DPO3B_ECOLI
ID DPO3B_ECOLI Reviewed; 366 AA.
AC P0A988; P00583; Q2M813;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Beta sliding clamp {ECO:0000303|PubMed:2040637};
DE Short=Beta clamp;
DE Short=Sliding clamp;
DE AltName: Full=Beta-clamp processivity factor;
DE AltName: Full=DNA polymerase III beta sliding clamp subunit;
GN Name=dnaN; OrderedLocusNames=b3701, JW3678;
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=6234204; DOI=10.1016/0378-1119(84)90253-1;
RA Ohmori H., Kimura M., Nagata T., Sakakibara Y.;
RT "Structural analysis of the dnaA and dnaN genes of Escherichia coli.";
RL Gene 28:159-170(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
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 1-14.
RX PubMed=2841344; DOI=10.1016/s0021-9258(18)37899-2;
RA Armengod M.E.E., Garcca-Sogo M., Lambies E.;
RT "Transcriptional organization of the dnaN and recF genes of Escherichia
RT coli K-12.";
RL J. Biol. Chem. 263:12109-12114(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-170.
RX PubMed=3527871; DOI=10.1016/0378-1119(86)90206-4;
RA Armengod M.E.E., Lambies E.;
RT "Overlapping arrangement of the recF and dnaN operons of Escherichia coli;
RT positive and negative control sequences.";
RL Gene 43:183-196(1986).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 297-366.
RX PubMed=6379647; DOI=10.1073/pnas.81.15.4622;
RA Blanar M.A., Sandler S.J., Armengod M.-E., Ream L.W., Clark A.J.;
RT "Molecular analysis of the recF gene of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4622-4626(1984).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 342-366.
RX PubMed=6089112; DOI=10.1093/nar/12.16.6389;
RA Adachi T., Mizuuchi K., Menzel R., Gellert M.;
RT "DNA sequence and transcription of the region upstream of the E. coli gyrB
RT gene.";
RL Nucleic Acids Res. 12:6389-6395(1984).
RN [9]
RP FUNCTION AS PROCESSIVITY FACTOR.
RX PubMed=3519609; DOI=10.1016/s0021-9258(17)38427-2;
RA LaDuca R.J., Crute J.J., McHenry C.S., Bambara R.A.;
RT "The beta subunit of the Escherichia coli DNA polymerase III holoenzyme
RT interacts functionally with the catalytic core in the absence of other
RT subunits.";
RL J. Biol. Chem. 261:7550-7557(1986).
RN [10]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [11]
RP FUNCTION WITH DNA POLYMERASE II (POLB), AND SUBUNIT.
RX PubMed=1999435; DOI=10.1016/s0021-9258(20)64360-5;
RA Hughes A.J. Jr., Bryan S.K., Chen H., Moses R.E., McHenry C.S.;
RT "Escherichia coli DNA polymerase II is stimulated by DNA polymerase III
RT holoenzyme auxiliary subunits.";
RL J. Biol. Chem. 266:4568-4573(1991).
RN [12]
RP FUNCTION AS A TETHER, SUBUNIT, AND INTERACTION WITH DNAE.
RX PubMed=2040637; DOI=10.1016/s0021-9258(18)99166-0;
RA Stukenberg P.T., Studwell-Vaughan P.S., O'Donnell M.;
RT "Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme.";
RL J. Biol. Chem. 266:11328-11334(1991).
RN [13]
RP FUNCTION WITH DNA POLYMERASE II (POLB), AND SUBUNIT.
RX PubMed=1534562; DOI=10.1016/s0021-9258(19)49928-6;
RA Bonner C.A., Stukenberg P.T., Rajagopalan M., Eritja R., O'Donnell M.,
RA McEntee K., Echols H., Goodman M.F.;
RT "Processive DNA synthesis by DNA polymerase II mediated by DNA polymerase
RT III accessory proteins.";
RL J. Biol. Chem. 267:11431-11438(1992).
RN [14]
RP IDENTIFICATION OF ISOFORM BETA*, FUNCTION, AND INDUCTION BY UV.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8576210; DOI=10.1074/jbc.271.5.2482;
RA Skaliter R., Paz-Elizur T., Livneh Z.;
RT "A smaller form of the sliding clamp subunit of DNA polymerase III is
RT induced by UV irradiation in Escherichia coli.";
RL J. Biol. Chem. 271:2478-2481(1996).
RN [15]
RP ALTERNATIVE PROMOTER USAGE (ISOFORMS BETA AND BETA*), INDUCTION BY
RP NALIDIXIC ACID, AND MUTAGENESIS OF ALA-133; MET-135 AND MET-146.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8576211; DOI=10.1074/jbc.271.5.2478;
RA Paz-Elizur T., Skaliter R., Blumenstein S., Livneh Z.;
RT "Beta*, a UV-inducible smaller form of the beta subunit sliding clamp of
RT DNA polymerase III of Escherichia coli. I. Gene expression and
RT regulation.";
RL J. Biol. Chem. 271:2482-2490(1996).
RN [16]
RP CHARACTERIZATION OF BETA*, AND SUBUNIT.
