RECB_ECOLI
ID RECB_ECOLI Reviewed; 1180 AA.
AC P08394; Q2MA17;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 188.
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=Exodeoxyribonuclease V 135 kDa polypeptide;
DE AltName: Full=Exodeoxyribonuclease V beta chain;
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}; Synonyms=ior, rorA;
GN OrderedLocusNames=b2820, JW2788;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3537960; DOI=10.1093/nar/14.21.8573;
RA Finch P.W., Storey A., Chapman K.E., Brown K., Hickson I.D., Emmerson P.T.;
RT "Complete nucleotide sequence of the Escherichia coli recB gene.";
RL Nucleic Acids Res. 14:8573-8582(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN RECA LOADING, AND
RP MUTAGENESIS OF THR-807.
RC STRAIN=V1000;
RX PubMed=10766864; DOI=10.1074/jbc.275.16.12261;
RA Arnold D.A., Kowalczykowski S.C.;
RT "Facilitated loading of RecA protein is essential to recombination by
RT RecBCD enzyme.";
RL J. Biol. Chem. 275:12261-12265(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RX PubMed=3534791; DOI=10.1093/nar/14.19.7695;
RA Finch P.W., Wilson R.E., Brown K., Hickson I.D., Emmerson P.T.;
RT "Complete nucleotide sequence of the Escherichia coli ptr gene encoding
RT protease III.";
RL Nucleic Acids Res. 14:7695-7703(1986).
RN [6]
RP PROTEIN SEQUENCE OF 2-11, FUNCTION AS AN EXONUCLEASE; HELICASE AND ATPASE,
RP AND SUBUNIT.
RX PubMed=1618858; DOI=10.1016/s0021-9258(18)42249-1;
RA Masterson C., Boehmer P.E., McDonald F., Chaudhuri S., Hickson I.D.,
RA Emmerson P.T.;
RT "Reconstitution of the activities of the RecBCD holoenzyme of Escherichia
RT coli from the purified subunits.";
RL J. Biol. Chem. 267:13564-13572(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1093-1180.
RX PubMed=3537961; DOI=10.1093/nar/14.21.8583;
RA Finch P.W., Storey A., Brown K., Hickson I.D., Emmerson P.T.;
RT "Complete nucleotide sequence of recD, the structural gene for the alpha
RT subunit of Exonuclease V of Escherichia coli.";
RL Nucleic Acids Res. 14:8583-8594(1986).
RN [8]
RP FUNCTION IN DEGRADATION OF LAMBDA VIRUS DNA, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=4562392; DOI=10.1128/jb.112.1.161-169.1972;
RA Simmon V.F., Lederberg S.;
RT "Degradation of bacteriophage lambda deoxyribonucleic acid after
RT restriction by Escherichia coli K-12.";
RL J. Bacteriol. 112:161-169(1972).
RN [9]
RP FUNCTION AS AN ENDO- AND EXODEOXYRIBONUCLEASE, ATP-DEPENDENCE, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=4552016; DOI=10.1016/s0021-9258(19)45550-6;
RA Goldmark P.J., Linn S.;
RT "Purification and properties of the recBC DNase of Escherichia coli K-12.";
RL J. Biol. Chem. 247:1849-1860(1972).
RN [10]
RP FUNCTION, SUBSTRATES, AND PROCESSIVITY.
RX PubMed=4268693; DOI=10.1016/s0021-9258(19)43644-2;
RA Karu A.E., MacKay V., Goldmark P.J., Linn S.;
RT "The recBC deoxyribonuclease of Escherichia coli K-12. Substrate
RT specificity and reaction intermediates.";
RL J. Biol. Chem. 248:4874-4884(1973).
RN [11]
RP ACTIVITY REGULATION BY LAMBDA GAM PROTEIN (MICROBIAL INFECTION).
RX PubMed=4275917; DOI=10.1073/pnas.70.8.2215;
RA Sakaki Y., Karu A.E., Linn S., Echols H.;
RT "Purification and properties of the gamma-protein specified by
RT bacteriophage lambda: an inhibitor of the host RecBC recombination
RT enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 70:2215-2219(1973).
RN [12]
RP FUNCTION IN DEGRADATION OF VIRUS DNA, AND DISRUPTION PHENOTYPE.
