ID A0A2Z6TGU6_9LACO Unreviewed; 1155 AA.
AC A0A2Z6TGU6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000256|HAMAP-Rule:MF_01453};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01453};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01453};
DE AltName: Full=ATP-dependent helicase/nuclease RexB {ECO:0000256|HAMAP-Rule:MF_01453};
GN Name=addB {ECO:0000313|EMBL:GBG05312.1};
GN Synonyms=rexB {ECO:0000256|HAMAP-Rule:MF_01453};
GN ORFNames=LrDSM24759_12260 {ECO:0000313|EMBL:GBG05312.1};
OS Lactobacillus rodentium.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=947835 {ECO:0000313|EMBL:GBG05312.1, ECO:0000313|Proteomes:UP000257317};
RN [1] {ECO:0000313|Proteomes:UP000257317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24759 {ECO:0000313|Proteomes:UP000257317};
RA Tanizawa Y., Tohno M., Endo A., Arita M.;
RT "New taxa in the Lactobacillus gasseri group.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01453};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01453};
CC -!- SUBUNIT: Heterodimer of AddA and RexB. {ECO:0000256|HAMAP-
CC Rule:MF_01453}.
CC -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01453}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01453}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBG05312.1}.
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DR EMBL; BFBY01000010; GBG05312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6TGU6; -.
DR OrthoDB; 9758506at2; -.
DR Proteomes; UP000257317; Unassembled WGS sequence.
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:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR HAMAP; MF_01453; AddB_type2; 1.
DR InterPro; IPR049035; ADDB_N.
DR InterPro; IPR014141; DNA_helicase_suRexB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR Pfam; PF21445; ADDB_N; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01453}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01453};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01453};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01453}; Helicase {ECO:0000313|EMBL:GBG05312.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01453};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01453};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01453};
KW Reference proteome {ECO:0000313|Proteomes:UP000257317}.
FT DOMAIN 5..285
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21445"
FT DOMAIN 767..1105
FT /note="PD-(D/E)XK endonuclease-like"
FT /evidence="ECO:0000259|Pfam:PF12705"
SQ SEQUENCE 1155 AA; 134667 MW; 8484E08B4AB588EC CRC64;
MINIITGRQT DPLQNQILDL AIKDYLKDPN HPIFIIVPNH IKFSVEVRTL NKLSNLTNQN
QVSVKNLQIL SFSRLAWYFL RNENKVIPEI LDDATSIMLL EEIVREKKDD LLLFRETEIT
QGALKQIYDA ILMMRQGNLD LNEIDENALN EETKYKIHDL SLIFDEYVDR LADKFAPKDE
MQFLLNQFLA ENNLADIDFY FSDFSHFSNQ EQLTLQLIAK KAHNLTIAFK TKNGDINPAV
EAGDYDYGVQ KTINKLEHFF KNQALHYQES TFPISSKLTK REKLNNVWAN NIKPTDSDLR
SFIQPVKADS RYAEAYFVAR TIYQQVALNN YRYSDFLVLA PNLEAYETYL TPILRQNKIP
FFNDLQRKMK FHPLVIAIEN LFQIYQRGFQ TSNLLALMKS NLFIPDWYHN ETEYQNDVDQ
LENFALAHGI NQNLWQHELN TFIDAQVITL DDAEAIVMRL EKLRKYYIDQ IEQLFEELKK
ETDTQLALTK FWDFLIQNKV HKQLEKWRSQ ANDTNDLQKA QQPEQVWSTL NQLLKDFLLL
NPNFDLESFF QVLIAGFSEA DFSQIPSTLD AVNISELGMV QGQTYKQIFI LGATSNDLPQ
IEKIPGFFST ENIDQLNQGL QGEQQIEDGQ KVNNLDQNYQ FGNALSLAQD RIYLSYPVLN
TANEELEPSI FYRQLLNRLD LDEFEQHDLP QSSSDILSFI TNPEASLGYL THLKRENYRQ
APALLKLSES KQPEVTKEVL AATEFKNIPH SLTPEIAQAL YGTNIETSVS QLETYYENSF
EYFLNYGLRL HKRFENELDV VQAGNYYHET FDRLVKFLQE TKLDLASLTV NQLQEILIKI
HTQMQEQGRY HQLLNDPFNQ YLFRQLDQTT ENVAKYWHRN LKKTTLRPQY SELSFGRSEQ
VKGLNYTFTN PTGKHQIDLR GKMDRIDLTK ENNKVIGAVV DYKSSAKKFD LGLFANGISL
QMVSYLDVLK KNHEFFANDQ ELDLLGAFYQ TITKNVERLN VDTNLNADFN LKDIKTNNEK
KLMYKGILNN DPALLESIEP LLQEDRASSE LYNSVKRKKD GSFSLPSDTS FNAEDLDQIL
EYNSYLIQQA AHKILDGNIE LNPYQYNKKT PLQYSDFKDI FFFDAMLKEN NYHKISSLKK
KELLQLIKET LEKED
//
