HERA_SACS2
ID HERA_SACS2 Reviewed; 500 AA.
AC Q97WG8;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=DNA double-strand break repair helicase HerA {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000269|PubMed:22135300, ECO:0000269|PubMed:25420454};
GN Name=herA {ECO:0000303|PubMed:22135300};
GN OrderedLocusNames=SSO2251 {ECO:0000312|EMBL:AAK42419.1};
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, INTERACTION
RP WITH NURA, AND MUTAGENESIS OF LYS-154.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=22135300; DOI=10.1093/nar/gkr1157;
RA Blackwood J.K., Rzechorzek N.J., Abrams A.S., Maman J.D., Pellegrini L.,
RA Robinson N.P.;
RT "Structural and functional insights into DNA-end processing by the archaeal
RT HerA helicase-NurA nuclease complex.";
RL Nucleic Acids Res. 40:3183-3196(2012).
RN [3]
RP SUBUNIT, AND INTERACTION WITH NURA.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=25447518; DOI=10.1016/j.febslet.2014.10.035;
RA Byrne R.T., Schuller J.M., Unverdorben P., Foerster F., Hopfner K.P.;
RT "Molecular architecture of the HerA-NurA DNA double-strand break resection
RT complex.";
RL FEBS Lett. 588:4637-4644(2014).
RN [4] {ECO:0007744|PDB:4D2I}
RP X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) IN COMPLEX WITH ATP ANALOG,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ARG-142;
RP LYS-154; ARG-381 AND ASP-471.
RX PubMed=25420454; DOI=10.1038/ncomms6506;
RA Rzechorzek N.J., Blackwood J.K., Bray S.M., Maman J.D., Pellegrini L.,
RA Robinson N.P.;
RT "Structure of the hexameric HerA ATPase reveals a mechanism of
RT translocation-coupled DNA-end processing in archaea.";
RL Nat. Commun. 5:5506-5506(2014).
CC -!- FUNCTION: Involved in DNA double-strand break (DSB) repair
CC (PubMed:22135300). Acts probably with NurA to stimulate resection of
CC the 5' strand and produce the long 3' single-strand that is required
CC for RadA loading (By similarity). Exhibits DNA-dependent ATPase
CC activity and DNA helicase activity (PubMed:22135300, PubMed:25420454).
CC {ECO:0000250|UniProtKB:Q8U1P0, ECO:0000269|PubMed:22135300,
CC ECO:0000269|PubMed:25420454}.
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:0000269|PubMed:22135300, ECO:0000269|PubMed:25420454};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated in the presence of
CC linear dsDNA (PubMed:22135300). Helicase activity requires the presence
CC of NurA (PubMed:22135300). {ECO:0000269|PubMed:22135300}.
CC -!- SUBUNIT: Homohexamer (PubMed:22135300, PubMed:25447518,
CC PubMed:25420454). Forms a complex with NurA (PubMed:22135300,
CC PubMed:25447518). {ECO:0000269|PubMed:22135300,
CC ECO:0000269|PubMed:25420454, ECO:0000269|PubMed:25447518}.
CC -!- INTERACTION:
CC Q97WG8; Q97WH1: nurA; NbExp=3; IntAct=EBI-10110451, EBI-10110462;
CC -!- DOMAIN: Contains an N-terminal HAS-barrel domain, which mediates
CC interaction with NurA, followed by a central RecA-like catalytic core
CC and a C-terminal four-helix bundle. {ECO:0000269|PubMed:25420454}.
CC -!- SIMILARITY: Belongs to the HerA family. {ECO:0000305}.
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DR EMBL; AE006641; AAK42419.1; -; Genomic_DNA.
DR PIR; D90395; D90395.
DR RefSeq; WP_009991539.1; NC_002754.1.
DR PDB; 4D2I; X-ray; 2.84 A; A/B=1-500.
DR PDBsum; 4D2I; -.
DR AlphaFoldDB; Q97WG8; -.
