ID   ADDB_LEVBA              Reviewed;        1201 AA.
AC   Q03NA6;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=LVIS_2268;
OS   Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM
OS   1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=387344;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB
RC   947 / NCTC 947;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000416; ABJ65316.1; -; Genomic_DNA.
DR   RefSeq; WP_011668933.1; NC_008497.1.
DR   AlphaFoldDB; Q03NA6; -.
DR   SMR; Q03NA6; -.
DR   STRING; 387344.LVIS_2268; -.
DR   EnsemblBacteria; ABJ65316; ABJ65316; LVIS_2268.
DR   KEGG; lbr:LVIS_2268; -.
DR   PATRIC; fig|387344.15.peg.2172; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000001652; 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; -; 3.
DR   HAMAP; MF_01453; AddB_type2; 1.
DR   InterPro; IPR014141; DNA_helicase_suRexB.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; Exonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1201
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379366"
SQ   SEQUENCE   1201 AA;  135650 MW;  D5574BB1BAE42D33 CRC64;
     MSLQFILGSA GQDHRTPMVT ALAQQVTAHP TDQSYYLVPN HIKFETEVDV LSALKEQIAP
     EQALFAQTQV QVFSFTRLAW FFMKNEPIYQ LPRISPAGLN MLIYQIIQTH ADELTIFRGE
     VDRPGFVSQL ATQLAEFKVG QVTAADLMSA IEQLDTTNTD LQAKLHDLMI IYEAFETQMM
     GKFVENTDLL NQLATYLEQQ VDLQHAHFYL EGFSQLSAQE RQLVAILIQR SASVTVALNL
     DHGYPQKLPD KTTLFFQSAK LYQQLYMVAQ ANRVPVLIDQ QAKTARVSAD LQALDTYWQA
     SQTLSPQPSA VEKPTHIQIV QAANRYVEVS RVATQIRQLV ATGNYRYRDF LVLTRHLDAY
     QTVIDPIFQA QAVPYFDDAD IRMADHPFVE LLNALFDVQR RNYRYADVFR VLKSELLLPR
     DADGELMAVP AYRQALALTE NFVLKNGLEG QHWWTQDKDW VYNRFAVGDG GVQTTRDDQI
     SAQINRIRRF VKQTLPPFFA RLKVAATYTD AAAVLYQFVA NAGVSERLMT WRDQAIAAGD
     LTKAGQPEQT WAAFCDILDE FHTILGDLPT VLPDFQALLQ AGFAGAKFSQ IPSTLDQVVI
     SESGIVQANN RKITFIMGAT ADTMPDNQIP TTLLADNDRQ DLSARLQQVD DGTYLRDDAA
     TQLAGEPYLN YLAFMSGSER LIFSYPAMSD DARSGLQLSP YVARIKDYFG LSIDIAAANP
     VAEDEAILPF VGTRRTTLRH LVQASHDSQL REVPLSRSWL YVLNLLRTDP TYGELTTKLL
     GSLSYRNVPT QLTPDIVTQL YGTKINTSIS KLEEYYANPY AYFLKYGLNL QERDVFALSP
     ASTGEFFHAT LDGLMKLVND QKLNLAALDD QQLREMTDEV MAKLLDTTEN PQFAILESSH
     RMGYIRQQLM KTMRQMAKTL QEQSKRTKLR PKRTEVQFGL GDERGLAALS FDVGKRRQVT
     VRGRIDRLDA VQVKDKTYLG IVDYKSSEHK FSYQEAYYGR AMQMLTYLDA VKQNLPTLLD
     APTAKDAELA GAVYLHLQNP ILKAAEVLGE DPLTSLLKAE QYQGLLLDDP DLLTNLDTLF
     GTPDYSGSSL LFRGLRRTKT GKITSYGKLL VNSNELDLLL THTERLIKRA ATDIFDGRVD
     LAPFREQNRT ALQYSPYKSV MQFDPLLKEN NYRDLPSLNK DDVMARIAAE QEQEATDEHE
     I