RX PubMed=8576212; DOI=10.1074/jbc.271.5.2491;
RA Skaliter R., Bergstein M., Livneh Z.;
RT "Beta*, a UV-inducible shorter form of the beta subunit of DNA polymerase
RT III of Escherichia coli. II. Overproduction, purification, and activity as
RT a polymerase processivity clamp.";
RL J. Biol. Chem. 271:2491-2496(1996).
RN [17]
RP RING OPENING BY DELTA SUBUNIT (HOLA), AND SUBUNIT.
RX PubMed=9927437; DOI=10.1093/emboj/18.3.771;
RA Turner J., Hingorani M.M., Kelman Z., O'Donnell M.;
RT "The internal workings of a DNA polymerase clamp-loading machine.";
RL EMBO J. 18:771-783(1999).
RN [18]
RP FUNCTION WITH DNA POLYMERASES IV (DINB) AND V (UMUCD).
RX PubMed=10801133; DOI=10.1038/35010020;
RA Tang M., Pham P., Shen X., Taylor J.S., O'Donnell M., Woodgate R.,
RA Goodman M.F.;
RT "Roles of E. coli DNA polymerases IV and V in lesion-targeted and
RT untargeted SOS mutagenesis.";
RL Nature 404:1014-1018(2000).
RN [19]
RP INTERACTION WITH MUTS; LIGASE AND POLA.
RX PubMed=11459978; DOI=10.1073/pnas.121009498;
RA Lopez de Saro F.J., O'Donnell M.;
RT "Interaction of the beta sliding clamp with MutS, ligase, and DNA
RT polymerase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8376-8380(2001).
RN [20]
RP INTERACTION WITH DINB; DNAE; HOLA; MUTS; POLB AND UMUC.
RC STRAIN=K12 / XL1-Blue;
RX PubMed=11573000; DOI=10.1073/pnas.191384398;
RA Dalrymple B.P., Kongsuwan K., Wijffels G., Dixon N.E., Jennings P.A.;
RT "A universal protein-protein interaction motif in the eubacterial DNA
RT replication and repair systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11627-11632(2001).
RN [21]
RP CONSENSUS SEQUENCE FOR BINDING TO THE SLIDING CLAMP.
RX PubMed=15134440; DOI=10.1021/bi036229j;
RA Wijffels G., Dalrymple B.P., Prosselkov P., Kongsuwan K., Epa V.C.,
RA Lilley P.E., Jergic S., Buchardt J., Brown S.E., Alewood P.F.,
RA Jennings P.A., Dixon N.E.;
RT "Inhibition of protein interactions with the beta(2) sliding clamp of
RT Escherichia coli DNA polymerase III by peptides from beta(2)-binding
RT proteins.";
RL Biochemistry 43:5661-5671(2004).
RN [22]
RP INTERACTION WITH HDA.
RX PubMed=15150238; DOI=10.1128/jb.186.11.3508-3515.2004;
RA Kurz M., Dalrymple B., Wijffels G., Kongsuwan K.;
RT "Interaction of the sliding clamp beta-subunit and Hda, a DnaA-related
RT protein.";
RL J. Bacteriol. 186:3508-3515(2004).
RN [23]
RP FUNCTION AT REPLICATION FORK, INTERACTION WITH DNAE, AND MUTAGENESIS OF
RP GLY-66 AND GLY-174.
RX PubMed=15466025; DOI=10.1128/jb.186.20.6738-6748.2004;
RA Sutton M.D.;
RT "The Escherichia coli dnaN159 mutant displays altered DNA polymerase usage
RT and chronic SOS induction.";
RL J. Bacteriol. 186:6738-6748(2004).
RN [24]
RP FUNCTION IN POLYMERASE CHOICE, SUBUNIT, AND MUTAGENESIS OF 272-ILE-LEU-273.
RX PubMed=16168375; DOI=10.1016/j.molcel.2005.08.011;
RA Indiani C., McInerney P., Georgescu R., Goodman M.F., O'Donnell M.;
RT "A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases
RT simultaneously.";
RL Mol. Cell 19:805-815(2005).
RN [25]
RP IDENTIFICATION IN RIDA COMPLEX.
RX PubMed=18977760; DOI=10.1074/jbc.m803158200;
RA Su'etsugu M., Nakamura K., Keyamura K., Kudo Y., Katayama T.;
RT "Hda monomerization by ADP binding promotes replicase clamp-mediated DnaA-
RT ATP hydrolysis.";
RL J. Biol. Chem. 283:36118-36131(2008).
RN [26]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [27]
RP REPLISOME COMPLEX, AND SUBUNIT.
RX PubMed=20413500; DOI=10.1126/science.1185757;
RA Reyes-Lamothe R., Sherratt D.J., Leake M.C.;
RT "Stoichiometry and architecture of active DNA replication machinery in
RT Escherichia coli.";
RL Science 328:498-501(2010).
RN [28]
RP REPLISOME COMPLEX, AND SUBUNIT.
RX PubMed=22157955; DOI=10.1038/nsmb.2179;
RA Georgescu R.E., Kurth I., O'Donnell M.E.;
RT "Single-molecule studies reveal the function of a third polymerase in the
RT replisome.";
RL Nat. Struct. Mol. Biol. 19:113-116(2011).
RN [29]
RP FUNCTION IN REPLICATION FORK, AND SUBUNIT.
