ADDB_STAHJ
ID ADDB_STAHJ Reviewed; 1162 AA.
AC Q4L4Y2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=SH1984;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05293.1; -; Genomic_DNA.
DR RefSeq; WP_011276251.1; NC_007168.1.
DR AlphaFoldDB; Q4L4Y2; -.
DR SMR; Q4L4Y2; -.
DR STRING; 279808.SH1984; -.
DR EnsemblBacteria; BAE05293; BAE05293; SH1984.
DR KEGG; sha:SH1984; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000000543; Chromosome.
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; -; 3.
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..1162
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379221"
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 1117
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1120
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1162 AA; 134679 MW; 068CDA697D333C36 CRC64;
MELNAYIGRA GTGKSHHMID NIKQQMKEDP LGDPIVLIAP TQSTFQLEQA FVNDKELNGS
LRTEVLHFER LSYRVFQEVG GLTEERLTQA ATEMMIYDLV QQHKSELKLY QSQVNYYGFS
EKLSEQIQDF KKYSVTPEHL HTFLQDNDLK TRTRHKLEDI SLIYQYFEER INGEFITSED
SLNHFIDILS QSEWIKRAEV YIDGFHNFST LEYQIIKALV QSAKKVTVLL TTDGNEDPFS
LFRKPSEVLT HLKEIAKDLN IELQQQFFKQ QYRFNNKDLI QLEQQFDALQ INPIAYDGSI
NILESSSIRE EVNEVARQII KDTRDKQYRY QDIAILYRDE AYAYLFDSVL PQYDIPFNID
TKRSMTHHPI MEMVRSLLEV IQTNWNISPM MRLIKTNILT NHFKDSAYLI DLLENFVVER
GVYGKRWLDE KLFSIDNFTK MGRKEHKLTT EEREDFEQVV HLKNDIIDKI LTFEKAMNEA
ENVRGFATAF YETMEAFDLP KYLMTHRDQL DVDGRHEEAE EIDQIWNGLI QILDDLVTVF
DNEEMTLKRF LEVFDIGLEQ LEFVMIPQTL DQVSIGTMDL AKVDNKKHIY MVGMNDGAMP
QPVSSSSLIT DEEKKVFEQQ AQVELSPTSD ILQMDEAFVC YIAMTRGSEQ VTFSYSLMGA
QGEDKEKSPF IDQIQGLFNG LEVMNIHYQH NAQPLSLMEH PHQTKVVLFE SLKAWLEAEM
VADVWVDAYQ VMRDNDKLNN GLEYLLTALT YDNETVKLDE PLAASLYGST INASVSRFEG
YNDCPFKHYA NHGLRLNERT KYKLENFDLG NIFHTALKYI SDKVDGDFKN LDNKKIHALT
VEALENVLPQ VQFNLMDSNA YYRYVSKRIG VIVESTLKAL RYQNKNTKFK PQRFEAGFRK
TPNNSEELIA QPLITKQGIP VNIRGQIDRI DAYTKDDKSY INIIDYKSSN PSAKLDLKKV
YYGKQMQMMT YMDIALQNAQ RLGLSNEIKP GGLLYFHVHD ERLSFKDWGE LEDDALTQDK
LEQAFLKEYK LRGLVNSDMD VVDALDIRLE EIGKSDIVPV SLKKDGSIGS RGSSVADETT
IHKFIKHNKD NFIKTATNIM EGHTEVAPLK FDDQLPCQFC NFQSVCHVDT IIDSKHYRHV
EETIDPIKAI QDVELESGDH NE
