ID F3YAD0_MELPT Unreviewed; 1202 AA.
AC F3YAD0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 OrderedLocusNames=MPTP_0999 {ECO:0000313|EMBL:BAK21458.1};
OS Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB
OS 702443).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Melissococcus.
OX NCBI_TaxID=940190 {ECO:0000313|EMBL:BAK21458.1, ECO:0000313|Proteomes:UP000008456};
RN [1] {ECO:0000313|EMBL:BAK21458.1, ECO:0000313|Proteomes:UP000008456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443
RC {ECO:0000313|Proteomes:UP000008456};
RX PubMed=21622755; DOI=10.1128/JB.05151-11;
RA Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M.,
RA Miyoshi-Akiyama T.;
RT "Complete genome sequence of Melissococcus plutonius ATCC 35311.";
RL J. Bacteriol. 193:4029-4030(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 35311;
RA Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D.,
RA Akiyama T.;
RT "Whole genome sequence of Melissococcus plutonius ATCC 35311.";
RL Submitted (APR-2011) 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01453};
CC Note=Binds 1 [4Fe-4S] cluster. {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}.
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DR EMBL; AP012200; BAK21458.1; -; Genomic_DNA.
DR RefSeq; WP_013773896.1; NC_015516.1.
DR AlphaFoldDB; F3YAD0; -.
DR STRING; 940190.MPTP_0999; -.
DR KEGG; mps:MPTP_0999; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OrthoDB; 9758506at2; -.
DR Proteomes; UP000008456; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
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 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01453};
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 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 Iron {ECO:0000256|HAMAP-Rule:MF_01453};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01453};
KW Metal-binding {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}; Reference proteome {ECO:0000313|Proteomes:UP000008456}.
FT DOMAIN 5..282
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21445"
FT DOMAIN 810..1156
FT /note="PD-(D/E)XK endonuclease-like"
FT /evidence="ECO:0000259|Pfam:PF12705"
FT BINDING 820
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01453"
FT BINDING 1150
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01453"
FT BINDING 1156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01453"
SQ SEQUENCE 1202 AA; 140130 MW; D927F0ABA59E4E5B CRC64;
MSLQFIRGKM TADLEEPLIQ QAVNWLDQSA NHEVFYLVPR HIEFEKEIDV LKKIRQMNRD
TMIASTRLQI FNFDRLAWYY LRDTSYYSSK LLPEAGAAML FRQVLLENEQ ELQIFQGEIT
KEGFIQQLFV FYQEIQDGNI TIDELDTFLT QLDKGAKEQE LQIKLKDLAL IFTKFEEKAK
NYQFDTKKIV ENLTKYLTNQ NLSHVSFLIS GFHQFTAKEL ELICLLIKKA GEVKISLPLD
RSYTNSLPEP MDIFAETGTL YYQFYQFART NRVPLFTDYV VNESSLIPTT GICQLENYWI
AAQKQYFPKM QQQILDNCVQ IWKGENVKEE ILSVACEIRR LVAEEGYRYK DIQLITRDMA
CYENLLKPLL ALYDIPIYLD HDQTMEQHPL VEWIQSFFAI YNYNYRYRDI LRFLRTELFF
PKENQKWETI EQWQAACREW RNKVDITENV VLAYGYEGTY WSRKQDWSFI QYDFEEHKLE
NTKQIEEDSN EIRQKVQKYL PVCFKKLKKA KNGLEAAKIF HHFLIESGVK YQMNQWRIQA
IEAGNLEEAK NHEQVWTALM TLLDEYVEIY KNEPFFFETF QEIFTSGLAG INYSRIPATI
DQVQVRLIDL TRAAAAKVIF AIGLTEEAFP KKIENKTLLS DEERQLIDLY LADDQFLANS
TEKKIAQEPF IAYKMLVSAT EKLYLTYHCT KDTKQEIKCS PYIRNIQQAF MLPIIEKREG
LPTDDEAISL THIGTYPALI GELTRLKRQN QEIGEPVSGF WLAMEKALTR QPEISQTASF
VFSSLGYTNN PENLTETFAE ALYGKHIYTS ISQMEAFHHC QFQYFLQFGL NLKERLLFQL
TSAATGEFFH EALDQFFKLL IRQNKYLPDL TDEEVANFSD NVLTAVLDEP KFSILTSSNR
MNYLRYQLSQ TIKKVSWALK KQSQKSGFST VQTEILFGQL AIQQGIPGLE LALEKQGKIS
VRGKIDRVDQ LITNDHEVYL GVIDYKSSHR KFNITEVYYG LAMQMLTYLD VALMDAVQLV
GKTAKPAGSF YLHVHNPTLS YDTTGAIEQK LLKKYQYDGL LINDSELLNY LDKELEEKTS
STIFPIEASA KGIIKPGRKQ ENKFVTEMEL QSLLKNNREK IKKAGNKIIN GEIQMNPAYQ
GKERIACRFC QFKSICTFDT MLKENNYHKI ATLSKKEVME RLSKEGIECI DDGKKDSITT
TK
//