RX PubMed=22716942; DOI=10.1111/j.1365-2958.2012.08129.x;
RA Baxter J.C., Sutton M.D.;
RT "Evidence for roles of the Escherichia coli Hda protein beyond regulatory
RT inactivation of DnaA.";
RL Mol. Microbiol. 85:648-668(2012).
RN [30]
RP INTERACTION WITH CRFC, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=23994470; DOI=10.1016/j.celrep.2013.07.040;
RA Ozaki S., Matsuda Y., Keyamura K., Kawakami H., Noguchi Y., Kasho K.,
RA Nagata K., Masuda T., Sakiyama Y., Katayama T.;
RT "A replicase clamp-binding dynamin-like protein promotes colocalization of
RT nascent DNA strands and equipartitioning of chromosomes in E. coli.";
RL Cell Rep. 4:985-995(2013).
RN [31] {ECO:0007744|PDB:2POL}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1349852; DOI=10.1016/0092-8674(92)90445-i;
RA Kong X.-P., Onrust R., O'Donnell M., Kuriyan J.;
RT "Three-dimensional structure of the beta subunit of E. coli DNA polymerase
RT III holoenzyme: a sliding DNA clamp.";
RL Cell 69:425-437(1992).
RN [32] {ECO:0007744|PDB:1JQJ, ECO:0007744|PDB:1JQL}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH DELTA SUBUNIT
RP (HOLA), PROBABLE MECHANISM OF CLAMP OPENING, AND MUTAGENESIS OF
RP 272-ILE-LEU-273.
RX PubMed=11525728; DOI=10.1016/s0092-8674(01)00462-7;
RA Jeruzalmi D., Yurieva O., Zhao Y., Young M., Stewart J., Hingorani M.,
RA O'Donnell M., Kuriyan J.;
RT "Mechanism of processivity clamp opening by the delta subunit wrench of the
RT clamp loader complex of E. coli DNA polymerase III.";
RL Cell 106:417-428(2001).
RN [33] {ECO:0007744|PDB:1MMI}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=12832762; DOI=10.1107/s0907444903009958;
RA Oakley A.J., Prosselkov P., Wijffels G., Beck J.L., Wilce M.C., Dixon N.E.;
RT "Flexibility revealed by the 1.85 A crystal structure of the beta sliding-
RT clamp subunit of Escherichia coli DNA polymerase III.";
RL Acta Crystallogr. D 59:1192-1199(2003).
RN [34] {ECO:0007744|PDB:1UNN}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH DINB, AND FUNCTION.
RX PubMed=14592985; DOI=10.1093/emboj/cdg568;
RA Bunting K.A., Roe S.M., Pearl L.H.;
RT "Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB
RT to the beta-clamp.";
RL EMBO J. 22:5883-5892(2003).
RN [35] {ECO:0007744|PDB:1OK7}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH PEPTIDE OF DINB,
RP FUNCTION, AND SUBUNIT.
RX PubMed=14729336; DOI=10.1016/j.jmb.2003.11.049;
RA Burnouf D.Y., Olieric V., Wagner J., Fujii S., Reinbolt J., Fuchs R.P.,
RA Dumas P.;
RT "Structural and biochemical analysis of sliding clamp/ligand interactions
RT suggest a competition between replicative and translesion DNA
RT polymerases.";
RL J. Mol. Biol. 335:1187-1197(2004).
RN [36] {ECO:0007744|PDB:3BEP}
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH PRIMED DNA,
RP FUNCTION, SUBUNIT, DNA-BINDING, AND MUTAGENESIS OF ARG-24; GLN-149;
RP 153-TYR-TYR-154 AND 272-ILE-LEU-273.
RX PubMed=18191219; DOI=10.1016/j.cell.2007.11.045;
RA Georgescu R.E., Kim S.S., Yurieva O., Kuriyan J., Kong X.P., O'Donnell M.;
RT "Structure of a sliding clamp on DNA.";
RL Cell 132:43-54(2008).
RN [37] {ECO:0007744|PDB:3D1E, ECO:0007744|PDB:3D1F, ECO:0007744|PDB:3D1G}
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) IN COMPLEX WITH VARIOUS PEPTIDES,
RP SUBUNIT, AND BIOTECHNOLOGY.
RX PubMed=18678908; DOI=10.1073/pnas.0804754105;
RA Georgescu R.E., Yurieva O., Kim S.S., Kuriyan J., Kong X.P., O'Donnell M.;
RT "Structure of a small-molecule inhibitor of a DNA polymerase sliding
RT clamp.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:11116-11121(2008).
RN [38] {ECO:0007744|PDB:5FKU, ECO:0007744|PDB:5FKV, ECO:0007744|PDB:5FKW}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.30 ANGSTROMS) OF DNAE; DNAN; DNAQ; DNAX
RP WITH AND WITHOUT DNA, FUNCTION, SUBUNIT, AND DNA-BINDING.
RX PubMed=26499492; DOI=10.7554/elife.11134;
RA Fernandez-Leiro R., Conrad J., Scheres S.H., Lamers M.H.;
RT "cryo-EM structures of the E. coli replicative DNA polymerase reveal its
RT dynamic interactions with the DNA sliding clamp, exonuclease and tau.";
RL Elife 4:0-0(2015).
RN [39]
RP REVIEW.