RX PubMed=123277; DOI=10.1128/jvi.15.4.861-871.1975;
RA Benzinger R., Enquist L.W., Skalka A.;
RT "Transfection of Escherichia coli spheroplasts. V. Activity of recBC
RT nuclease in rec+ and rec minus spheroplasts measured with different forms
RT of bacteriophage DNA.";
RL J. Virol. 15:861-871(1975).
RN [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=6389498; DOI=10.1128/jb.160.2.788-791.1984;
RA Chaudhury A.M., Smith G.R.;
RT "Escherichia coli recBC deletion mutants.";
RL J. Bacteriol. 160:788-791(1984).
RN [14]
RP OPERON, AND SUBUNIT.
RX PubMed=3526335; DOI=10.1073/pnas.83.15.5558;
RA Amundsen S.K., Taylor A.F., Chaudhury A.M., Smith G.R.;
RT "recD: the gene for an essential third subunit of exonuclease V.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5558-5562(1986).
RN [15]
RP ACTIVITY REGULATION BY LAMBDA GAM PROTEIN (MICROBIAL INFECTION), AND
RP INTERACTION WITH LAMBDA GAMS (MICROBIAL INFECTION).
RX PubMed=1653221; DOI=10.1128/jb.173.18.5808-5821.1991;
RA Murphy K.C.;
RT "Lambda Gam protein inhibits the helicase and chi-stimulated recombination
RT activities of Escherichia coli RecBCD enzyme.";
RL J. Bacteriol. 173:5808-5821(1991).
RN [16]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=1535156; DOI=10.1073/pnas.89.12.5226;
RA Taylor A.F., Smith G.R.;
RT "RecBCD enzyme is altered upon cutting DNA at a chi recombination
RT hotspot.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5226-5230(1992).
RN [17]
RP FUNCTION IN HOMOLOGOUS RECOMBINATION.
RX PubMed=7608206; DOI=10.1074/jbc.270.27.16360;
RA Dixon D.A., Kowalczykowski S.C.;
RT "Role of the Escherichia coli recombination hotspot, chi, in RecABCD-
RT dependent homologous pairing.";
RL J. Biol. Chem. 270:16360-16370(1995).
RN [18]
RP FUNCTION IN RECA-LOADING.
RX PubMed=9230304; DOI=10.1016/s0092-8674(00)80315-3;
RA Anderson D.G., Kowalczykowski S.C.;
RT "The translocating RecBCD enzyme stimulates recombination by directing RecA
RT protein onto ssDNA in a chi-regulated manner.";
RL Cell 90:77-86(1997).
RN [19]
RP FUNCTION IN RECOGNITION OF CHI.
RX PubMed=9192629; DOI=10.1073/pnas.94.13.6706;
RA Bianco P.R., Kowalczykowski S.C.;
RT "The recombination hotspot Chi is recognized by the translocating RecBCD
RT enzyme as the single strand of DNA containing the sequence 5'-GCTGGTGG-
RT 3'.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6706-6711(1997).
RN [20]
RP FUNCTION, ACTIVE SITE, DOMAIN, AND MUTAGENESIS OF ASP-1080.
RX PubMed=9790841; DOI=10.1006/jmbi.1998.2127;
RA Yu M., Souaya J., Julin D.A.;
RT "Identification of the nuclease active site in the multifunctional RecBCD
RT enzyme by creation of a chimeric enzyme.";
RL J. Mol. Biol. 283:797-808(1998).
RN [21]
RP FUNCTION, INTERACTION WITH RECC, DOMAIN, AND DNA-BINDING.
RX PubMed=9448271; DOI=10.1073/pnas.95.3.981;
RA Yu M., Souaya J., Julin D.A.;
RT "The 30-kDa C-terminal domain of the RecB protein is critical for the
RT nuclease activity, but not the helicase activity, of the RecBCD enzyme from
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:981-986(1998).
RN [22]
RP FUNCTION, ACTIVE SITE, DOMAIN, AND MUTAGENESIS OF ASP-1080.
RX PubMed=10518611; DOI=10.1093/nar/27.21.4200;
RA Zhang X.J., Julin D.A.;
RT "Isolation and characterization of the C-terminal nuclease domain from the
RT RecB protein of Escherichia coli.";
RL Nucleic Acids Res. 27:4200-4207(1999).
RN [23]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=10197988; DOI=10.1101/gad.13.7.890;
RA Taylor A.F., Smith G.R.;
RT "Regulation of homologous recombination: Chi inactivates RecBCD enzyme by
RT disassembly of the three subunits.";
RL Genes Dev. 13:890-900(1999).
