ID A0AAN3XES7_LACRH Unreviewed; 1179 AA. AC A0AAN3XES7; DT 02-OCT-2024, integrated into UniProtKB/TrEMBL. DT 02-OCT-2024, sequence version 1. DT 27-NOV-2024, entry version 2. 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 AltName: Full=ATP-dependent helicase/nuclease subunit RexB {ECO:0000256|HAMAP-Rule:MF_01453}; GN Name=rexB {ECO:0000256|HAMAP-Rule:MF_01453}; GN ORFNames=LRHMDP2_722 {ECO:0000313|EMBL:EKS52650.1}; OS Lacticaseibacillus rhamnosus LRHMDP2. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lacticaseibacillus. OX NCBI_TaxID=1203258 {ECO:0000313|EMBL:EKS52650.1, ECO:0000313|Proteomes:UP000009330}; RN [1] {ECO:0000313|EMBL:EKS52650.1, ECO:0000313|Proteomes:UP000009330} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LRHMDP2 {ECO:0000313|EMBL:EKS52650.1, RC ECO:0000313|Proteomes:UP000009330}; RX PubMed=23405363; RA Chen Z., Wilkins M.R., Hunter N., Nadkarni M.A.; RT "Draft Genome Sequences of Two Clinical Isolates of Lactobacillus rhamnosus RT from Initial Stages of Dental Pulp Infection."; RL Genome Announc. 1:E00073-E00012(2013). 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 but not helicase activity. {ECO:0000256|HAMAP- CC 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 -!- MISCELLANEOUS: Despite having helicase-like domains, this subunit does CC not have helicase activity. {ECO:0000256|HAMAP-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:EKS52650.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AMQW01000003; EKS52650.1; -; Genomic_DNA. DR RefSeq; WP_005715396.1; NZ_AMQW01000003.1. DR Proteomes; UP000009330; Unassembled WGS sequence. DR Gene3D; 3.90.320.10; -; 1. 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; IPR011604; PDDEXK-like_dom_sf. DR InterPro; IPR038726; PDDEXK_AddAB-type. DR PANTHER; PTHR30591; RECBCD ENZYME SUBUNIT RECC; 1. DR PANTHER; PTHR30591:SF1; RECBCD ENZYME SUBUNIT RECC; 1. 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}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_01453}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_01453}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_01453}; KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP- KW Rule:MF_01453}; KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01453}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01453}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01453}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01453}. FT DOMAIN 5..279 FT /note="ATP-dependent helicase/deoxyribonuclease subunit B FT N-terminal" FT /evidence="ECO:0000259|Pfam:PF21445" FT DOMAIN 793..1051 FT /note="PD-(D/E)XK endonuclease-like" FT /evidence="ECO:0000259|Pfam:PF12705" SQ SEQUENCE 1179 AA; 132464 MW; 332CD2435381BA41 CRC64; MGLQFILGDA TTDHTQTMAA MIHEKLTADS QNRIFLLVPN HIKFEAEIDL LKRLRQLQQG NSETYVQSRV QVLSFSRLAW FYLKNTPLYQ QPRLDQASNT MLVAKILAER QADLTIYAGE AQHTGFVTQL ADQLSELMIG RITAEDLANT VAALTPGDRH RAKLRDLGII LDQYEAEIGP YATTASLLSG LQQAMRTHDL THTFIYLNHF NVFSASESAL VETMLETAAE VTIGLVLDRP YPTAPPVAPN LFLPAGRLYH RLYQKAKTMR IPIRLDRFAQ PRHLSLGMRQ VASWWQANTN IEPQPAPPAN VADQVHLATA TDPYQELRHV AQSIYQAVRN GARYRDFVIL ARRLDPYATI IPAIFAEFQI PQFTDLQRPM KDHPLVVLIE SLFAIQDHDY QYQDIMRLLH TELLLPQGMP VADYRDAIDT LDNHLVRTGI AGKRRWTQAE PWRYFQRNPA ADETEMDPEA DKTAQINAIK TLVAQTVPAL LKQWQAAKTG LEAARSLYHW LTKTGVEDQL NAWREAASTV GELARSRAHE QAWTTFTALL DDYVTILGNA KFNREQFHEL LAAGFASATY TQIPATLDAV VISETGLVRL AKAKHVFVIG ATSTAMPDVP NDDGVLNSEE RQLLASQLPD DRFLPEQGPT TTLGDPFINY LGFMAASETL TLSYPMQNPQ ENSENQASPY FQQLKRALHL VPETWAPVTL ATTVKSVLGS PRAMLSDFIR AAGDAQQQKQ PLSLAWQSVL SALKQTDLAN LAQRLAGSLT YQNDPGRLDP QLAVQLYGRD MNVSVSRLET YYLNHFEYFL KYGLLLQPRP EFELSPADTG SLFHAVLDRY LTQLRDQQQN LVDVDPAAIM AAVPPMVAEI AKQPGYEILG STYRMTYLTK RLSRLLIQVL LNMRQQQQRS GFRPVRTELQ FGRIGDTKGL PGLSWPLPHG GRVNVRGKID RLDIYREPDA RRFIIVDYKS GQRRFDDSDA YYGIALQMLT YIEAMTNVTA EPPFVPAGAL YFHLQDPKLK YTPELEPALE RLKAFKYLGF LVAEHGDELA AVDRTISPES GGRSEIAPLG FKKDGSFNQN QSNVLTPEAL RAYLAHNQAL IIDAATQILA GDIALEPFQY GQSSTIVSRS DYQSIMLFDP ATGFDHYHHV PKLKRKDVIG RLTADPTQIP HSEKEHPQS //