RX PubMed=1575709; DOI=10.1002/bies.950140206;
RA O'Donnell M.;
RT "Accessory protein function in the DNA polymerase III holoenzyme from E.
RT coli.";
RL Bioessays 14:105-111(1992).
RN [40]
RP REVIEW.
RX PubMed=15952889; DOI=10.1146/annurev.biochem.73.011303.073859;
RA Johnson A., O'Donnell M.;
RT "Cellular DNA replicases: components and dynamics at the replication
RT fork.";
RL Annu. Rev. Biochem. 74:283-315(2005).
CC -!- FUNCTION: Confers DNA tethering and processivity to DNA polymerases and
CC other proteins. Acts as a clamp, forming a ring around DNA (a reaction
CC catalyzed by the clamp-loading complex) which diffuses in an ATP-
CC independent manner freely and bidirectionally along dsDNA
CC (PubMed:2040637). DNA bound in the ring is bent 22 degrees, in solution
CC primed DNA is bound more tightly than dsDNA, suggesting the clamp binds
CC both ss- and dsDNA (PubMed:18191219). In a complex of DNA with this
CC protein, alpha, epsilon and tau subunits however the DNA is only
CC slightly bent (PubMed:26499492). Coordinates protein traffic at the
CC replication fork, where it interacts with multiple DNA polymerases,
CC repair factors and other proteins (PubMed:15466025, PubMed:16168375,
CC PubMed:22716942, PubMed:14592985, PubMed:14729336, PubMed:26499492,
CC PubMed:15952889). Initially characterized for its ability to contact
CC the alpha subunit (dnaE) of DNA polymerase III (Pol III), tethering it
CC to the DNA and conferring very high processivity (PubMed:2040637). Pol
CC III is a complex, multichain enzyme responsible for most of the
CC replicative synthesis in bacteria; it also exhibits 3'-5' exonuclease
CC proofreading activity. The beta chain is required for initiation of
CC replication as well as for processivity of DNA replication
CC (PubMed:3519609, PubMed:2040637). A single clamp can bind both Pol III
CC and IV, allowing the repair Pol IV to access DNA when it is damaged and
CC needs to be fixed, a process the replicative polymerase cannot perform;
CC when DNA is repaired Pol III takes over again (PubMed:16168375). Serves
CC as a processivity factor for DNA polymerases II (PubMed:1999435,
CC PubMed:1534562), IV (PubMed:10801133) and V (PubMed:10801133). A
CC shorter protein beta* may be important for increasing survival after UV
CC irradiation, and stimulates DNA synthesis with increased processivity
CC in the presence of core Pol III plus the clamp loader complex
CC (PubMed:8576210, PubMed:8576212). {ECO:0000269|PubMed:10801133,
CC ECO:0000269|PubMed:14592985, ECO:0000269|PubMed:14729336,
CC ECO:0000269|PubMed:1534562, ECO:0000269|PubMed:15466025,
CC ECO:0000269|PubMed:16168375, ECO:0000269|PubMed:18191219,
CC ECO:0000269|PubMed:1999435, ECO:0000269|PubMed:2040637,
CC ECO:0000269|PubMed:22716942, ECO:0000269|PubMed:26499492,
CC ECO:0000269|PubMed:3519609, ECO:0000269|PubMed:8576210,
CC ECO:0000269|PubMed:8576212, ECO:0000305|PubMed:15952889}.
CC -!- SUBUNIT: Forms a ring-shaped head-to-tail homodimer (PubMed:2040637,
CC PubMed:9927437, PubMed:1349852, PubMed:12832762, PubMed:14592985,
CC PubMed:14729336, PubMed:18191219, PubMed:18678908) around DNA
CC (PubMed:18191219), which can be opened by the delta subunit
CC (PubMed:9927437, PubMed:11525728). Binds interacting factors in a
CC hydrophobic surface cleft between domains 2 and 3, each monomer is able
CC to bind different proteins simultaneously (PubMed:16168375,
CC PubMed:11525728, PubMed:14592985, PubMed:14729336, PubMed:26499492).
CC The beta* isoform probably forms homotrimers which probably load onto
CC DNA (PubMed:8576212). The DNA polymerase III holoenzyme complex
CC contains at least 10 different subunits organized into 3 functionally
CC essential subassemblies: the Pol III core, the beta sliding clamp
CC processivity factor and the clamp-loading complex. The Pol III core
CC (subunits alpha, epsilon and theta) contains the polymerase and the 3'-
CC 5' exonuclease proofreading activities. The polymerase is tethered to
CC the template via the dimeric beta sliding clamp processivity factor
CC (this entry) (PubMed:15466025). The clamp loader (also called gamma
CC complex) assembles the beta sliding clamp onto the primed template and
CC plays a central role in the organization and communication at the
CC replication fork. The clamp loader contains delta, delta', psi and chi,
CC and 3 copies of either or both of two different DnaX proteins, gamma
CC and tau. The DNA replisome complex has a single clamp loader (3 tau and
CC 1 each of delta, delta', psi and chi subunits) which binds 3 Pol III
CC cores (1 core on the leading strand and 2 on the lagging strand) each
CC with a beta sliding clamp dimer. Additional proteins in the replisome
CC are other copies of gamma, psi and chi, Ssb, DNA helicase and RNA
CC primase (PubMed:20413500, PubMed:22157955, PubMed:26499492). The beta
CC sliding clamp can also be part of the RIDA complex (regulatory
CC inactivation of DnaA), consisting of ATP-DnaA, ADP-Hda and DNA-loaded
CC beta clamp (PubMed:15150238, PubMed:18977760, PubMed:22716942). Also
CC interacts with a number of other DNA machines such as DNA polymerases I
CC (PubMed:11459978), II (PubMed:1999435, PubMed:1534562), IV
CC (PubMed:14729336) and V, DNA mismatch repair enzyme MutS
CC (PubMed:11459978, PubMed:11573000) and DNA ligase (PubMed:11459978).
