNPDK VKNLLGQKLG EKVVQEAARL LNRFH