RECB_CHLTR
ID RECB_CHLTR Reviewed; 1026 AA.
AC O84645;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=CT_639;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC68243.1; -; Genomic_DNA.
DR PIR; C71490; C71490.
DR RefSeq; NP_220157.1; NC_000117.1.
DR RefSeq; WP_009872009.1; NC_000117.1.
DR AlphaFoldDB; O84645; -.
DR SMR; O84645; -.
DR STRING; 813.O172_03505; -.
DR EnsemblBacteria; AAC68243; AAC68243; CT_639.
DR GeneID; 884422; -.
DR KEGG; ctr:CT_639; -.
DR PATRIC; fig|272561.5.peg.700; -.
DR HOGENOM; CLU_001114_6_3_0; -.
DR InParanoid; O84645; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0000725; P:recombinational repair; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
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; 2.
DR PANTHER; PTHR11070:SF23; PTHR11070:SF23; 2.
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.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1026
FT /note="RecBCD enzyme subunit RecB"
FT /id="PRO_0000102045"
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..773
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"
SQ SEQUENCE 1026 AA; 117829 MW; 63000D548C0F7A33 CRC64;
MSSFDIFSPT ASVSGKFFLE ASAGTGKTFT IEQVVLRSLL EGSIEQTKNI LVVTFTNAAT
NELKLRIQAS LKQALSLFSQ ALSHPGTPLP PYISSSETKV KQLYMKIRNS LATLDEMNIF
TIHGFCRFTL EQHFPWIQPI QPSSIFSEPQ TIQQHILDYL RKNLWDTVLS PKQYAFLSYH
HRATTQQTRH LIERLLQDYT STPNLALSPL SITLQKLKAW VSRYQHLAPL SLEEMQAFSL
RFKQSDLSIE RELPAFVQQF ETNPYSLDML FFPGMVQKFQ EENRNKKKLS APASPLDPFF
QDWIQLAHPF CQKEPIFHTL LKSVQQHLKT HCAQSYSHDE SIATLESLLA HNDTVVSQLR
KQFQLVLIDE FQDTDKRQWQ IFSKLFASPD YSGSLFLIGD PKQSIYEWRN ADLPTYLQAK
HSFPKEAQLI LDTNYRSTPE LMQALNHLFS LPTPFLETPQ NILYHPLHSK GSAEISYSEF
SPIHFFSSED IQEETLWISK TASYLRSAYS IPFGNMAVLV QDYPQALKLI THSTIPMAYC
KEKRIFDRTE SPYLLILLLE ALLYPENQQK IQAILMSRLF QLSSTEIHQH LKTFSSLFFT
LNRHLYHYSL LATFYKLMGE NVLSQTIGET LLQTPLGDII FQELEALCLY LDKTTENPHH
KLLHLINILI TGKYDEELSF SSQSNDENMI KITTVHSSKG LEYDVVFCSC LNKAKEKTPS
VHMREMYVAC TRAKKFLFIP FSPIEKRSLS TKKLSALANY ANVTKHHSVP HLVETLTSSS
PELFSSSFQP PESSLTPDRE RLPQQTYFSL PHLPSRTIHS FSSTVENLHF SEPIQELSPS
LLFPGGSLTG TLIHKLLESL AGNFAACFEE IFNKAQTLLK NTPLEGYESI IAEKICTVFS
TTLPFSSGSF ALRNVHPHNI RAEETFLLQE EGELWQGIVD LFFEHKDRFF IIDWKTSFLG
DETSCYSPDQ LHLYIQRQGL DRQERLYRKA AKRFLHQFNS LLQVEMAFVF IRGLDDKGNG
FLQPGR