CC Binds to CrfC homooligomers at the midcell position during DNA
CC replication (PubMed:23994470). Many proteins that bind the beta sliding
CC clamp have the consensus sequence Gln-Leu[Ser/Asp]Leu-Phe
CC (PubMed:15134440). {ECO:0000269|PubMed:11459978,
CC ECO:0000269|PubMed:11525728, ECO:0000269|PubMed:11573000,
CC ECO:0000269|PubMed:12832762, ECO:0000269|PubMed:1349852,
CC ECO:0000269|PubMed:14592985, ECO:0000269|PubMed:14729336,
CC ECO:0000269|PubMed:15134440, ECO:0000269|PubMed:15150238,
CC ECO:0000269|PubMed:1534562, ECO:0000269|PubMed:15466025,
CC ECO:0000269|PubMed:16168375, ECO:0000269|PubMed:18191219,
CC ECO:0000269|PubMed:18678908, ECO:0000269|PubMed:18977760,
CC ECO:0000269|PubMed:1999435, ECO:0000269|PubMed:2040637,
CC ECO:0000269|PubMed:20413500, ECO:0000269|PubMed:22157955,
CC ECO:0000269|PubMed:22716942, ECO:0000269|PubMed:23994470,
CC ECO:0000269|PubMed:26499492, ECO:0000269|PubMed:8576212,
CC ECO:0000269|PubMed:9927437}.
CC -!- INTERACTION:
CC P0A988; P77395: cnoX; NbExp=2; IntAct=EBI-542385, EBI-545297;
CC P0A988; Q47155: dinB; NbExp=2; IntAct=EBI-542385, EBI-1037359;
CC P0A988; P10443: dnaE; NbExp=19; IntAct=EBI-542385, EBI-549111;
CC P0A988; P0A988: dnaN; NbExp=9; IntAct=EBI-542385, EBI-542385;
CC P0A988; P03007: dnaQ; NbExp=6; IntAct=EBI-542385, EBI-549131;
CC P0A988; P06710: dnaX; NbExp=4; IntAct=EBI-542385, EBI-549140;
CC P0A988; P69931: hda; NbExp=9; IntAct=EBI-542385, EBI-545453;
CC P0A988; P28630: holA; NbExp=10; IntAct=EBI-542385, EBI-549153;
CC P0A988; P0AFX0: hpf; NbExp=2; IntAct=EBI-542385, EBI-561113;
CC P0A988; P0AG07: rpe; NbExp=4; IntAct=EBI-542385, EBI-546020;
CC P0A988; P0A8E7: yajQ; NbExp=2; IntAct=EBI-542385, EBI-370752;
CC P0A988; P0AC53: zwf; NbExp=2; IntAct=EBI-542385, EBI-555656;
CC P0A988; P05845: tnsE; Xeno; NbExp=4; IntAct=EBI-542385, EBI-2434514;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23994470}.
CC Note=Localizes to midcell position when chromosomes are condensed
CC during DNA replication (PubMed:23994470).
CC {ECO:0000269|PubMed:23994470}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=Beta {ECO:0000269|PubMed:8576211};
CC IsoId=P0A988-1; Sequence=Displayed;
CC Name=Beta* {ECO:0000269|PubMed:8576211};
CC IsoId=P0A988-2; Sequence=VSP_059030;
CC -!- INDUCTION: Induced 1.5-fold by hydroxyurea (PubMed:20005847). A shorter
CC isoform, beta* is induced by UV treatment and also at low levels in
CC late logarithmic/early stationary phase growth (at protein level)
CC (PubMed:8576210). Beta* transcription induced by naldixic acid
CC (PubMed:8576211). {ECO:0000269|PubMed:20005847,
CC ECO:0000269|PubMed:8576210, ECO:0000269|PubMed:8576211}.
CC -!- BIOTECHNOLOGY: Small molecules can bind to the hydrophobic cleft and
CC inhibit binding of various protein factors, suggesting this may make
CC and attractive antibiotic target (PubMed:18678908).
CC {ECO:0000269|PubMed:18678908}.
CC -!- MISCELLANEOUS: The temperature- and UV-sensitive allele dnaN159 does
CC not grow at temperatures higher than 37 degrees Celsius. The global SOS
CC response is chronically induced. The UV-sensitivity of dnaN159 is
CC dependent upon Pol IV (dinB), it has an enhanced Pol V-dependent
CC mutation rate (umuC, umuD), and is absolutely dependent on the
CC polymerase activity of Pol I (polA) for viability.
CC {ECO:0000269|PubMed:15466025}.
