DOSC_ECOLI
ID DOSC_ECOLI Reviewed; 460 AA.
AC P0AA89; P77793;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Diguanylate cyclase DosC;
DE Short=DGC;
DE EC=2.7.7.65;
DE AltName: Full=Direct oxygen-sensing cyclase;
GN Name=dosC; Synonyms=dgcO {ECO:0000303|PubMed:26148715}, yddV;
GN OrderedLocusNames=b1490, JW5241;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
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 [3]
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 [4]
RP FUNCTION AS A DIGUANYLATE CYCLASE, AND OPERON STRUCTURE.
RC STRAIN=K12 / MG1655 / ATCC 47076, K12 / W3110 / ATCC 27325 / DSM 5911, and
RC TOB1;
RX PubMed=16418169; DOI=10.1074/jbc.m510701200;
RA Mendez-Ortiz M.M., Hyodo M., Hayakawa Y., Membrillo-Hernandez J.;
RT "Genome-wide transcriptional profile of Escherichia coli in response to
RT high levels of the second messenger 3',5'-cyclic diguanylic acid.";
RL J. Biol. Chem. 281:8090-8099(2006).
RN [5]
RP RPOS-DEPENDENCE.
RC STRAIN=K12 / MC4100;
RX PubMed=17010156; DOI=10.1111/j.1365-2958.2006.05440.x;
RA Weber H., Pesavento C., Possling A., Tischendorf G., Hengge R.;
RT "Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia
RT coli.";
RL Mol. Microbiol. 62:1014-1034(2006).
RN [6]
RP CATALYTIC ACTIVITY, HEME COFACTOR, O(2)-BINDING, INTERACTION WITH DOSP, AND
RP OPERON STRUCTURE.
RX PubMed=19764732; DOI=10.1021/bi901409g;
RA Tuckerman J.R., Gonzalez G., Sousa E.H., Wan X., Saito J.A., Alam M.,
RA Gilles-Gonzalez M.A.;
RT "An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-
RT di-GMP control.";
RL Biochemistry 48:9764-9774(2009).
RN [7]
RP INDUCTION, AND RPOS-DEPENDENCE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=19332833; DOI=10.1099/mic.0.024257-0;
RA Sommerfeldt N., Possling A., Becker G., Pesavento C., Tschowri N.,
RA Hengge R.;
RT "Gene expression patterns and differential input into curli fimbriae
RT regulation of all GGDEF/EAL domain proteins in Escherichia coli.";
RL Microbiology 155:1318-1331(2009).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DOMAIN, O(2)-BINDING,
RP CO-BINDING, CYANIDE-BINDING, IMIDAZOLE-BINDING, KINETIC PARAMETERS, REDOX
RP POTENTIAL, MUTAGENESIS OF TYR-43; GLN-60; HIS-98; HIS-223; ARG-365;
RP ASP-368; ASP-376 AND GLU-377, ABSORPTION SPECTROSCOPY, AND RESONANCE RAMAN
RP SPECTROSCOPY.
RC STRAIN=K12;
RX PubMed=21067162; DOI=10.1021/bi100733q;
RA Kitanishi K., Kobayashi K., Kawamura Y., Ishigami I., Ogura T.,
RA Nakajima K., Igarashi J., Tanaka A., Shimizu T.;
RT "Important roles of Tyr43 at the putative heme distal side in the oxygen
RT recognition and stability of the Fe(II)-O2 complex of YddV, a globin-
RT coupled heme-based oxygen sensor diguanylate cyclase.";
RL Biochemistry 49:10381-10393(2010).
RN [9]
RP ROLE IN MOTILITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20303158; DOI=10.1016/j.cell.2010.01.018;
RA Boehm A., Kaiser M., Li H., Spangler C., Kasper C.A., Ackermann M.,
RA Kaever V., Sourjik V., Roth V., Jenal U.;
RT "Second messenger-mediated adjustment of bacterial swimming velocity.";
RL Cell 141:107-116(2010).
