ID Q9RPH6_MYCSM Unreviewed; 1083 AA.
AC Q9RPH6;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 123.
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 ECO:0000313|EMBL:AAD46808.1};
GN ORFNames=NCTC7017_00822 {ECO:0000313|EMBL:STZ33262.1};
OS Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1772 {ECO:0000313|EMBL:AAD46808.1};
RN [1] {ECO:0000313|EMBL:AAD46808.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Mc2155 {ECO:0000313|EMBL:AAD46808.1};
RX PubMed=10481025; DOI=10.1093/nar/27.19.3859;
RA Griffin IV T.J., Parsons L., Leschziner A.E., DeVost J., Derbyshire K.M.,
RA Grindley N.D.;
RT "In vitro transposition of Tn552: a tool for DNA sequencing and
RT mutagenesis.";
RL Nucleic Acids Res. 27:3859-3865(1999).
RN [2] {ECO:0000313|EMBL:STZ33262.1, ECO:0000313|Proteomes:UP000255288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC7017 {ECO:0000313|EMBL:STZ33262.1};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AF157643; AAD46808.1; -; Genomic_DNA.
DR EMBL; UGQO01000001; STZ33262.1; -; Genomic_DNA.
DR RefSeq; WP_011727605.1; NZ_UGQO01000001.1.
DR SMR; Q9RPH6; -.
DR GeneID; 66732787; -.
DR KEGG; msh:LI98_06615; -.
DR KEGG; msn:LI99_06615; -.
DR OMA; VDYKTNW; -.
DR Proteomes; UP000255288; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 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; 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};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01485};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01485};
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};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01485};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01485}.
FT DOMAIN 1..323
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 349..607
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..740
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT REGION 765..1083
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT ACT_SITE 975
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 830
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 962
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 975
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1083 AA; 117443 MW; A531F5FBA85EB748 CRC64;
MKVFDLLGPL PAPNTTTVLE ASAGTGKTFA LAGLVTRFVA EGVATLDQML LITFGRAASQ
ELRERVRAQI VAALVALDDP SRACNDLEEY LVKTDQQARR RRLRDALAGF DAATIATTHQ
FCQIVLKSLG VAGDSDAGVT LVESLDDLVS EIVDDLYLAH FGGQKDDPEL SYPEALKLAR
VVVGNPATQL RPRDPDPDSP AAVRLKFARD VLAELEIRKR RRGVLGYDDL LTRLADALEP
EDSPARVRMQ QRWPIVMVDE FQDTDPVQWQ VIERAFSGRS TLVLIGDPKQ AIYAFRGGDI
ATYLRAAATA GDKQTLGTNW RSDRALVDRL QAVLRGAQLG GPDIVVHDVQ ARHQGHRLVG
APRNDPFRLR VVSRKPGNTR VIPIDQLRRH IGRDLAADIS ALLNSGATWC DQPVQAKDIA
VITETHKDAR ACHAALLAAG IPAVYTGDSD VFTSEAAEDW LYLLEAFDQP HRPGLVRAAA
ATMFFGETAE SLAAGGDALT DRVADTLREW AGHARERGVA AIFEAAQLAG MGKRVLSWQG
GERLMTDLAH MTQLLQDTAH REGFGLAALR DWLRTQRSER GGESERNRRL DSDAAAVQIM
TVWVSKGLQF PVVYLPFAFN RYVPEPDLVL FHDDGQRCLH VGGADPAVAR AGRAEAAGDD
SRLTYVALTR AQSQVVAWWA PSYDEPNGGL SRLMRGRAPG EAIVPDKCSP PKISDEDALE
RLRAWEAAGG PVIEESVIGA VSPVPPEPAP EDLAARKFFR AIDMAWKRTS YSGLLRAAET
AGVGVSSEPE VTERDDEFDD IPVVAPAEGA DVPSPMAHLP TGAAFGSLVH AVLETADPFA
EDLTAELATH IDAHSQHWPV EVETAELAAA LVPMHDTPLG PLAPGLTLRQ IGLRDRLCEL
DFEFPMAGGD LRGGRFARLS DVGELLREYL PADDPLAVYA ERLSTGILGV QPLRGYLSGS
VDAVLRVGEK FVIVDYKTNW LGTGDGTLTA ADYGRRRMVE AMLHSDYPLQ ALLYAVVLHR
YLGWRLSGYD PATHLGGVLY LFVRGMCGAG TPVVDGHPAG VFSWEPPADL VVALSKLLDA
EAP
//
