ADDA_STAES
ID ADDA_STAES Reviewed; 1224 AA.
AC Q8CPT9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=SE_0664;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04261.1; -; Genomic_DNA.
DR RefSeq; NP_764219.1; NC_004461.1.
DR RefSeq; WP_011082636.1; NZ_WBME01000043.1.
DR AlphaFoldDB; Q8CPT9; -.
DR SMR; Q8CPT9; -.
DR STRING; 176280.SE_0664; -.
DR EnsemblBacteria; AAO04261; AAO04261; SE_0664.
DR KEGG; sep:SE_0664; -.
DR PATRIC; fig|176280.10.peg.637; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000001411; 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..1224
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379322"
FT DOMAIN 15..480
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 497..791
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1224 AA; 143016 MW; 4B204F41A1ADF6A1 CRC64;
MKVVKDMIPT KPHDVIWTDA QWQSIYAKGQ DILVAAAAGS GKTAVLVERI IQRILRDDVD
VDRLLVVTFT NLSAREMKHR VDKRIQEASF KDPNNEHLKN QRIKIHQAQI STLHSFCLKL
IQQHYDVLDI DPHFRTSSEA ENILLLEQTI DDVLEQHYDK LDPHFIELTE QLSSDRNDDQ
FRSIIKQLYF FSIANPQPFE WLNQLAQPYK EENKQQQLMQ LINDLAMIFM KAGYEELQKS
YDLFSMMESV DKQLEVIETE RMFITKAIEG KVLNTDVITQ HEFMSRFPAI NSKIKEANEG
MEDALNEAKQ HYDKYKSLVM KVKNDYFSRN AEDLQRDMQQ LAPRVAYLAQ IVQDVIQSFG
VQKRSRNILD FSDYEHFALC ILTNEDGSPS RIAETYREHF KEILVDEYQD TNRVQEKILS
CIKTGEEHDG NLFMVGDVKQ SIYKFRQADP SLFIEKYNRF SSSGNESGLR IDLSQNFRSR
QEVLSTTNYL FKHMMDEQVG EISYDDAAQL YFGAPYDEVS HPVQLRALVE ASSENSDLTG
SEQEANYIVE QVKDIINHQN VYDMKTGQYR KATYKDIVIL ERSFGQARNL QQAFKNNDIP
FHVNSKEGYF EQTEVRLVLS FLRTIDNPLQ DIYLVGLMRS VIYQFTEEEL AEIRVVSPHD
DYFYQSIKNY MIDEKADSRL VDKLNRFIQD IQKYQNYSQS QPVYQLIDKF YNDHFVIQYF
SGLIGGKGRR ANLYGLFNKA VEFENSSFRG LFQFIRFIDE LIDRKKDFGE ENVVGPNDNV
VRMMTIHSSK GLEFPFVIYS GLSKKFNKGD LNAPVILNQQ YGLGMDYFDV NKDMAFPSLA
SVAYRAINEK ELISEEMRLI YVALTRAKEQ LILVGRVKDE KSLIKYEQLA VSDTHIAVNE
RLTATNPFVL IYGVLAKHQS PSLPNDQRFE RDIDQLNSEV KPRVSIVIDH YEDVSTEEVV
NDNEIRTIEE LKAINTGNED VKIKIHQQLS YDYPFKVNTM KPSKQSVSEL KRQLETEESN
TNYDRVRQYR IGVASYERPK FLTQTKKRKA NEIGTLMHTV MQHLPFREQR LTKDELFQYI
DRLIDKQLID EDAKEDIRID EIMHFIDGPL YMEIAQADNV YTELPFVVNQ IKVDGLTSED
EDVSIIQGMI DLIYESDGQF YFVDYKTDAF NRRKGMSDEE IGNQLKEKYQ IQMTYYRNTL
ETILKRPVKG YLYFFKFGTL EIDD