CC -!- MISCELLANEOUS: [Isoform Beta*]: Beta* protein is expressed in late
CC logarithmic/early stationary phase and induced by UV treatment
CC (PubMed:8576210). Mutations in the Shine-Dalgarno region of beta* (some
CC silent at the amino acid level) decrease production of beta*
CC (PubMed:8576211). {ECO:0000269|PubMed:8576210,
CC ECO:0000269|PubMed:8576211}.
CC -!- SIMILARITY: Belongs to the beta sliding clamp family. {ECO:0000305}.
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DR EMBL; J01602; AAB59150.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62052.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76724.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77593.1; -; Genomic_DNA.
DR EMBL; M19876; AAA23695.1; -; Genomic_DNA.
DR EMBL; M13822; AAA24512.1; -; Genomic_DNA.
DR EMBL; K02179; AAA24510.1; -; Genomic_DNA.
DR EMBL; X04341; CAA27869.1; -; Genomic_DNA.
DR PIR; A91510; DJEC3B.
DR RefSeq; NP_418156.1; NC_000913.3.
DR RefSeq; WP_000673464.1; NZ_STEB01000015.1.
DR PDB; 1JQJ; X-ray; 2.90 A; A/B=1-366.
DR PDB; 1JQL; X-ray; 2.50 A; A=1-366.
DR PDB; 1MMI; X-ray; 1.85 A; A/B=1-366.
DR PDB; 1OK7; X-ray; 1.65 A; A/B=1-366.
DR PDB; 1UNN; X-ray; 1.90 A; A/B=1-366.
DR PDB; 2POL; X-ray; 2.50 A; A/B=1-366.
DR PDB; 2XUR; X-ray; 1.90 A; A/B=1-366.
DR PDB; 3BEP; X-ray; 1.92 A; A/B=1-366.
DR PDB; 3D1E; X-ray; 1.90 A; A/B=1-366.
DR PDB; 3D1F; X-ray; 2.00 A; A/B=1-366.
DR PDB; 3D1G; X-ray; 1.64 A; A/B=1-366.
DR PDB; 3F1V; X-ray; 1.77 A; A/B=1-366.
DR PDB; 3PWE; X-ray; 2.20 A; A/B=1-366.
DR PDB; 3Q4J; X-ray; 2.30 A; A/B/C/D/E/F=1-366.
DR PDB; 3Q4K; X-ray; 2.60 A; A/B=1-366.
DR PDB; 3Q4L; X-ray; 1.95 A; A/B=1-366.
DR PDB; 3QSB; X-ray; 1.90 A; A/B=1-366.
DR PDB; 4K3K; X-ray; 1.85 A; A/B=1-366.
DR PDB; 4K3L; X-ray; 1.50 A; A/B=1-366.
DR PDB; 4K3M; X-ray; 1.85 A; A/B=1-366.
DR PDB; 4K3O; X-ray; 2.00 A; A/B=1-366.
DR PDB; 4K3P; X-ray; 2.15 A; A/B=1-366.
DR PDB; 4K3Q; X-ray; 1.85 A; A/B=1-366.
DR PDB; 4K3R; X-ray; 1.86 A; A/B=1-366.
DR PDB; 4K3S; X-ray; 1.75 A; A/B=1-366.
DR PDB; 4MJP; X-ray; 1.86 A; A/B=1-366.
DR PDB; 4MJQ; X-ray; 1.73 A; A/B=1-366.
DR PDB; 4MJR; X-ray; 1.62 A; A/B=1-366.
DR PDB; 4N94; X-ray; 1.73 A; A/B=1-366.
DR PDB; 4N95; X-ray; 1.80 A; A/B=1-366.
DR PDB; 4N96; X-ray; 1.70 A; A/B=1-366.
DR PDB; 4N97; X-ray; 1.97 A; A/B=1-366.
DR PDB; 4N98; X-ray; 1.70 A; A/B=1-366.
DR PDB; 4N99; X-ray; 2.30 A; A/B=1-366.
DR PDB; 4N9A; X-ray; 1.90 A; A/B=1-366.
DR PDB; 5FKU; EM; 8.34 A; B/C=1-366.
DR PDB; 5FKV; EM; 8.00 A; B/C=1-366.
DR PDB; 5FKW; EM; 7.30 A; B/C=1-366.
DR PDB; 5M1S; EM; 6.70 A; B/C=1-366.
DR PDB; 6E8E; X-ray; 2.25 A; A/B=1-366.
DR PDB; 6FVL; X-ray; 1.98 A; A/B/C/D=1-366.
DR PDB; 7AZ5; X-ray; 1.87 A; A/B/C/D=1-366.
DR PDB; 7AZ6; X-ray; 1.93 A; A=1-366.
DR PDB; 7AZ7; X-ray; 1.65 A; A=1-366.
DR PDB; 7AZ8; X-ray; 1.61 A; A/B=1-366.
DR PDB; 7AZC; X-ray; 1.77 A; A/B/C/D=1-366.
DR PDB; 7AZD; X-ray; 2.19 A; A/B/C/D=1-366.
DR PDB; 7AZE; X-ray; 1.82 A; A/B=1-366.
DR PDB; 7AZF; X-ray; 1.93 A; A/B/C/D=1-366.
DR PDB; 7AZG; X-ray; 2.92 A; A/B/C/D/E/F/G/H=1-366.
