ID   ADDB_STRU0              Reviewed;        1086 AA.
AC   B9DRU9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000255|HAMAP-Rule:MF_01453};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01453};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01453};
DE   AltName: Full=ATP-dependent helicase/nuclease RexB {ECO:0000255|HAMAP-Rule:MF_01453};
GN   Name=rexB {ECO:0000255|HAMAP-Rule:MF_01453}; OrderedLocusNames=SUB0685;
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J;
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA   Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA   Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA   Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(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. This subunit has 5' -> 3'
CC       nuclease activity. {ECO:0000255|HAMAP-Rule:MF_01453}.
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_01453};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01453};
CC   -!- SUBUNIT: Heterodimer of AddA and RexB. {ECO:0000255|HAMAP-
CC       Rule:MF_01453}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01453}.
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DR   EMBL; AM946015; CAR41581.1; -; Genomic_DNA.
DR   RefSeq; WP_012658203.1; NC_012004.1.
DR   AlphaFoldDB; B9DRU9; -.
DR   SMR; B9DRU9; -.
DR   STRING; 218495.SUB0685; -.
DR   PRIDE; B9DRU9; -.
DR   EnsemblBacteria; CAR41581; CAR41581; SUB0685.
DR   KEGG; sub:SUB0685; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_1_0_9; -.
DR   OMA; NESSEDM; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000000449; Chromosome.
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: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_01453; AddB_type2; 1.
DR   InterPro; IPR014141; DNA_helicase_suRexB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR02774; rexB_recomb; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; Exonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1086
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379418"
SQ   SEQUENCE   1086 AA;  126354 MW;  E0A24A5839C1B0DA CRC64;
     MKLLYTDIEN SLTEILVQEA EVFANSGARV FYIAPNSLSF EKERTVLEHL TKESSFSITV
     TRFAQMARYF TLNKQKAQKS LDDLSLTMLF HLVLHDLSQN ELTIYHALKS DQTFIKQLVD
     LFKEMQSANL TIADIEMENL ARKEDLITIF SALSRELLRY DFQQMSSLAV FQEAIRSGLL
     DQELAKTVVI IDGFTRFSAE EESLIHQLHQ KCQEIVIGTY ISSKAMKQNF TKGNLYEASI
     DFLRQLSVTY QVKSLYLSGE KTFKNSFTTM SRLLESQYDY SLTELTISED IKNDVQIWQQ
     LNQKEEIENI ARDIRQKLNE GYRYKDILVL LGDVEAYQLQ VGPIFDKYDI PYYLGKAESM
     SHHPLVQFMD SLENCRRYNW RKEDIINLLK SRMLGDFTIR ECDQFESYLN YADINGFTAF
     SKDFTANTFN QKNEKGYDLD KINLIRKYLF SHLNQFFKSR AQKGSNILNH FLQFLSDIDF
     VSSFQRLSQK QSALQQEKDE EVWKSFTSIL ESFYNIFKDE TLTQELTLML IKSAMQAADY
     RVVPATLDVV SVKSYDLVEP HSKSLVYALG LTRTHFPKTV QQTGLISDQE RAKTNEKWDS
     HHRFDISSIE NSKKNHYTAL SLFNAATDKL VLSYPMVLNE VVEEASPYLK LLHSFGIPIV
     EKQKNTFSDL ENGIGNYKSL LSQWIALNQE PLTEELYQEE KSFWLVMSRY LKKQLAAKKL
     TFPEQKSHLA TSRLSPEVLA IKYPDHQPLS LSSSALTVYH DNQYKYFLQY VLGLQELESI
     HPDARHHGTY LHRVFEYVVD DQRSIPFDDK IEEAIQRTNQ ERLFQTYYQS DAESRFSLSL
     LEDIAKSTAS IFPITPTKVL SQEERFQLHF DEKVRVNGII DRIDQLDDGS IGIVDYKSSQ
     TVFDIGKFYN GLNSQLPTYL EALNTREKSK DMPPQLFGAM YLHMQDPKMD LNEFKLFDDK
     VVEKLYSRLT YKGIFLEREK EHLASGAYQM KSNLYSEEEL RNLLDYNQFL YLKAEKEIRA
     GHFLINPYTE DGKTVKGDQL KAITRFEADL DLGQARMLLK LPTKEKREGF LKLMKEDMKG
     GKKDEI