DR SMR; Q97WG8; -.
DR IntAct; Q97WG8; 1.
DR MINT; Q97WG8; -.
DR STRING; 273057.SSO2251; -.
DR EnsemblBacteria; AAK42419; AAK42419; SSO2251.
DR GeneID; 44127985; -.
DR KEGG; sso:SSO2251; -.
DR PATRIC; fig|273057.12.peg.2346; -.
DR eggNOG; arCOG00280; Archaea.
DR HOGENOM; CLU_023842_2_0_2; -.
DR InParanoid; Q97WG8; -.
DR OMA; CLVSQRP; -.
DR PhylomeDB; Q97WG8; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR008571; HerA-like.
DR InterPro; IPR018538; HerA_barrel_dom.
DR InterPro; IPR033186; HerA_C.
DR InterPro; IPR002789; HerA_central.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR42957; PTHR42957; 1.
DR Pfam; PF05872; DUF853; 1.
DR Pfam; PF01935; DUF87; 1.
DR Pfam; PF09378; HAS-barrel; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA repair; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..500
FT /note="DNA double-strand break repair helicase HerA"
FT /id="PRO_0000434025"
FT BINDING 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25420454,
FT ECO:0007744|PDB:4D2I"
FT BINDING 151..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25420454,
FT ECO:0007744|PDB:4D2I"
FT BINDING 459..460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:25420454,
FT ECO:0007744|PDB:4D2I"
FT MUTAGEN 142
FT /note="R->A: Stimulates activity of the HerA-NurA complex."
FT /evidence="ECO:0000269|PubMed:25420454"
FT MUTAGEN 154
FT /note="K->A: Lack of ATPase and helicase activities."
FT /evidence="ECO:0000269|PubMed:22135300,
FT ECO:0000269|PubMed:25420454"
FT MUTAGEN 381
FT /note="R->A: Severely impairs ATPase activity. Lack of
FT helicase activity."
FT /evidence="ECO:0000269|PubMed:25420454"
FT MUTAGEN 471
FT /note="D->A: Impairs DNA translocation and destruction.
FT Increases ATPase activity."
FT /evidence="ECO:0000269|PubMed:25420454"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 12..21
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 36..48
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:4D2I"
FT TURN 86..90
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:4D2I"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 154..167
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:4D2I"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 217..240
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:4D2I"
FT TURN 287..290
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 317..341
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 368..379
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 385..392
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 416..423
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 431..434
FT /evidence="ECO:0007829|PDB:4D2I"
FT HELIX 435..439
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:4D2I"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:4D2I"
SQ SEQUENCE 500 AA; 56329 MW; 6CCFAA3F2DB23879 CRC64;
MIIGYVIGQA TTQEALILAE RPVRLGTYVV LEYDNVKALG LITNVTRGSP MLDDNMNDIE
IVQRLKQFNN SIPVYTKAKV KMLCDMNNHF LMPDIPPFAG TPAREAEDEE LKSIYSQDGQ
IRIGSLIGKN VEVKLNINSF ARHLAILAAT GSGKSNTVAV LSQRISELGG SVLIFDYHGE
YYDSDIKNLN RIEPKLNPLY MTPREFSTLL EIRENAIIQY RILRRAFIKV TNGIREKLKE
GQIPFSTLNS QFYELMKDEL ETQGNSDKKS SAKDEVLNKF EEFMDRYSNV IDLTSSDIIE
KVKRGKVNVV SLTQLDEDSM DAVVSHYLRR ILDSRKDFKR SKNSGLKFPI IAVIEEAHVF
LSKNENTLTK YWASRIAREG RKFGVGLTIV SQRPKGLDEN ILSQMTNKII LKIIEPTDKK
YILESSDNLS EDLAEQLSSL DVGEAIIIGK IVKLPAVVKI DMFEGKLLGS DPDMIGEWKK
VEESEKIAKG FADFGTEIGD