DR PDB; 7AZK; X-ray; 2.05 A; A/B/C/D=1-366.
DR PDB; 7AZL; X-ray; 2.42 A; A/B/C/D=1-366.
DR PDBsum; 1JQJ; -.
DR PDBsum; 1JQL; -.
DR PDBsum; 1MMI; -.
DR PDBsum; 1OK7; -.
DR PDBsum; 1UNN; -.
DR PDBsum; 2POL; -.
DR PDBsum; 2XUR; -.
DR PDBsum; 3BEP; -.
DR PDBsum; 3D1E; -.
DR PDBsum; 3D1F; -.
DR PDBsum; 3D1G; -.
DR PDBsum; 3F1V; -.
DR PDBsum; 3PWE; -.
DR PDBsum; 3Q4J; -.
DR PDBsum; 3Q4K; -.
DR PDBsum; 3Q4L; -.
DR PDBsum; 3QSB; -.
DR PDBsum; 4K3K; -.
DR PDBsum; 4K3L; -.
DR PDBsum; 4K3M; -.
DR PDBsum; 4K3O; -.
DR PDBsum; 4K3P; -.
DR PDBsum; 4K3Q; -.
DR PDBsum; 4K3R; -.
DR PDBsum; 4K3S; -.
DR PDBsum; 4MJP; -.
DR PDBsum; 4MJQ; -.
DR PDBsum; 4MJR; -.
DR PDBsum; 4N94; -.
DR PDBsum; 4N95; -.
DR PDBsum; 4N96; -.
DR PDBsum; 4N97; -.
DR PDBsum; 4N98; -.
DR PDBsum; 4N99; -.
DR PDBsum; 4N9A; -.
DR PDBsum; 5FKU; -.
DR PDBsum; 5FKV; -.
DR PDBsum; 5FKW; -.
DR PDBsum; 5M1S; -.
DR PDBsum; 6E8E; -.
DR PDBsum; 6FVL; -.
DR PDBsum; 7AZ5; -.
DR PDBsum; 7AZ6; -.
DR PDBsum; 7AZ7; -.
DR PDBsum; 7AZ8; -.
DR PDBsum; 7AZC; -.
DR PDBsum; 7AZD; -.
DR PDBsum; 7AZE; -.
DR PDBsum; 7AZF; -.
DR PDBsum; 7AZG; -.
DR PDBsum; 7AZK; -.
DR PDBsum; 7AZL; -.
DR AlphaFoldDB; P0A988; -.
DR SMR; P0A988; -.
DR BioGRID; 4259535; 183.
DR BioGRID; 852520; 8.
DR ComplexPortal; CPX-1927; DNA polymerase III, beta sliding clamp processivity factor complex.
DR ComplexPortal; CPX-1945; Regulatory inactivation of dnaA (RIDA) complex.
DR ComplexPortal; CPX-1954; hda-beta clamp complex.
DR DIP; DIP-36038N; -.
DR IntAct; P0A988; 39.
DR MINT; P0A988; -.
DR STRING; 511145.b3701; -.
DR BindingDB; P0A988; -.
DR ChEMBL; CHEMBL3562169; -.
DR DrugBank; DB06998; [(5R)-5-(2,3-dibromo-5-ethoxy-4-hydroxybenzyl)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid.
DR jPOST; P0A988; -.
DR PaxDb; P0A988; -.
DR PRIDE; P0A988; -.
DR EnsemblBacteria; AAC76724; AAC76724; b3701.
DR EnsemblBacteria; BAE77593; BAE77593; BAE77593.
DR GeneID; 66672401; -.
DR GeneID; 948218; -.
DR KEGG; ecj:JW3678; -.
DR KEGG; eco:b3701; -.
DR PATRIC; fig|1411691.4.peg.3002; -.
DR EchoBASE; EB0238; -.
DR eggNOG; COG0592; Bacteria.
DR HOGENOM; CLU_038149_4_2_6; -.
DR InParanoid; P0A988; -.
DR OMA; YLIMPVR; -.
DR PhylomeDB; P0A988; -.
DR BioCyc; EcoCyc:EG10242-MON; -.
DR BioCyc; MetaCyc:EG10242-MON; -.
DR EvolutionaryTrace; P0A988; -.
DR PRO; PR:P0A988; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009360; C:DNA polymerase III complex; IDA:EcoCyc.
DR GO; GO:0044775; C:DNA polymerase III, beta sliding clamp processivity factor complex; IPI:ComplexPortal.
DR GO; GO:1990085; C:Hda-beta clamp complex; IPI:ComplexPortal.
DR GO; GO:1990078; C:replication inhibiting complex; IPI:ComplexPortal.
DR GO; GO:0030894; C:replisome; IC:ComplexPortal.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044787; P:bacterial-type DNA replication; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0006260; P:DNA replication; IDA:ComplexPortal.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IDA:EcoCyc.
DR GO; GO:0006261; P:DNA-templated DNA replication; IC:ComplexPortal.
DR GO; GO:0042276; P:error-prone translesion synthesis; IMP:EcoCyc.
DR GO; GO:0032297; P:negative regulation of DNA-templated DNA replication initiation; IC:ComplexPortal.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IC:ComplexPortal.
DR CDD; cd00140; beta_clamp; 1.