RN [24]
RP FUNCTION AS A SLOW 3'-5' HELICASE, AND MUTAGENESIS OF LYS-29.
RX PubMed=12815437; DOI=10.1038/nature01674;
RA Taylor A.F., Smith G.R.;
RT "RecBCD enzyme is a DNA helicase with fast and slow motors of opposite
RT polarity.";
RL Nature 423:889-893(2003).
RN [25]
RP FUNCTION AS A BIPOLAR HELICASE.
RX PubMed=12815438; DOI=10.1038/nature01673;
RA Dillingham M.S., Spies M., Kowalczykowski S.C.;
RT "RecBCD enzyme is a bipolar DNA helicase.";
RL Nature 423:893-897(2003).
RN [26]
RP FUNCTION, RATE, DNA-BINDING, AND MUTAGENESIS OF LYS-29.
RX PubMed=16041061; DOI=10.1074/jbc.m505520200;
RA Dillingham M.S., Webb M.R., Kowalczykowski S.C.;
RT "Bipolar DNA translocation contributes to highly processive DNA unwinding
RT by RecBCD enzyme.";
RL J. Biol. Chem. 280:37069-37077(2005).
RN [27]
RP FUNCTION AS A NUCLEASE, COFACTOR, AND MUTAGENESIS OF ASP-1067 AND ASP-1080.
RX PubMed=16388588; DOI=10.1021/bi051150v;
RA Sun J.Z., Julin D.A., Hu J.S.;
RT "The nuclease domain of the Escherichia coli RecBCD enzyme catalyzes
RT degradation of linear and circular single-stranded and double-stranded
RT DNA.";
RL Biochemistry 45:131-140(2006).
RN [28]
RP INTERACTION WITH RECA, SUBUNIT, AND DOMAIN.
RX PubMed=16483938; DOI=10.1016/j.molcel.2006.01.007;
RA Spies M., Kowalczykowski S.C.;
RT "The RecA binding locus of RecBCD is a general domain for recruitment of
RT DNA strand exchange proteins.";
RL Mol. Cell 21:573-580(2006).
RN [29]
RP FUNCTION, AND MUTAGENESIS OF TYR-803 AND VAL-804.
RX PubMed=18079176; DOI=10.1101/gad.1605807;
RA Amundsen S.K., Taylor A.F., Reddy M., Smith G.R.;
RT "Intersubunit signaling in RecBCD enzyme, a complex protein machine
RT regulated by Chi hot spots.";
RL Genes Dev. 21:3296-3307(2007).
RN [30]
RP FUNCTION IN DUAL DIRECTION TRANSLOCATION.
RX PubMed=20852646; DOI=10.1038/nsmb.1901;
RA Wu C.G., Bradford C., Lohman T.M.;
RT "Escherichia coli RecBC helicase has two translocase activities controlled
RT by a single ATPase motor.";
RL Nat. Struct. Mol. Biol. 17:1210-1217(2010).
RN [31]
RP INTERACTION WITH CAS1.
RC STRAIN=K12;
RX PubMed=21219465; DOI=10.1111/j.1365-2958.2010.07465.x;
RA Babu M., Beloglazova N., Flick R., Graham C., Skarina T., Nocek B.,
RA Gagarinova A., Pogoutse O., Brown G., Binkowski A., Phanse S.,
RA Joachimiak A., Koonin E.V., Savchenko A., Emili A., Greenblatt J.,
RA Edwards A.M., Yakunin A.F.;
RT "A dual function of the CRISPR-Cas system in bacterial antivirus immunity
RT and DNA repair.";
RL Mol. Microbiol. 79:484-502(2011).
RN [32]
RP FUNCTION, ENZYME RATE, ENZYME STATE SWITCHING, AND MUTAGENESIS OF LYS-29.
RX PubMed=23851395; DOI=10.1038/nature12333;
RA Liu B., Baskin R.J., Kowalczykowski S.C.;
RT "DNA unwinding heterogeneity by RecBCD results from static molecules able
RT to equilibrate.";
RL Nature 500:482-485(2013).
RN [33]
RP FUNCTION, AND MODEL OF DOMAIN MOVEMENT.
