RECB_CHLMU
ID RECB_CHLMU Reviewed; 1026 AA.
AC Q9PLT8;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=RecBCD enzyme subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01485};
DE AltName: Full=Exonuclease V subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE Short=ExoV subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
GN Name=recB {ECO:0000255|HAMAP-Rule:MF_01485}; OrderedLocusNames=TC_0007;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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:0000255|HAMAP-Rule:MF_01485}.
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:0000255|HAMAP-
CC Rule:MF_01485};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01485};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. Interacts with RecA. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01485}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01485}.
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DR EMBL; AE002160; AAF38900.2; -; Genomic_DNA.
DR PIR; G81751; G81751.
DR STRING; 243161.TC_0007; -.
DR PRIDE; Q9PLT8; -.
DR EnsemblBacteria; AAF38900; AAF38900; TC_0007.
DR KEGG; cmu:TC_0007; -.
DR PATRIC; fig|243161.6.peg.17; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_6_3_0; -.
DR Proteomes; UP000000800; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 3.
DR Gene3D; 3.90.320.10; -; 1.
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 PANTHER; PTHR11070; PTHR11070; 1.
DR PANTHER; PTHR11070:SF23; PTHR11070:SF23; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR00609; recB; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleotide-binding.
FT CHAIN 1..1026
FT /note="RecBCD enzyme subunit RecB"
FT /id="PRO_0000102043"
FT DOMAIN 1..438
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT DOMAIN 452..700
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 1..776
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 815..1026
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT ACT_SITE 953
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 854
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 940
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 953
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT UNSURE 125
FT /note="L or I"
SQ SEQUENCE 1026 AA; 117832 MW; 4804515055FF6F93 CRC64;
MSSFDIFSPT TSVSGKFFLE ASAGTGKTFT IEQVILRSLL EGNVEQTKNI LVVTFTNAAT
NELKLRIQES LKQALTLFSQ ALSHPETPLP PYVSSQETKV KQLYXKXRNS LATLDEMNIF
TIHGLCRFTL EQHFPWVQPI HPSSMFSEPQ TIQQYILDYL RQNSWENVLS PKQYAFLSYH
HRATTQQTRH LADRLLQDYA STPNLALPPL SITLQKVKNW SSQYKHLSPL SLEELQDFSL
RFKQSDLPID RELPDFVKQF ETDPNSLDIL FFPGMVQKFQ EENRNKKKLG PPFSPLDPFL
KDWLLIAQPF CQKEPIFHTL LKSVQQHLKT YCAQSYSHDE SIATLESLLA QNDHVVSQLR
KQFQLVLIDE FQDTDKRQWK IFSKLFASPD YSGSLFLIGD PKQSIYEWRN ADLPTYLQAK
NSFPKESQLI LDTNYRSTPQ LMQALNHLFS LPSPFLETPQ TILYHPLQSK GSASTSYSEF
RPIHFFTTQD SQEEALWISK TASYLRSTFA IPFGNMAVLV QDYPQALKLI THSTIPMAYC
KEKRIFDRTE SPYLLILLLE ALLYPENQQK IQAILLSRFF HLSATDIHQH LKIFSSLFFM
LNTYLHQYSL LATFYKLMGE TVFSQTIGET LLQTPLGDII FQELEELCLY LDKTTENPHH
KLFHLINILD TGKYDEELSF SSQSNDDNVL KITTVHSSKG LEYDVVFCSS LNKVKEKSPS
VHMREMYVAC TRAKKFLFIP FSSIEKRLQS NKKVSALANY ANITQHDNIP HLVETLTASH
PEFFSSGTQP PESNISIFSE PLPEQEFFSL PILSSQPIYS FSSTTESQYF TEPFQEISSS
SLFPGGSLTG TLIHKLLESL SGNFNASLEE ITHKAQTLLK NTILEGFESI ISEKIYTAFS
TKLPFVSGSF ALKDVHPYNI RVEETFLLQE NGELWQGIVD LFFEHNNRFF IIDWKTSFLG
DEPSLYSPDK LLLYIQRQGL DKQGVLYKRA AKKFLHQFNS SLQIEMAFVF IRGIDDKGNG
FLQPSP