RN [10]
RP FUNCTION IN REGULATION OF CSGBAC EXPRESSION, DISRUPTION PHENOTYPE, AND
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20553324; DOI=10.1111/j.1574-695x.2010.00702.x;
RA Tagliabue L., Maciag A., Antoniani D., Landini P.;
RT "The yddV-dos operon controls biofilm formation through the regulation of
RT genes encoding curli fibers' subunits in aerobically growing Escherichia
RT coli.";
RL FEMS Immunol. Med. Microbiol. 59:477-484(2010).
RN [11]
RP FUNCTION IN REGULATION OF PGAABCD EXPRESSION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 376-ASP-GLU-377.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20576684; DOI=10.1099/mic.0.041350-0;
RA Tagliabue L., Antoniani D., Maciag A., Bocci P., Raffaelli N., Landini P.;
RT "The diguanylate cyclase YddV controls production of the exopolysaccharide
RT poly-N-acetylglucosamine (PNAG) through regulation of the PNAG biosynthetic
RT pgaABCD operon.";
RL Microbiology 156:2901-2911(2010).
RN [12]
RP MUTAGENESIS OF LEU-65, AND ABSORPTION SPECTROSCOPY.
RC STRAIN=K12;
RX PubMed=22005448; DOI=10.1016/j.jinorgbio.2011.09.019;
RA Nakajima K., Kitanishi K., Kobayashi K., Kobayashi N., Igarashi J.,
RA Shimizu T.;
RT "Leu65 in the heme distal side is critical for the stability of the Fe(II)-
RT O(2) complex of YddV, a globin-coupled oxygen sensor diguanylate cyclase.";
RL J. Inorg. Biochem. 108:163-170(2012).
RN [13]
RP NOMENCLATURE.
RX PubMed=26148715; DOI=10.1128/jb.00424-15;
RA Hengge R., Galperin M.Y., Ghigo J.M., Gomelsky M., Green J., Hughes K.T.,
RA Jenal U., Landini P.;
RT "Systematic nomenclature for GGDEF and EAL domain-containing cyclic di-GMP
RT turnover proteins of Escherichia coli.";
RL J. Bacteriol. 198:7-11(2015).
CC -!- FUNCTION: Globin-coupled heme-based oxygen sensor protein displaying
CC diguanylate cyclase (DGC) activity in response to oxygen availability.
CC Thus, catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the
CC condensation of 2 GTP molecules. Is involved in the modulation of
CC intracellular c-di-GMP levels, in association with DosP which catalyzes
CC the degradation of c-di-GMP (PDE activity). Cyclic-di-GMP is a second
CC messenger which controls cell surface-associated traits in bacteria.
CC DosC regulates biofilm formation through the oxygen-dependent
CC activation of the csgBAC operon, which encodes curli structural
CC subunits, while not affecting the expression of the regulatory operon
CC csgDEFG. DosC, but not the other DGCs in E.coli, also promotes the
CC production of the exopolysaccharide poly-N-acetylglucosamine (PNAG)
CC through up-regulation of the expression of the PNAG biosynthetic
CC pgaABCD operon, independently of CsrA.
