ADDB_STACT
ID ADDB_STACT Reviewed; 1155 AA.
AC B9DIT7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Sca_0574;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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; AM295250; CAL27488.1; -; Genomic_DNA.
DR AlphaFoldDB; B9DIT7; -.
DR SMR; B9DIT7; -.
DR STRING; 396513.SCA_0574; -.
DR KEGG; sca:SCA_0574; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR BioCyc; SCAR396513:SCA_RS02935-MON; -.
DR Proteomes; UP000000444; 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..1155
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379218"
FT DOMAIN 1..278
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 270..584
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 785
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 1155 AA; 134146 MW; 45F941D699C28341 CRC64;
MSQLNAYIGR AGTGKSHAML DEIKTKMKQD PLGDPIIIIA PTQSTFQLEQ DFVKDPELNG
SLRTEVLHFE RLSHRIFQEI GGLTEEYASK GALEMMIFDI LQSHRSELNL YQSQTKYYGF
SAKLSEQIQD FKKYAVSPEQ LEQFISENPL QTRTQDKLHD IALVYRHLEE RLADNFVSSE
DTLYKFIEKM DESKWLKRAE IYIDGFHNFS TLEYQIIEKL AQCAKSVSIL LTTNGDKDPF
SLFRKTSSTL THIEEIAQRQ NIDFNLRRFT KQERFENRDL SHLEHSFNEV FFDKAAAEGN
INILETSNVR EEVNAIARDI IRKAREENIR FQDVAVLYRD ETYAHLMESV FPEFDIPFNI
DTKKSMTHHP VMEMIRSLLE VIESKWSFEP LMRLFKTQVL TKKFKDNRYL TDILENYVLE
RGIYGQRWLD DKYFKIEQFN LMGLKRQPMT EETEADYQRV IDLKNYVIDK ILRFEKALAE
ADTAETYAAA FYEAFEQFNL PSQLMTERDE LDLAGEHQQA EELDQVWNGF IQTLDDLATV
FGNREMTQKR FLELFDVGLE QLEFVMIPQT LDQVSIGSMD LAKVDNKKHI YMLGMNDGTM
PQAISNSGLI SDDEKKYFQE ETQLELSPTA DVLQMDEAFV CYIAMTRAST HVTFSYSLMG
LNNDDKEVSP FIQNIRDLYT NLDVLNVQYA AQHNPLTVME HPHQTKIALF EELQSWLNHE
LTAETWLEAY QAMLHNERLS RGLQYLTSAL TFDNKTIQLN QSLSKALYGD KINASVSRFE
GYQQCPFKHY TSHGLRLNER TKYKLENFDL GDIFHSVLKY IADKIHGDFR NLTDASIRKL
TQEALENILP EVQYNLLNSS AYYRYMSVRI GAIVQSTLTA LKYQGTFSKF RPQAFEKSFR
KNPKSNEQLA AESLYTSQGI SINIRGQIDR IDTFNSKDRS FVNIIDYKSS GYSGTLDLTK
VYYGLQMQMM TYMDVVLQNK ERLNLAETTE PGGLLYFHVH EPRVNFANWA EMDEDKRQEE
LLKSFKLNGL INSDPEVLDA EDTRLEPKFK SDIVPIDVGA KGNLNKSSKV ADSQTIYKFI
EHNKNNFIQI ASDIMDGHTQ VAPMKYKQKL PCEYCNYRSV CHVDGMIDSK KYRTVDESIN
PIDLLNQESD EDDEE
