ID A0A0R1LFF9_9LACO Unreviewed; 1201 AA.
AC A0A0R1LFF9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=rexB {ECO:0000256|HAMAP-Rule:MF_01453};
GN ORFNames=FC99_GL001440 {ECO:0000313|EMBL:KRK91796.1};
OS Levilactobacillus koreensis JCM 16448.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1423819 {ECO:0000313|EMBL:KRK91796.1, ECO:0000313|Proteomes:UP000050910};
RN [1] {ECO:0000313|EMBL:KRK91796.1, ECO:0000313|Proteomes:UP000050910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16448 {ECO:0000313|EMBL:KRK91796.1,
RC ECO:0000313|Proteomes:UP000050910};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRK91796.1}.
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DR EMBL; AZDP01000023; KRK91796.1; -; Genomic_DNA.
DR RefSeq; WP_048733808.1; NZ_AZDP01000023.1.
DR AlphaFoldDB; A0A0R1LFF9; -.
DR STRING; 637971.ABN16_05905; -.
DR PATRIC; fig|1423819.3.peg.1551; -.
DR Proteomes; UP000050910; 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:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
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 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}; Coiled coil {ECO:0000256|SAM:Coils};
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 Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW 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..287
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21445"
FT DOMAIN 807..1145
FT /note="PD-(D/E)XK endonuclease-like"
FT /evidence="ECO:0000259|Pfam:PF12705"
FT COILED 144..178
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1201 AA; 136090 MW; A9A5256EFF9A00E3 CRC64;
MSLQFVLGSA GMDHRTPMVA AMAAQLTSVP TDQCYYLVPN HIKFETEVDV LAELKERMAP
DQPLFAQTQV QVFSFTRLAW FFMKNEPVYQ LPRISTAGLN MLIYQIIQSH ADELIIFRGE
VDRPGFITQL TAQLAELKVG QVTAADLLTA VENLTTTNAD LQAKLHDLMI LYEAFETQML
GKYVENTDLL NQLADYLATR IDLSHAHFYL EGFSQLSAQE RKLVAVLIQR SASVEVALNL
DKGYPQELPD TTTLFFQSAK LYHQLYVEAR ADNVPVLIDQ QAASSRVSAD LLALDHFWQE
TNTLSPQPKP AVAALKNVKI VQAANRYVEV SHVATQIRQL VASGQYRYQD FLVLARHLDS
YQTVIDPIFK AQEIPYFDDA DVQMADHPFV ELINALFDVQ RKNYRYADIF RVLKSELLLP
QDDDGEPLEL NVYRRALALT ENLVLKNGYE GQYRWTQEKD WLYTRFSAGD DSVQTTHDEQ
VTAQINVIRH FVKAVLPPFF AKLKAAKTYT EASATLYQFL ENHGVSQRLM AWRDQAIAAG
DLFRAGQPEQ TWATFCQMLD ECHSILGEQP FNQADFQSLL QAGFAGAKFS QIPSTLDQVM
ISESGIVQAN NRKVTFLMGA TADSMPDDQV PTTLLADNDR QDLSEQLQAT DANSYLRDDA
ATQLAGEPYL NYLAFLSGSD RLIFSYPATS DGDGSLQISP YVARIRDYFK LPVTLAVAAP
EAQQTDILPF VGTRRTTLRH LVQASHDSQT REQPLSPNWL YVLRLLRADT TYGELTTKLL
GSLSYRNVPQ QLTPDIVTQL YGNKISTSIS KLEEYYANPY AYFLKYGLKL QERDVFELSP
ASTGEFFHAT MDGLMKIVNE QKLNLSDLDD QQLREMTDEV IAKVLDTTTN PQFAILESSN
RMVYIRQQLI KTMRQMAKTL HEQSKRTKLR PKRTEVQFGL GDERGLEALS FDLAKRRKVT
VRGRIDRLDA MQLQDKTYLG IVDYKSSEHK FSYQDAYYGQ AMQMLTYLDA VKKNLPELLA
NDTPVNAELA GAVYLHLQNP ILKAADVLGT DPLEALLKAE QYQGLLLDDP DLLTNLDSLF
ATDNYSGSSL LFRGLRRTVK GTITSYSKML VKPAELDLLL KHTERLIKRA ATEIFDGHVD
LAPFREQNRT ALQFSPYKSI MQFDPLLKEN NYRELPTLKK DDVMARIKAE QEKEAADERK
I
//
