HERA_SULTO
ID HERA_SULTO Reviewed; 495 AA.
AC Q96YR7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=DNA double-strand break repair helicase HerA {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000269|PubMed:18243819};
DE AltName: Full=StoHerA {ECO:0000303|PubMed:18243819};
GN Name=herA {ECO:0000303|PubMed:18243819};
GN OrderedLocusNames=STK_21060 {ECO:0000312|EMBL:BAB67210.1};
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, INTERACTION
RP WITH MRE11, AND MUTAGENESIS OF LYS-153; ASP-175; GLU-355 AND ARG-380.
RX PubMed=18243819; DOI=10.1016/j.dnarep.2007.10.010;
RA Zhang S., Wei T., Hou G., Zhang C., Liang P., Ni J., Sheng D., Shen Y.;
RT "Archaeal DNA helicase HerA interacts with Mre11 homologue and unwinds
RT blunt-ended double-stranded DNA and recombination intermediates.";
RL DNA Repair 7:380-391(2008).
CC -!- FUNCTION: Involved in DNA double-strand break (DSB) repair
CC (PubMed:18243819). 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:18243819). Loads on either a
CC 3' or a 5' DNA tail for subsequent DNA unwinding (PubMed:18243819). Can
CC also unwind blunt-ended dsDNA, Holliday junction and splayed-arm DNA
CC (PubMed:18243819). {ECO:0000250|UniProtKB:Q8U1P0,
CC ECO:0000269|PubMed:18243819}.
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:18243819};
CC -!- ACTIVITY REGULATION: ATPase activity is slightly stimulated by either
CC circular single- or double-stranded DNA with a weak preference for
CC double-stranded DNA (PubMed:18243819). Helicase activity is stimulated
CC by Mre11 (PubMed:18243819). {ECO:0000269|PubMed:18243819}.
CC -!- SUBUNIT: Forms a hexamer or a heptamer (PubMed:18243819). Interacts
CC with Mre11 (PubMed:18243819). {ECO:0000269|PubMed:18243819}.
CC -!- SIMILARITY: Belongs to the HerA family. {ECO:0000305}.
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DR EMBL; BA000023; BAB67210.1; -; Genomic_DNA.
DR RefSeq; WP_010980185.1; NC_003106.2.
DR AlphaFoldDB; Q96YR7; -.
DR SMR; Q96YR7; -.
DR STRING; 273063.STK_21060; -.
DR EnsemblBacteria; BAB67210; BAB67210; STK_21060.
DR GeneID; 1460178; -.
DR KEGG; sto:STK_21060; -.
DR PATRIC; fig|273063.9.peg.2398; -.
DR eggNOG; arCOG00280; Archaea.
DR OMA; CLVSQRP; -.
DR OrthoDB; 33242at2157; -.
DR BRENDA; 3.6.4.12; 15396.
DR Proteomes; UP000001015; 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 ATP-binding; DNA damage; DNA repair; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..495
FT /note="DNA double-strand break repair helicase HerA"
FT /id="PRO_0000434026"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97WG8"
FT BINDING 150..155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97WG8"
FT BINDING 458..459
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97WG8"
FT MUTAGEN 153
FT /note="K->A: Lack of ATPase and helicase activities."
FT /evidence="ECO:0000269|PubMed:18243819"
FT MUTAGEN 175
FT /note="D->A: Strong decrease in ATPase and helicase
FT activities."
FT /evidence="ECO:0000269|PubMed:18243819"
FT MUTAGEN 355
FT /note="E->A: Lack of ATPase and helicase activities.
FT Decreases ssDNA-binding ability. Does not bind to blunt-
FT ended dsDNA and Holliday junction substrate."
FT /evidence="ECO:0000269|PubMed:18243819"
FT MUTAGEN 380
FT /note="R->A: Strong decrease in ATPase and helicase
FT activities."
FT /evidence="ECO:0000269|PubMed:18243819"
SQ SEQUENCE 495 AA; 55518 MW; 304D6577AB36B1D2 CRC64;
MIIGYVVGSA TTQEANVLLE KKVRSGYYVT LEYDDEKVLG LVTLITTGSP LVDDSLNDIE
LVQRIKQMGN KIPIYMKAKV KLLCKLDGKL SQPDLPPVAG TPVRLATNEE LSTIFSEGTI
RIGKLIGSDV EVRIRVNALT RHLAILAATG SGKSNTVAVL SSRLSEVFGS VLIFDYHGEY
YESEIKNLNN IEPKINPLNL TPDEFATLLE IRENATIQYR ILRRAFKSFL EETKEKLKNG
NVNYNELNNN FRNLILKKVD EVSKNEKRKD SKDEVINKIE DFLDRYSEII DFTAGDVVDK
IKIGKVNVIN LSSLDEDAID AIVSHYLRKI LTSRKENKMK RKIGLKFPVL VVIEEAHVLL
SKDSNTLTKH WAGRIAREGR KFGVGLIIVS QRPKGIDENI LSQMTNKIIL KMVEPSDKKY
VLETSDNLSE DIVEGLSALD TGEAVIVGNI VRMPAIVKID KFEGKLAGSD PNLIEEWKKA
KEEIEEHADV LNWGE
