ADDB_STAAS
ID ADDB_STAAS Reviewed; 1158 AA.
AC Q6GAW0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000255|HAMAP-Rule:MF_01452};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01452};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01452};
DE AltName: Full=ATP-dependent helicase/nuclease AddB {ECO:0000255|HAMAP-Rule:MF_01452};
GN Name=addB {ECO:0000255|HAMAP-Rule:MF_01452}; OrderedLocusNames=SAS0836;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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 AddB nuclease domain is not
CC required for chi fragment generation; this subunit has 5' -> 3'
CC nuclease activity. {ECO:0000255|HAMAP-Rule:MF_01452}.
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_01452};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01452};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000255|HAMAP-
CC Rule:MF_01452}.
CC -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01452}.
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DR EMBL; BX571857; CAG42611.1; -; Genomic_DNA.
DR RefSeq; WP_000172347.1; NC_002953.3.
DR AlphaFoldDB; Q6GAW0; -.
DR SMR; Q6GAW0; -.
DR KEGG; sas:SAS0836; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008409; F:5'-3' 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-EC.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_01452; AddB_type1; 1.
DR InterPro; IPR014140; DNA_helicase_suAddB.
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 PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02773; addB_Gpos; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; DNA damage; DNA repair; Exonuclease; Hydrolase; Iron;
KW Iron-sulfur; Metal-binding; Nuclease; Nucleotide-binding.
FT CHAIN 1..1158
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379209"
FT DOMAIN 1..275
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 269..583
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 784
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1158 AA; 134699 MW; EE9A1E6A910009E5 CRC64;
MTLHAYLGRA GTGKSTKMLT EIKQKMKADP LGDPIILIAP TQSTFQLEQA FVNDPELNGS
LRTEVLHFER LSHRIFQEVG SYSEQKLSKA ATEMMIYNIV QEQQKYLKLY QSQAKYYGFS
EKLTEQIQDF KKYAVTPEHL EHFIADKNMQ TRTKNKLEDI ALIYREFEQR IQNEFITGED
SLQYFIDCMP KSEWLKRADI YIDGFHNFST IEYLIIKGLI KYAKSVTIIL TTDGNHDQFS
LFRKPSEVLR HIEEIANELN ISIERQYFNQ LYRFNNQDLK HLEQEFDVLQ INRVACQGHI
NILESATMRE EINEIARRII VDIRDKQLRY QDIAILYRDE SYAYLFDSIL PLYNIPYNID
TKRSMTHHPV MEMIRSLIEV IQSNWQVNPM LRLLKTDVLT ASYLKSAYLV DLLENFVLER
GIYGKRWLDD ELFNVEHFSK MGRKAHKLTE DERNTFEQVV KLKKDVIDKI LHFEKQMSQA
ETVKDFATAF YESMEYFELP NQLMTERDEL DLNGNHEKAE EIDQIWNGLI QILDDLVLVF
GDEPMSMERF LEVFDIGLEQ LEFVMIPQTL DQVSIGTMDL AKVDNKQHVF LVGMNDGTMP
QPVTASSLIT DEEKKYFEQQ ANVELSPTSD ILQMDEAFVC YIAMTRARQD VTFSYRLMGS
SGDDKEISPF LNQIQSLFNQ LEITNIPQYH EVNPLSLMQH AKQTKITLFE ALRAWLYDEI
VADSWLDAYQ VIRDSDHLNQ GLDYLMSALT FDNETVKLGE TLSKDLYGKE INASVSRFEG
YQQCPFKHYA SHGLKLNERT KYELQNFDLG DIFHSVLKYI SERINGDFKQ LDLKKIRQLT
NEALEEILPK VQFNLLNSSA YYRYLSRRIG AIVETTLSAL KYQGTYSKFM PKHFETSFRR
KPRTNDELIA QTLTTTQGIP INIRGQIDRI DTYTKNDTSF VNIIDYKSSE GSATLDLTKV
YYGMQMQMMT YMDIVLQNKQ RLGLTDIVKP GGLLYFHVHE PRIKFKSWSD IDEDKLEQDL
IKKFKLSGLV NADQTVIDAL DIRLEPKFTS DIVPVGLNKD GSLSKRGSQV ADEATIYKFI
QHNKENFIET ASNIMDGHTE VAPLKYKQKL PCAFCSYQSV CHVDGMIDSK RYRTVDETIN
PIEAIQNINI NDEFGGEQ
