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Database: UniProt
Entry: I0RPV8_MYCXE
LinkDB: I0RPV8_MYCXE
Original site: I0RPV8_MYCXE 
ID   I0RPV8_MYCXE            Unreviewed;      1085 AA.
AC   I0RPV8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=RecBCD enzyme subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
DE            EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01485};
DE   AltName: Full=Exonuclease V subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
DE            Short=ExoV subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
DE   AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
GN   Name=recB {ECO:0000256|HAMAP-Rule:MF_01485};
GN   ORFNames=MXEN_11720 {ECO:0000313|EMBL:EID13161.1};
OS   Mycobacterium xenopi RIVM700367.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID13161.1, ECO:0000313|Proteomes:UP000003584};
RN   [1] {ECO:0000313|EMBL:EID13161.1, ECO:0000313|Proteomes:UP000003584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIVM700367 {ECO:0000313|EMBL:EID13161.1,
RC   ECO:0000313|Proteomes:UP000003584};
RX   PubMed=22628510; DOI=10.1128/JB.00482-12;
RA   Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S.,
RA   van Soolingen D., Bitter W., Pain A.;
RT   "Complete Genome Sequence of Mycobacterium xenopi Type Strain RIVM700367.";
RL   J. Bacteriol. 194:3282-3283(2012).
CC   -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
CC       recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly
CC       rapid and processive ATP-dependent bidirectional helicase activity.
CC       Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator)
CC       sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the
CC       Chi site. The properties and activities of the enzyme are changed at
CC       Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and
CC       facilitates RecA-binding to the ssDNA for homologous DNA recombination
CC       and repair. Holoenzyme degrades any linearized DNA that is unable to
CC       undergo homologous recombination. In the holoenzyme this subunit
CC       contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA
CC       onto ssDNA. {ECO:0000256|HAMAP-Rule:MF_01485}.
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=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage (in the presence of ATP) in either
CC         5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC         phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01485};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01485};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01485};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC       to DNA-binding. Interacts with RecA. {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- DOMAIN: The C-terminal domain has nuclease activity and interacts with
CC       RecD. It interacts with RecA, facilitating its loading onto ssDNA.
CC       {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent ATPase
CC       and has ATP-dependent 3'-5' helicase function. This domain interacts
CC       with RecC. {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01485}.
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:EID13161.1}.
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DR   EMBL; AJFI01000062; EID13161.1; -; Genomic_DNA.
DR   RefSeq; WP_003921186.1; NZ_AJFI01000062.1.
DR   AlphaFoldDB; I0RPV8; -.
DR   PATRIC; fig|1150591.3.peg.2353; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000003584; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   CDD; cd22352; RecB_C-like; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01485; RecB; 1.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
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   InterPro; IPR004586; RecB.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   NCBIfam; TIGR00609; recB; 1.
DR   PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01485}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01485};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01485};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01485};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000313|EMBL:EID13161.1};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01485};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01485}; Nuclease {ECO:0000256|HAMAP-Rule:MF_01485};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01485}; Reference proteome {ECO:0000313|Proteomes:UP000003584}.
FT   DOMAIN          1..326
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          357..613
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          1..750
FT                   /note="DNA-binding and helicase activity, interacts with
FT                   RecC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   REGION          775..1085
FT                   /note="Nuclease activity, interacts with RecD and RecA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   ACT_SITE        985
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   BINDING         21..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT   BINDING         838
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   BINDING         971
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   BINDING         985
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
SQ   SEQUENCE   1085 AA;  118945 MW;  73BD98C273D6E83A CRC64;
     MDRFDLLGPL PRDGSTTVLE ASAGTGKTFA LAALVTRYLA ETGITLDEML LITFNRNASR
     ELRERVRGQI VEAVAALEGR MPAGADLLGQ LTRDDGDERL VRRARLRDAL ANFDAATIAT
     THEFCGRVLK SLGVAGDTAA DVKLQENLDD LVTEIVDDLY LAHFGSAEND PVLSYQQARE
     LAHCVVNDPC AQLRPQDPDP ESEAGIRLRF AADVTRELDH RKRRLRILSY NDLLTRLAKA
     LEAQDSPARD RMRRRWRIVL VDEFQDTDPI QWQVLERAFS GYATLILIGD PKQAIYGFRG
     GDIHTYLKAA RTADARYTLG VNWRSDKPLV DSLQTVLQGA ALGHSEIVVH DIDAHHDGHR
     LAGAPHNAPF RLRVVKRSAL GYDPDELIPI ARLRQHIPAD LAADIADLLA SGATYAGRPV
     QPGHIAVIVN RHEDARACRD ALASAGIAAI YSGDSDVFES QAAKDWLCLL EAFDAPHRSG
     LVRAAACTLF FGETAETLAA EGDALTDRVA ETLREWAGHA RRRGVAAVFE AAQRAGMGRR
     VLAEQGGERH MTDLAHITQL LHQTAHRERY SLPALRDWLR RQCDTRARVT EHSRRLDSDA
     DAVQIMTVFV AKGLQFPIVY LPFAFNRNAR SDDILLYHDD DTRCLYIGGQ DRSAEREAAK
     ELNLRENAHD NLRATYVALT RAQSQVVTWW APTKDEVNGG LSRLLRGRGI GEPKVPDTCE
     RRITDDDAWA VFKCWEAAGG PAVEESVIVS PATVETGGPP TGFEVRHFHR AIDTGWRRTS
     YSALVREPES VDVASEPEAT TRDDEVDSVV VTAPAPGFDI ASPLAAMPSG AAFGSLVHAV
     LETADPSAAD LQAELDAQVR RHLAWWPVDV AADELASALV PMHDTPLGPL AAGLTLRQIG
     AGDRLRELDF EMPMAGGDLR DAAPEVWVRD VGELLRSHLP AGDPLAPYAE RLTSAPLAHQ
     SLRGYLTGSI DVVLRIPGPR YLLADYKTNR LGDTAADYSA ARLAEAMLHS DYPLQALLYV
     VVLHRFLRWR QPGYDPGTHL GGVLYLFVRG MCGPDTPGCG VFGWRPPAQL VVALSDLLDA
     GRQAA
//
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