HERA_SULAC
ID HERA_SULAC Reviewed; 495 AA.
AC F2Z5Z6; Q4JCJ6; Q7LYV9;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=DNA double-strand break repair helicase HerA {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000269|PubMed:14990749};
DE AltName: Full=Helicase repair of Archaea {ECO:0000303|PubMed:14990749};
GN Name=herA {ECO:0000303|PubMed:14990749};
GN Synonyms=P4 {ECO:0000312|EMBL:CAE51870.1};
GN OrderedLocusNames=Saci_0053 {ECO:0000312|EMBL:AAY79483.1};
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=12052775; DOI=10.1093/embo-reports/kvf112;
RA Constantinesco F., Forterre P., Elie C.;
RT "NurA, a novel 5'-3' nuclease gene linked to rad50 and mre11 homologs of
RT thermophilic Archaea.";
RL EMBO Rep. 3:537-542(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [3]
RP FUNCTION AS AN ATPASE AND AS AN HELICASE, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND MUTAGENESIS OF LYS-154.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=14990749; DOI=10.1093/nar/gkh283;
RA Constantinesco F., Forterre P., Koonin E.V., Aravind L., Elie C.;
RT "A bipolar DNA helicase gene, herA, clusters with rad50, mre11 and nurA
RT genes in thermophilic archaea.";
RL Nucleic Acids Res. 32:1439-1447(2004).
RN [4]
RP INTERACTION WITH RAD50 AND MRE11.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=18294364; DOI=10.1186/1471-2199-9-25;
RA Quaiser A., Constantinesco F., White M.F., Forterre P., Elie C.;
RT "The Mre11 protein interacts with both Rad50 and the HerA bipolar helicase
RT and is recruited to DNA following gamma irradiation in the archaeon
RT Sulfolobus acidocaldarius.";
RL BMC Mol. Biol. 9:25-25(2008).
CC -!- FUNCTION: Involved in DNA double-strand break (DSB) repair
CC (PubMed:14990749). 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:14990749). Loads on either a
CC 3' or a 5' DNA tail for subsequent DNA unwinding (PubMed:14990749).
CC {ECO:0000250|UniProtKB:Q8U1P0, ECO:0000269|PubMed:14990749}.
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:14990749};
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. {ECO:0000269|PubMed:14990749}.
CC -!- SUBUNIT: Interacts with Rad50 and Mre11. {ECO:0000269|PubMed:18294364}.
CC -!- SIMILARITY: Belongs to the HerA family. {ECO:0000305}.
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DR EMBL; AJ437617; CAE51870.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY79483.1; -; Genomic_DNA.
DR RefSeq; WP_011276984.1; NC_007181.1.
DR AlphaFoldDB; F2Z5Z6; -.
DR SMR; F2Z5Z6; -.
DR STRING; 330779.Saci_0053; -.
DR EnsemblBacteria; AAY79483; AAY79483; Saci_0053.
DR GeneID; 3472968; -.
DR KEGG; sai:Saci_0053; -.
DR PATRIC; fig|330779.12.peg.50; -.
DR eggNOG; arCOG00280; Archaea.
DR HOGENOM; CLU_023842_2_0_2; -.
DR OMA; CLVSQRP; -.
DR Proteomes; UP000001018; 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_0000434024"
FT BINDING 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97WG8"
FT BINDING 151..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97WG8"
FT BINDING 459..460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97WG8"
FT MUTAGEN 154
FT /note="K->A: Abolishes both the ATPase and the helicase
FT activities."
FT /evidence="ECO:0000269|PubMed:14990749"
SQ SEQUENCE 495 AA; 55449 MW; A01C73FADE27120F CRC64;
MTIGYIIGSA TINEATAILE QKIRAGYYVI LEYDGDKILG LITNVYTGSP LLDDNLNDVK
FVQRIKQLEA NKIPFFIKAR IKLLCKLDGK FTQPDLPPVA GTPVRLASDE ELSTVFSAGD
VRIGKLIGSN VEVKIRLNPL SRHLAILAAT GSGKSNTVAI LSQRLVEIGG SILIFDYHGE
YYDSTLPNLN IIEPKLNPLY LSVNEFATLL EIRENANIQY RIIRRTFNQL KEEINNEIKE
GKTSLAELNS NFFERLKVKI EEEGRNEKRK ESKDEVLNKV EDFAERYSDI IDITFGDVIN
KIKLGKINVV NLSSLDEDAI DAIVAHYLRR ILTSRKENKI KKDSGLKFPI LTVVEEAHVL
LSKDTNTLTK KWAGRIAREG RKFGVGLIIV SQRPKGLDEN ILSQMTNKII LKIVEPSDKK
YVLETSDNLS EDLADGLSSL DTGEAIIIGN VVKLPTIIKI DKFEGKLSGS DPNLTEEWKR
AKEEEIVHSD VSDWG