RX PubMed=25073102; DOI=10.1016/j.jmb.2014.07.017;
RA Taylor A.F., Amundsen S.K., Guttman M., Lee K.K., Luo J., Ranish J.,
RA Smith G.R.;
RT "Control of RecBCD enzyme activity by DNA binding- and Chi hotspot-
RT dependent conformational changes.";
RL J. Mol. Biol. 426:3479-3499(2014).
RN [34]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25141;
RX PubMed=33157039; DOI=10.1016/j.cell.2020.09.065;
RA Millman A., Bernheim A., Stokar-Avihail A., Fedorenko T., Voichek M.,
RA Leavitt A., Oppenheimer-Shaanan Y., Sorek R.;
RT "Bacterial Retrons Function In Anti-Phage Defense.";
RL Cell 183:1551-1561(2020).
RN [35] {ECO:0007744|PDB:1W36}
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH DNA, COFACTOR, AND
RP SUBUNIT.
RX PubMed=15538360; DOI=10.1038/nature02988;
RA Singleton M.R., Dillingham M.S., Gaudier M., Kowalczykowski S.C.,
RA Wigley D.B.;
RT "Crystal structure of RecBCD enzyme reveals a machine for processing DNA
RT breaks.";
RL Nature 432:187-193(2004).
RN [36] {ECO:0007744|PDB:3K70}
RP X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) IN COMPLEX WITH DNA, COFACTOR, AND
RP SUBUNIT.
RX PubMed=18668125; DOI=10.1038/emboj.2008.144;
RA Saikrishnan K., Griffiths S.P., Cook N., Court R., Wigley D.B.;
RT "DNA binding to RecD: role of the 1B domain in SF1B helicase activity.";
RL EMBO J. 27:2222-2229(2008).
RN [37] {ECO:0007744|PDB:5LD2}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.83 ANGSTROMS) OF RECBCD IN COMPLEX WITH
RP FORKED DNA SUBSTRATE, MUTAGENESIS OF ASP-1080, AND DNA-BINDING.
RX PubMed=27644322; DOI=10.7554/elife.18227;
RA Wilkinson M., Chaban Y., Wigley D.B.;
RT "Mechanism for nuclease regulation in RecBCD.";
RL Elife 5:0-0(2016).
RN [38] {ECO:0007744|PDB:5MBV}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF RECBCD IN COMPLEX WITH
RP LAMBDA GAMS PROTEIN.
RX PubMed=28009252; DOI=10.7554/elife.22963;
RA Wilkinson M., Troman L., Wan Nur Ismah W.A., Chaban Y., Avison M.B.,
RA Dillingham M.S., Wigley D.B.;
RT "Structural basis for the inhibition of RecBCD by Gam and its synergistic
RT antibacterial effect with quinolones.";
RL Elife 5:0-0(2016).
RN [39]
RP REVIEW.
RX PubMed=19052323; DOI=10.1128/mmbr.00020-08;
RA Dillingham M.S., Kowalczykowski S.C.;
RT "RecBCD enzyme and the repair of double-stranded DNA breaks.";
RL Microbiol. Mol. Biol. Rev. 72:642-671(2008).
RN [40]
RP REVIEW.
RX PubMed=22688812; DOI=10.1128/mmbr.05026-11;
RA Smith G.R.;
RT "How RecBCD enzyme and Chi promote DNA break repair and recombination: a
RT molecular biologist's view.";
RL Microbiol. Mol. Biol. Rev. 76:217-228(2012).
