ADDB_STAA1
ID ADDB_STAA1 Reviewed; 1157 AA.
AC A7X0I1;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=SAHV_0961;
OS Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=418127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu3 / ATCC 700698;
RX PubMed=17954695; DOI=10.1128/aac.00534-07;
RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT "Mutated response regulator graR is responsible for phenotypic conversion
RT of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT resistance to vancomycin-intermediate resistance.";
RL Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF77844.1; -; Genomic_DNA.
DR RefSeq; WP_000172350.1; NC_009782.1.
DR AlphaFoldDB; A7X0I1; -.
DR SMR; A7X0I1; -.
DR KEGG; saw:SAHV_0961; -.
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..1157
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379210"
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 1157 AA; 134357 MW; EC09A392895A82C7 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 AKVDNKQHVY LVGMNDGTMP
QPVTASSLIT DEEKKYFEQQ ANVELSPTSD ILQMDEAFVC YVAMTRAKGD VTFSYSLMGS
SGDDKEISPF LNQIQSLFNQ LEITNIPQYH EVNPLSLMQH AKQTKITLFE ALRAWLDDEI
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 NDEFGGE
