ADDA_STAAB
ID ADDA_STAAB Reviewed; 1217 AA.
AC Q2YWW4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=SAB0836;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI80524.1; -; Genomic_DNA.
DR RefSeq; WP_000154917.1; NC_007622.1.
DR AlphaFoldDB; Q2YWW4; -.
DR SMR; Q2YWW4; -.
DR KEGG; sab:SAB0836; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
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..1217
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379307"
FT DOMAIN 10..475
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 491..786
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1217 AA; 141321 MW; 42F524A5FA4CD66F CRC64;
MTIPEKPQGV IWTDAQWQSI YATGQDVLVA AAAGSGKTAV LVERIIQKIL RDGIDVDRLL
VVTFTNLSAR EMKHRVDQRI QEASIADPAN AHLKNQRIKI HQAQISTLHS FCLKLIQQHY
DVLNIDPNFR TSSEAENILL LEQTIDEVIE QHYDILDPAF IELTEQLSSD RSDDQFRMII
KQLYFFSVAN PNPTNWLDQL VTPYEEEAQQ AQLIQILTDL SKVFITAAYD ALNKAYDLFS
MMDGVDKHLA VIEDERRLMG RVLEGGFIDI PYLTGHEFGA RLPNITAKIK EANEMMVDAL
KDAKLQYKKY KSLIDKVKSD YFSREADDLK ADMQQLAPRV KYLARIVKDV MSEFNRKKRS
KNILDFSDYE HFALQILTNE DGSPSEIAES YRQHFQEILV DEYQDTNRVQ EKILSCIKTG
DEHNGNLFMV GDVKQSIYKF RQADPSLFIE KYQRFTIDGD GTGRRMDLSQ NFRSRKEVLS
TTNYIFKHMM DEQVGEVNYD ESAQLYYGAP YDESDHPVNL KVLIEADQEH SDLTGSEQEA
HFIVEQVKDI LEHQKVYDMK TRSYRSATYK DIVILERSFG QARNLQQAFK NEDIPFHVNS
REGYFEQTEV RLALSFLRAI DNPLQDIYLV GLMRSVIYQF KEDELAQIRI LSPNDDYFYQ
SIVNYINDEA ADAILVDKLK MFLSDIQSYQ QYSKDHPVYQ LIDKFYNDHY VIQYFSGLIG
GRGRRANLYG LFNKAIEFEN SSFRGLYQFI RFIDELIERG KDFGEENVVG PNDNVVRMMT
IHSSKGLEFP FVIYSGLSKD FNKRDLKQPV ILNQQFGLGM DYFDVDKEMA FPSLASVAYR
AVAEKELVSE EMRLVYVALT RAKEQLYLIG RVKNDKSLLE LEQLSISGEH IAVNERLTSP
NPFHLIYSIL SKHQSASIPD DLKFEKDIAQ VEDSSRPNVN ISIIYFEDVS TETILDNDEY
RSVNQLETMQ NGNEDVKAQI KHQLDYQYPY VNDTKKPSKQ SVSELKRQYE TEESGTSYER
VRQYRIGFST YERPKFLSEQ GKRKANEIGT LMHTVMQHLP FKKERISEVE LHQYIDGLID
KHIIEADAKK DIRMDEIMTF INSELYSIIA EAEQVYRELP FVVNQALVDQ LPQGDEDVSI
IQGMIDLIFV KDGVHYFVDY KTDAFNRRRG MTDEEIGTQL KNKYKIQMKY YQNTLQTILN
KEVKGYLYFF KFGTLQL