CC -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
CC recombinational DNA repair. Binds to DSBs and unwinds DNA via a rapid
CC (>1 kb/second) and highly processive (>30 kb) ATP-dependent
CC bidirectional helicase. Unwinds dsDNA until it encounters a Chi
CC (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence from the 3'
CC direction. Cuts ssDNA a few nucleotides 3' to Chi site, by nicking one
CC strand or switching the strand degraded (depending on the reaction
CC conditions). The properties and activities of the enzyme are changed at
CC Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang which
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 (PubMed:4562392, PubMed:4552016,
CC PubMed:123277). In the holoenzyme this subunit contributes ATPase, 3'-
CC 5' helicase, exonuclease activity and loads RecA onto ssDNA. The RecBC
CC complex requires the RecD subunit for nuclease activity, but can
CC translocate along ssDNA in both directions. Probably interacts with a
CC component of retron Ec48 which moniters RecBCD stability; when RecB is
CC missing or impaired the retron is activated and becomes toxic
CC (Probable). {ECO:0000269|PubMed:10197988, ECO:0000269|PubMed:10518611,
CC ECO:0000269|PubMed:10766864, ECO:0000269|PubMed:123277,
CC ECO:0000269|PubMed:12815437, ECO:0000269|PubMed:12815438,
CC ECO:0000269|PubMed:1535156, ECO:0000269|PubMed:16041061,
CC ECO:0000269|PubMed:1618858, ECO:0000269|PubMed:16388588,
CC ECO:0000269|PubMed:18079176, ECO:0000269|PubMed:20852646,
CC ECO:0000269|PubMed:23851395, ECO:0000269|PubMed:25073102,
CC ECO:0000269|PubMed:4268693, ECO:0000269|PubMed:4552016,
CC ECO:0000269|PubMed:4562392, ECO:0000269|PubMed:7608206,
CC ECO:0000269|PubMed:9192629, ECO:0000269|PubMed:9230304,
CC ECO:0000269|PubMed:9448271, ECO:0000269|PubMed:9790841,
CC ECO:0000305|PubMed:33157039}.
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 ECO:0000269|PubMed:15538360, ECO:0000269|PubMed:16388588,
CC ECO:0000269|PubMed:18668125};
CC Note=Magnesium is required for both helicase and nuclease activity; its
CC relative concentration alters helicase speed and nuclease activity in a
CC complicated fashion. {ECO:0000255|HAMAP-Rule:MF_01485,
CC ECO:0000269|PubMed:15538360, ECO:0000269|PubMed:16388588,
CC ECO:0000269|PubMed:18668125};
CC -!- ACTIVITY REGULATION: After reacting with DNA bearing a Chi site the
CC holoenzyme is disassembled and loses exonuclease activity, DNA
CC unwinding and Chi-directed DNA cleavage; RecB remains complexed with
CC ssDNA, which may prevent holoenzyme reassembly (PubMed:10197988). High
CC levels of Mg(2+) (13 mM MgCl(2+)) or incubation with DNase allow
CC holoenyzme reassembly, suggesting it is DNA bound to RecB that prevents
CC reassembly (PubMed:10197988). {ECO:0000269|PubMed:10197988,
CC ECO:0000269|PubMed:1535156}.
CC -!- ACTIVITY REGULATION: (Microbial infection) RecBCD is inhibited by the
CC lambda virus gam protein (both GamL and GamS isoforms); in vitro a
CC short preincubation prior to adding DNA results in maximal inhibition.
CC {ECO:0000269|PubMed:1653221, ECO:0000269|PubMed:4275917}.
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. The C-terminus interacts with RecA (PubMed:16483938).
CC Interacts with YgbT (Cas1) (PubMed:21219465).
CC {ECO:0000269|PubMed:15538360, ECO:0000269|PubMed:1618858,
CC ECO:0000269|PubMed:16483938, ECO:0000269|PubMed:18668125,
CC ECO:0000269|PubMed:21219465, ECO:0000269|PubMed:3526335,
CC ECO:0000269|PubMed:4552016, ECO:0000269|PubMed:9448271}.
CC -!- SUBUNIT: (Microbial infection) Lambda virus GamS protein interacts with
CC the enzyme without displacing any of the subunits.
CC {ECO:0000269|PubMed:1653221}.
CC -!- DOMAIN: The N-terminal DNA-binding domain (residues 1-929) is a ssDNA-
CC dependent ATPase and has ATP-dependent 3'-5' helicase function; both
CC are stimulated in the presence of RecC, suggesting this domain
CC interacts with RecC. Holoenzyme reconstituted with this RecB N-terminal
CC fragment has no nuclease activity (PubMed:9448271). The C-terminal
CC domain (residues 928-1180) has weak ssDNA endonuclease activity as an
CC isolated fragment (PubMed:9790841) (PubMed:10518611). RecD probably
CC interacts with this domain. The C-terminal domain interacts with RecA,
CC facilitating its loading onto ssDNA. Interaction is decreased by ATP
CC (PubMed:16483938). The RecB helicase domains change conformation upon
CC nucleotide binding. As ssDNA is unwound and fed to the RecD subunit the
CC latter transmits conformational changes through each subunit to
CC activate the RecB nuclease (PubMed:15538360).
CC {ECO:0000269|PubMed:10518611, ECO:0000269|PubMed:15538360,
CC ECO:0000269|PubMed:16483938, ECO:0000269|PubMed:9448271,
CC ECO:0000269|PubMed:9790841}.
