ADDA_STACT
ID ADDA_STACT Reviewed; 1220 AA.
AC B9DIS2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=Sca_0575;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
CC -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA helicase
CC and an ATP-dependent, dual-direction single-stranded exonuclease.
CC Recognizes the chi site generating a DNA molecule suitable for the
CC initiation of homologous recombination. The AddA nuclease domain is
CC required for chi fragment generation; this subunit has the helicase and
CC 3' -> 5' nuclease activities. {ECO:0000255|HAMAP-Rule:MF_01451}.
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_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000255|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01451}.
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DR EMBL; AM295250; CAL27489.1; -; Genomic_DNA.
DR RefSeq; WP_015899833.1; NC_012121.1.
DR AlphaFoldDB; B9DIS2; -.
DR SMR; B9DIS2; -.
DR STRING; 396513.SCA_0575; -.
DR PRIDE; B9DIS2; -.
DR GeneID; 60545725; -.
DR KEGG; sca:SCA_0575; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR BioCyc; SCAR396513:SCA_RS02940-MON; -.
DR Proteomes; UP000000444; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 4.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; DNA_helicase_suAddA.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR02785; addA_Gpos; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Nuclease; Nucleotide-binding.
FT CHAIN 1..1220
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379321"
FT DOMAIN 9..473
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 474..782
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1220 AA; 142644 MW; 5A90BEF9302672B1 CRC64;
MIPEKPNDVI WTDDQWKSIY AKGQDTLVAA AAGSGKTAVL VERIIQRILR DEIDVDRLLV
VTFTNLSARE MKHRVEKRIQ KASLEDPSNT HLKNQRVKIH QAQISTLHSF CLKLIQQHYD
VLDIDPNFRT SSEAENILLL EQTIDEVLEK YYAELNPAFI DLSEQLSSDR SDERLRQIIK
SVYYFAVANP QPEQWLKSLV SPYKDNQAQD EFLELLMNLA KVFMNTALEN LNKSFDLYSE
LAGCDKQLEV IEDERAFIAR AMEGGILNTE LISKHSFISR FPSATKKIKE ANDGNLELLE
SAKAYYDDYK GAVEKVQQDY FSRSAEDLKA DMAKLAPRVE VLSQITRDVI DTFSKKKRSR
NILDFSDYEH FALKILMNED GTPTDLAKHY RNGFDEILVD EYQDTNRVQE QILSCIKRGD
ETDGNLFMVG DVKQSIYKFR QADPSLFIEK YSRFSHDGTT GMRIDLSQNF RSRPEVLSTT
NYLFKHMMDE SVGEIIYDEA AQLYYGAPFD DKPHPLNLNV MVEDKESELT GTEQEAEYIA
NQVEEIMNHR EVYDMGTGSY RKPSYKDIVI LERGYNRSRE LQQAFKNRDI PFHVNSKEGY
FEQTEVRLVL SFLRTVDNPL QDIYLVGLMR SVIYQFTEDE LARIRVTSPN DDYFYQSIQH
YLKTKEADPD LVAKLQDFLK DLKFYQEFSL EHPVYQLIDR FYNNRLVIQY FSGMIGGKGR
RANLYGLYNK AIEFENSSFR GLFQFIRFID ELIDRGKDFG EENVVGPNDD VVRMMTIHAS
KGLEFPFVIY SGLSKSFNRS DLYKPVILNQ KYGMGMTYFD VEKDFAFPSL ASVTLRAITE
KEMISEEMRL MYVALTRAKE QLFLVGRVKA EKELDKMLNT AISNNMLPMS YRLEVKNPLQ
LIYAILAKYQ ANHLTNDLKF ERNIDELDDA IHPYAEIHID EYSDIAQDIH QNEDEEFRTV
NDIVNYQSTN TERQQAIETQ LDYQYPYQKD VVKPTKQSVS ELKRQLETEE TGTSYERVRQ
YQLGASTYER PKFMRQHKKR KANEIGTLMH TVMQHLPFKE ERMTSAELDE YIDGLIEKNI
IEDDAKPDIR MDEVMNFIKS DLYLEIAQSD QIMREMPFVV NQSKVDHQMN DDEDVSIIQG
MIDLIYRKDN QYYFVDYKTD TFNQRRGVSD EELGEQLKAR YKIQMYYYRS ALETILQKEV
KGYLYFFKFG TLSLEETEKH
