ADDB_STAS1
ID ADDB_STAS1 Reviewed; 1153 AA.
AC Q49WA5;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=SSP1809;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18954.1; -; Genomic_DNA.
DR RefSeq; WP_011303504.1; NZ_MTGA01000039.1.
DR AlphaFoldDB; Q49WA5; -.
DR SMR; Q49WA5; -.
DR STRING; 342451.SSP1809; -.
DR PRIDE; Q49WA5; -.
DR EnsemblBacteria; BAE18954; BAE18954; SSP1809.
DR KEGG; ssp:SSP1809; -.
DR PATRIC; fig|342451.11.peg.1805; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000006371; 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; -; 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;
KW Reference proteome.
FT CHAIN 1..1153
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379222"
FT DOMAIN 1..289
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 1110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1119
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1153 AA; 133645 MW; 1CB1EBB3BB36845D CRC64;
MELNAYIGRA GTGKSKAIIE EIKEKMKQDP LGDPIVLIAP TQNTFQLEQA FVNDKTLNGS
LRTEVLHFER LSYRVFQEVG GLMEQQLSKA GTEMMIYDII QQHQSELRLY QSQVKYYGFS
EKLYEQIQDF KKYAVSPQQL ETYIAENNLQ TRTKHKLQDI ALVYKHLEDR INGEYVSTED
SLQRFIEMMD QSEWLKRAEI YIDGFHNFST LEYQIIQSLV KYAKKVTIVL TTDGDRDLFS
LFRKPSESLT HIEEIANNLN IQLHSRQFLD VQRFIHNDLK HLEQNFNALQ FEPIPTEGNV
EILEASGMRE EINEVARRIL RENREQGRRF QDIAILYRDE SYAYLMESIL PQYDIPYNID
VKSSMTHHPI MEMIRSLIEV IQTGWQFDPL MRLFKTNILT KKFKDSQYLI DILENFVLER
GIYGKRWIDD KYFDIEQFRK MGLKRQPLTD EERETFERVI QLKNDVMKKV MLFEEKINNA
STAIAFATAF YEAMEAFDLP SQLMTDRDTL DVNGEHKKAE EIDQIWNGLI QILDDLVTVF
DDQSMSKTRF LELFDIGLEQ LEFIMIPQTL DQVSIGTMDL AKVDNKQHVY LVGANDGVLP
QTVTASSLIT DEEKKYFQEQ SSIELSPTAD ILQMDEAFVC YIAMTRSRAH VTFSYALMGA
SGDVKEPSPF LHQIQQLYTN LEVQNIHHQH QAEPLRLMEH PHQTKIALFE SLKAWLDDEL
VAETWLDTYQ VMRNDTRLND GLTYLLSALT YDNQTVQLNP SLSKALYGST INASVSRFEG
YQACPFKHFA SHGLRLNERT KYKLENFDLG DIFHRVLKFI SEKVNGDFKN LNPKQIHKLT
TEALSEILPE VQFNLLNSTA YYRYLSQRIG AIVETTLTAL KYQGSHTKFT PQRFEASFRR
KPKDQSELLA TPLQTKQGIP INIRGQIDRI DTYQQGDESF VNIIDYKSSK YSGTLDLTKV
YYGLQMQMMT YMDIVLQNKS RLGLTDMTKP GGLLYFHVHE PRIKLAWNQL SEDKRDTEFI
NSFKLSGLLN SATSVLDAFD TRLEPSYNSD IVPLGLKKDG GIKSNSKVAD EQTIYKLIKH
NKQNFIETAS NIMDGHTEVA PMKYNQTLPC DFCNYKSVCH VDGMIDSKRY RTVDESINPL
EAIQDVDLES EGE