CC -!- DOMAIN: The holoenzyme may undergo conformational shifts upon DNA
CC binding: the nuclease domain of RecB may swing away from the DNA exit
CC tunnel in RecC. When Chi DNA binds to the RecC tunnel, the nuclease
CC domain may then swing back to its original position (that seen in
CC crystal structures), allowing it to nick the DNA 3' of the Chi site and
CC then rotate to load RecA. At high Mg(2+) the nuclease domain may swing
CC back more frequently, explaining differences seen in assays performed
CC at high Mg(2+). {ECO:0000269|PubMed:25073102}.
CC -!- DISRUPTION PHENOTYPE: Decreased degradation of DNA with free ends that
CC is unable to undergo homologous recombination, which can fortuitously
CC lead to more efficient viral infection (PubMed:4562392, PubMed:123277).
CC Cells are deficient in DNA recombination repair and have increased
CC sensitivity to UV light. The cultures have many inviable cells
CC (PubMed:6389498). Cells cannot be transformed with retron Ec48-
CC containing plasmids (PubMed:33157039). {ECO:0000269|PubMed:123277,
CC ECO:0000269|PubMed:33157039, ECO:0000269|PubMed:4562392,
CC ECO:0000269|PubMed:6389498}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01485}.
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DR EMBL; X04581; CAA28250.1; -; Genomic_DNA.
DR EMBL; AF179304; AAD56369.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40467.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75859.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76889.1; -; Genomic_DNA.
DR EMBL; X06227; CAA29577.1; -; Genomic_DNA.
DR EMBL; X04582; CAA28252.1; -; Genomic_DNA.
DR PIR; A25532; NCECX5.
DR RefSeq; NP_417297.1; NC_000913.3.
DR RefSeq; WP_001285993.1; NZ_LN832404.1.
DR PDB; 1W36; X-ray; 3.10 A; B/E=1-1180.
DR PDB; 3K70; X-ray; 3.59 A; B/E=1-1180.
DR PDB; 5LD2; EM; 3.83 A; B=1-1180.
DR PDB; 5MBV; EM; 3.80 A; B=1-1180.
DR PDB; 6SJB; EM; 3.70 A; B=1-1180.
DR PDB; 6SJE; EM; 4.10 A; B=1-1180.
DR PDB; 6SJF; EM; 3.90 A; B=1-1180.
DR PDB; 6SJG; EM; 3.80 A; B=1-1180.
DR PDB; 6T2U; EM; 3.60 A; B=1-1180.
DR PDB; 6T2V; EM; 3.80 A; B=1-1180.
DR PDB; 7MR0; EM; 3.70 A; B=1-1180.
DR PDB; 7MR1; EM; 4.20 A; B=1-1180.
DR PDB; 7MR2; EM; 4.30 A; B=1-1180.
DR PDB; 7MR3; EM; 3.60 A; B=1-1180.
DR PDB; 7MR4; EM; 4.50 A; B=1-1180.
DR PDBsum; 1W36; -.
DR PDBsum; 3K70; -.
DR PDBsum; 5LD2; -.
DR PDBsum; 5MBV; -.
DR PDBsum; 6SJB; -.
DR PDBsum; 6SJE; -.
DR PDBsum; 6SJF; -.
DR PDBsum; 6SJG; -.
DR PDBsum; 6T2U; -.
DR PDBsum; 6T2V; -.
DR PDBsum; 7MR0; -.
DR PDBsum; 7MR1; -.
DR PDBsum; 7MR2; -.
DR PDBsum; 7MR3; -.
DR PDBsum; 7MR4; -.
DR AlphaFoldDB; P08394; -.
DR SMR; P08394; -.
DR BioGRID; 4262307; 585.
DR BioGRID; 851614; 3.
DR ComplexPortal; CPX-2197; Exodeoxyribonuclease V complex.
DR DIP; DIP-540N; -.
DR IntAct; P08394; 20.
DR MINT; P08394; -.
DR STRING; 511145.b2820; -.
DR ChEMBL; CHEMBL2095232; -.
DR jPOST; P08394; -.
DR PaxDb; P08394; -.
DR PRIDE; P08394; -.
DR EnsemblBacteria; AAC75859; AAC75859; b2820.
DR EnsemblBacteria; BAE76889; BAE76889; BAE76889.