DR InterPro; IPR001001; DNA_polIII_beta.
DR InterPro; IPR022635; DNA_polIII_beta_C.
DR InterPro; IPR022637; DNA_polIII_beta_cen.
DR InterPro; IPR022634; DNA_polIII_beta_N.
DR PANTHER; PTHR30478; PTHR30478; 1.
DR Pfam; PF00712; DNA_pol3_beta; 1.
DR Pfam; PF02767; DNA_pol3_beta_2; 1.
DR Pfam; PF02768; DNA_pol3_beta_3; 1.
DR PIRSF; PIRSF000804; DNA_pol_III_b; 1.
DR SMART; SM00480; POL3Bc; 1.
DR TIGRFAMs; TIGR00663; dnan; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Cytoplasm; DNA replication;
KW DNA-binding; DNA-directed DNA polymerase; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..366
FT /note="Beta sliding clamp"
FT /id="PRO_0000105434"
FT REGION 1..120
FT /note="1"
FT /evidence="ECO:0000305"
FT REGION 129..243
FT /note="2"
FT /evidence="ECO:0000305"
FT REGION 245..365
FT /note="3"
FT /evidence="ECO:0000305"
FT BINDING 24
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000305|PubMed:18191219"
FT BINDING 73
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000269|PubMed:18191219"
FT BINDING 149
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000305|PubMed:18191219"
FT BINDING 153..154
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000305|PubMed:18191219"
FT VAR_SEQ 1..134
FT /note="Missing (in isoform Beta*)"
FT /evidence="ECO:0000269|PubMed:8576211"
FT /id="VSP_059030"
FT MUTAGEN 24
FT /note="R->A: Mild defect in DNA replication, impaired
FT loading of clamp on DNA, polymerase speed is wild-type.
FT More severe replication defect and very poor clamp loading;
FT when associated with A-149."
FT /evidence="ECO:0000269|PubMed:18191219"
FT MUTAGEN 66
FT /note="G->E: In dnaN159; a temperature- and UV-sensitive
FT mutation, displays altered DNA polymerase usage,
FT chronically induced SOS response; when associated with A-
FT 174."
FT /evidence="ECO:0000269|PubMed:15466025"
FT MUTAGEN 133
FT /note="A->T: Reduction of synthesis of beta*, probably due
FT to mutation of its promoter."
FT /evidence="ECO:0000269|PubMed:8576211"
FT MUTAGEN 135
FT /note="M->L: 3-fold reduction of synthesis of beta*,
FT probably due to loss of its start codon."
FT /evidence="ECO:0000269|PubMed:8576211"
FT MUTAGEN 146
FT /note="M->L: No effect on synthesis of beta*."
FT /evidence="ECO:0000269|PubMed:8576211"
FT MUTAGEN 149
FT /note="Q->A: Mild defect in DNA replication, impaired
FT loading of clamp on DNA, polymerase speed is wild-type.
FT More severe replication defect and very poor clamp loading;
FT when associated with A-24."
FT /evidence="ECO:0000269|PubMed:18191219"
FT MUTAGEN 153..154
FT /note="YY->SS: Very poor loading of clamp on DNA,
FT polymerase speed is wild-type."
FT /evidence="ECO:0000269|PubMed:18191219"
FT MUTAGEN 174
FT /note="G->A: In dnaN159; a temperature- and UV-sensitive
FT mutation, displays altered DNA polymerase usage,
FT chronically induced SOS response; when associated with A-
FT 66."
FT /evidence="ECO:0000269|PubMed:15466025"
FT MUTAGEN 272..273
FT /note="IL->AA: Monomeric in solution, binds very tightly to
FT subunit delta (holA). The monomer binds tightly to linear
FT and circular DNA. Cannot bind both Pol III and IV
FT simultaneously."
FT /evidence="ECO:0000269|PubMed:11525728,
FT ECO:0000269|PubMed:16168375, ECO:0000269|PubMed:18191219"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4K3L"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:4K3L"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:4N95"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1JQL"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4K3L"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:4K3L"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:4K3L"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:4K3L"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:4K3L"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:4K3L"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:3D1G"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:4K3L"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:4K3L"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:4K3L"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:4MJR"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:4K3L"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:1JQL"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:4K3L"
FT STRAND 354..361
FT /evidence="ECO:0007829|PDB:4K3L"
SQ SEQUENCE 366 AA; 40587 MW; 7A45646F61255B5A CRC64;
MKFTVEREHL LKPLQQVSGP LGGRPTLPIL GNLLLQVADG TLSLTGTDLE MEMVARVALV
QPHEPGATTV PARKFFDICR GLPEGAEIAV QLEGERMLVR SGRSRFSLST LPAADFPNLD
DWQSEVEFTL PQATMKRLIE ATQFSMAHQD VRYYLNGMLF ETEGEELRTV ATDGHRLAVC
SMPIGQSLPS HSVIVPRKGV IELMRMLDGG DNPLRVQIGS NNIRAHVGDF IFTSKLVDGR
FPDYRRVLPK NPDKHLEAGC DLLKQAFARA AILSNEKFRG VRLYVSENQL KITANNPEQE
EAEEILDVTY SGAEMEIGFN VSYVLDVLNA LKCENVRMML TDSVSSVQIE DAASQSAAYV
VMPMRL
