ADDB_LACP3
ID ADDB_LACP3 Reviewed; 1179 AA.
AC Q038V6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=LSEI_1490;
OS Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 /
OS CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=321967;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 / NRRL
RC B-441;
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; CP000423; ABJ70266.1; -; Genomic_DNA.
DR RefSeq; WP_011674520.1; NC_008526.1.
DR RefSeq; YP_806708.1; NC_008526.1.
DR AlphaFoldDB; Q038V6; -.
DR SMR; Q038V6; -.
DR STRING; 321967.LSEI_1490; -.
DR EnsemblBacteria; ABJ70266; ABJ70266; LSEI_1490.
DR KEGG; lca:LSEI_1490; -.
DR PATRIC; fig|321967.11.peg.1471; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000001651; 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 Gene3D; 3.90.320.10; -; 1.
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; IPR011604; PDDEXK-like_dom_sf.
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.
FT CHAIN 1..1179
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379367"
SQ SEQUENCE 1179 AA; 131760 MW; F92B793EF71C969D CRC64;
MGLQFILGDA TTDHAGTMAT MVQANLQADS QNQIFYLVPN HIKFEAEVDL LKRLRAQAAS
VNGVYAQNRV QVLSFSRLAW YFLKNTALYQ QPRLDRASNT MLVAKILGES KEELTIYAGE
AHNTGFVTQL ADQLSELVTG RITAEDLNTT VAALTPGDRH RAKLRDLGII LDHYEAEIGP
YATNASLLSG LQQVMRNQDL SHTFIYLNDF NVFSASETGL VETMIETAAE VTVSLVLDKP
YPAAPPVAPN LFLPAGRLYH RLYQKAKTMK VPIRLDRFAK PRPLSEGMKH LADWWQTSTN
LQPQAPAQTA QNKEVELAVA TDPYHELRTV ARQIYQAVRQ GARYRDFLIL ARRLDPYAAV
IPAIFEEFNI PQFTDLERPM KDHPLVVLIE SLFAIQDHDY QYQDVMRLLH TELLLPENMD
IAAFRDALDT TDNHLVRTGI TGKKRWTQTD PWRYFQRNPN ADDSQLDPEA DKTAQINAIK
TLVADTVPQL LRQWQTAKTG REAAASLYQW LQTTGVIDQL NVWRQTANAD GDLSRSQANE
QAWDTFTQLL NDYATILGEA DFNRDQFREL LAAGFASATY TQIPSTLDSV VISETGLVRL
AKAKHVYVIG ATNTAMPDVP NDSGVLNSEE RQLLAAQLPD DRFLPEQGPT TTLGDPFINY
LGFMAASEKL TLSYPMQNTQ ENSENQASPY FRQLAQALQL TPATWAPAGL GTSLKAVLGS
QRAMLSDFVR AAGEAQHQKL PLSRSWQGVL ASLKQTTLAP LAQKLAGSLT YQNDPGRLDP
TLAVQLYGRD MNVSVSRLET YYRNQFEYFL KYGLLLQPRP EFELSPADTG SLFHAVLDQY
LTQLRDAGQT LADVTAADVA AAVPPLVAAI TKRPGYEILG STHRMAYLTS RLSRLLIQVL
TNMRQQQRRT GFRPMRTELQ FGRIGDTRGL PGLSWPLPHG GRVNVRGKID RLDVYRESDA
QRFMVVDYKS TQHRFDDSDA YYGIALQMLT YVEAMANVPA DPPFVPAGAL YFHLQDPKFK
FSTDLDLDID RLKAFKYLGF LVAKDGADLA AVDKTISAET GGRSMMVPLG FKKDGAFNYN
QSNILTPEDL SAYLLHNQAL IIDAASRILA GDIALAPFQY GQESTVISNS DYQSIMLFDP
ATGFDHYNHV PKLKRKEVLG RVTTDPTQIP HHRQEDSQA