DR GeneID; 947286; -.
DR KEGG; ecj:JW2788; -.
DR KEGG; eco:b2820; -.
DR PATRIC; fig|1411691.4.peg.3916; -.
DR EchoBASE; EB0817; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_6_0_6; -.
DR InParanoid; P08394; -.
DR OMA; KQSIYRW; -.
DR PhylomeDB; P08394; -.
DR BioCyc; EcoCyc:EG10824-MON; -.
DR BioCyc; MetaCyc:EG10824-MON; -.
DR BRENDA; 3.1.11.5; 2026.
DR EvolutionaryTrace; P08394; -.
DR PRO; PR:P08394; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IDA:EcoCyc.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IDA:EcoCyc.
DR GO; GO:0015616; F:DNA translocase activity; IDA:EcoCyc.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:EcoCyc.
DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044355; P:clearance of foreign intracellular DNA; IMP:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IDA:EcoCyc.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; TAS:EcoCyc.
DR GO; GO:0000725; P:recombinational repair; IDA:ComplexPortal.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
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; IPR038726; PDDEXK_AddAB-type.
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; PF12705; PDDEXK_1; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; DNA damage;
KW DNA repair; DNA-binding; Exonuclease; Helicase; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1618858"
FT CHAIN 2..1180
FT /note="RecBCD enzyme subunit RecB"
FT /id="PRO_0000102046"
FT DOMAIN 2..450
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT DOMAIN 480..746
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT DNA_BIND 252..254
FT DNA_BIND 511..512
FT DNA_BIND 560..561
FT DNA_BIND 761
FT REGION 2..927
FT /note="ATPase, DNA-binding and helicase activity, interacts
FT with RecC"
FT REGION 928..1180
FT /note="Nuclease activity, interacts with RecD and RecA"
FT ACT_SITE 1080
FT /note="For nuclease activity"
FT /evidence="ECO:0000269|PubMed:10518611,
FT ECO:0000269|PubMed:9790841"
FT BINDING 23..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15538360"
FT BINDING 447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15538360"
FT BINDING 956
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:15538360,
FT ECO:0000305|PubMed:18668125"
FT BINDING 1067
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:15538360,
FT ECO:0000305|PubMed:18668125"
FT BINDING 1080
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:15538360,
FT ECO:0000305|PubMed:18668125"
FT BINDING 1081
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:15538360,
FT ECO:0000305|PubMed:18668125"
FT MUTAGEN 29
FT /note="K->Q: Subunit loses ATPase and 3'-5' helicase
FT activity, holoenzyme has 3-5 fold less helicase activity,
FT 20-fold less processivity."
FT /evidence="ECO:0000269|PubMed:12815437,
FT ECO:0000269|PubMed:16041061, ECO:0000269|PubMed:23851395"
FT MUTAGEN 803
FT /note="Y->H: Large decrease in recombination, loss of Chi
FT hotspot activity, decreased RecB helicase rate, retains
FT nuclease activity but not Chi-sequence specificity, does
FT not load RecA."
FT /evidence="ECO:0000269|PubMed:18079176"
FT MUTAGEN 804
FT /note="V->E: Large decrease in recombination, loss of Chi
FT hotspot activity, decreased RecB helicase rate, retains
FT nuclease activity but not Chi-sequence specificity, does
FT not load RecA."
FT /evidence="ECO:0000269|PubMed:18079176"
FT MUTAGEN 807
FT /note="T->I: In recB-2109; absence of nuclease modification
FT at Chi sites."
FT /evidence="ECO:0000269|PubMed:10766864"
FT MUTAGEN 1067
FT /note="D->A: Subunit loses nuclease activity."
FT /evidence="ECO:0000269|PubMed:16388588"
FT MUTAGEN 1080
FT /note="D->A: Loss of holoenzyme nuclease activity, retains
FT full helicase activity, does not act at Chi, no loading of
FT RecA on ssDNA and no recombinational repair."
FT /evidence="ECO:0000269|PubMed:10518611,
FT ECO:0000269|PubMed:16388588, ECO:0000269|PubMed:27644322,
FT ECO:0000269|PubMed:9790841"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 66..88
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 157..172
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:1W36"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 218..234
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 312..316
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 324..346
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 351..363
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 367..377
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 391..401
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:1W36"
FT TURN 421..424
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 427..436
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 451..462
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 498..503
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 513..534
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 538..542
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 551..553
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 554..560
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 561..572
FT /evidence="ECO:0007829|PDB:1W36"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 587..589
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 592..603
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 609..617
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 625..633
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 635..655
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 657..667
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 670..676
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 677..679
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 680..698
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 704..716
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 732..734
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 735..740
FT /evidence="ECO:0007829|PDB:1W36"
FT TURN 741..744
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 749..754
FT /evidence="ECO:0007829|PDB:1W36"
FT TURN 755..758
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 767..769
FT /evidence="ECO:0007829|PDB:1W36"
FT TURN 771..773
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 776..781
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 784..806
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 809..817
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 832..835
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 837..842
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 850..859
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 865..869
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 901..906
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 908..910
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 917..920
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 942..944
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 949..958
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 964..966
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 970..979
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 984..986
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 987..998
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 1002..1006
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 1009..1011
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 1014..1016
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 1017..1027
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 1033..1043
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 1059..1074
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 1079..1082
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 1090..1092
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 1095..1104
FT /evidence="ECO:0007829|PDB:1W36"
FT TURN 1105..1107
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 1108..1125
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 1126..1128
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 1131..1134
FT /evidence="ECO:0007829|PDB:1W36"
FT STRAND 1139..1145
FT /evidence="ECO:0007829|PDB:1W36"
FT HELIX 1164..1173
FT /evidence="ECO:0007829|PDB:1W36"
SQ SEQUENCE 1180 AA; 133959 MW; F9AC331808E8F281 CRC64;
MSDVAETLDP LRLPLQGERL IEASAGTGKT FTIAALYLRL LLGLGGSAAF PRPLTVEELL
VVTFTEAATA ELRGRIRSNI HELRIACLRE TTDNPLYERL LEEIDDKAQA AQWLLLAERQ
MDEAAVFTIH GFCQRMLNLN AFESGMLFEQ QLIEDESLLR YQACADFWRR HCYPLPREIA
QVVFETWKGP QALLRDINRY LQGEAPVIKA PPPDDETLAS RHAQIVARID TVKQQWRDAV
GELDALIESS GIDRRKFNRS NQAKWIDKIS AWAEEETNSY QLPESLEKFS QRFLEDRTKA
GGETPRHPLF EAIDQLLAEP LSIRDLVITR ALAEIRETVA REKRRRGELG FDDMLSRLDS
ALRSESGEVL AAAIRTRFPV AMIDEFQDTD PQQYRIFRRI WHHQPETALL LIGDPKQAIY
AFRGADIFTY MKARSEVHAH YTLDTNWRSA PGMVNSVNKL FSQTDDAFMF REIPFIPVKS
AGKNQALRFV FKGETQPAMK MWLMEGESCG VGDYQSTMAQ VCAAQIRDWL QAGQRGEALL
MNGDDARPVR ASDISVLVRS RQEAAQVRDA LTLLEIPSVY LSNRDSVFET LEAQEMLWLL
QAVMTPEREN TLRSALATSM MGLNALDIET LNNDEHAWDV VVEEFDGYRQ IWRKRGVMPM
LRALMSARNI AENLLATAGG ERRLTDILHI SELLQEAGTQ LESEHALVRW LSQHILEPDS
NASSQQMRLE SDKHLVQIVT IHKSKGLEYP LVWLPFITNF RVQEQAFYHD RHSFEAVLDL
NAAPESVDLA EAERLAEDLR LLYVALTRSV WHCSLGVAPL VRRRGDKKGD TDVHQSALGR
LLQKGEPQDA AGLRTCIEAL CDDDIAWQTA QTGDNQPWQV NDVSTAELNA KTLQRLPGDN
WRVTSYSGLQ QRGHGIAQDL MPRLDVDAAG VASVVEEPTL TPHQFPRGAS PGTFLHSLFE
DLDFTQPVDP NWVREKLELG GFESQWEPVL TEWITAVLQA PLNETGVSLS QLSARNKQVE
MEFYLPISEP LIASQLDTLI RQFDPLSAGC PPLEFMQVRG MLKGFIDLVF RHEGRYYLLD
YKSNWLGEDS SAYTQQAMAA AMQAHRYDLQ YQLYTLALHR YLRHRIADYD YEHHFGGVIY
LFLRGVDKEH PQQGIYTTRP NAGLIALMDE MFAGMTLEEA