CC -!- FUNCTION: Overexpression leads to an increased level of c-di-GMP, which
CC leads to changes in the cell surface, to abnormal cell division,
CC increased biofilm formation and decreased swimming (the latter 2 in
CC strain W3110). In a strain able to produce cellulose (strain TOB1, a
CC fecal isolate) overexpression leads to an increase in cellulose
CC production.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 GTP = cyclic di-3',5'-guanylate + 2 diphosphate;
CC Xref=Rhea:RHEA:24898, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:58805; EC=2.7.7.65;
CC Evidence={ECO:0000269|PubMed:19764732, ECO:0000269|PubMed:21067162};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group per subunit. The Fe(2+) state binds O(2) and CO
CC while the Fe(3+) state can bind CN(-) and imidazole.;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activity depends on O(2)-binding and heme redox
CC state: the Fe(III), Fe(II)-O(2), and Fe(II)-CO complexes of DosC are
CC active forms, whereas Fe(II) and Fe(II)-NO complexes are inactive
CC forms. {ECO:0000269|PubMed:21067162}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=The Fe(III), Fe(II)-O(2), and Fe(II)-CO complexes of DosC
CC display DGC activity with turnover numbers of 0.066, 0.022, and 0.022
CC min(-1), respectively. The DGC reaction catalyzed by DosC is the
CC rate-determining step for c-di-GMP homeostasis. Binds O(2), CO,
CC cyanide and imidazole with a dissociation constant of 14 uM, 0.095
CC uM, 4.7 uM and 0.055 uM, respectively. {ECO:0000269|PubMed:21067162};
CC Redox potential:
CC E(0) is -17 mV.;
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
CC -!- SUBUNIT: Forms a complex with DosP.
CC -!- INDUCTION: By RpoS in the late exponential growth phase and upon entry
CC into stationary phase. Expression is higher at 28 than 37 degrees
CC Celsius. In rich medium DosC and DgcM are the major RpoS-dependent
CC GGDEF-domain containing proteins in the cell, whereas in minimal medium
CC it is the major RpoS-dependent GGDEF-domain containing protein. Highly
CC expressed on solid medium. A member of the dosCP operon.
CC {ECO:0000269|PubMed:19332833, ECO:0000269|PubMed:20553324}.
CC -!- DOMAIN: Is composed of an N-terminal sensory globin-fold domain that
CC binds heme and oxygen, and a C-terminal GGDEF diguanylate cyclase
CC domain. {ECO:0000269|PubMed:21067162}.
CC -!- DISRUPTION PHENOTYPE: Disruption results in a 2.5-fold reduction in
CC surface adhesion, a 3.5-fold reduction in biofilm formation, a large
CC reduction in curli production, a drastic decrease in csgB expression
CC (400-fold reduction in aerobic growth) and in an approximately 3.5-fold
CC reduction in pgaA transcript levels in comparison with wild-type.
CC Disruption partially suppresses the reduced motility of a pdeH
CC disruption; concomitant disruption of dosC, dgcE, dgcQ and dgcN
CC completely restores motility, suggesting these 4 genes, together with
CC the c-di-GMP phosphodiesterase PdeH, form a network that regulates cell
CC motility by altering levels of c-di-GMP. {ECO:0000269|PubMed:20303158,
CC ECO:0000269|PubMed:20553324, ECO:0000269|PubMed:20576684}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA15155.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC74563.3; -; Genomic_DNA.
DR EMBL; AP009048; BAA15155.2; ALT_INIT; Genomic_DNA.
DR PIR; E64902; E64902.
DR RefSeq; NP_416007.3; NC_000913.3.
DR RefSeq; WP_000426292.1; NZ_SSZK01000038.1.
DR PDB; 4ZVA; X-ray; 2.00 A; A/B=8-170.
DR PDB; 4ZVB; X-ray; 2.40 A; A/B/C/D=1-155.
DR PDB; 4ZVC; X-ray; 1.50 A; A/B=173-298.
DR PDB; 4ZVD; X-ray; 1.90 A; A/B=173-298.
DR PDB; 4ZVE; X-ray; 1.20 A; A=297-460.
DR PDB; 4ZVF; X-ray; 1.15 A; A=297-460.
DR PDB; 4ZVG; X-ray; 2.20 A; A/B=297-460.
DR PDB; 4ZVH; X-ray; 3.30 A; A/B=297-460.
DR PDBsum; 4ZVA; -.
DR PDBsum; 4ZVB; -.
DR PDBsum; 4ZVC; -.
DR PDBsum; 4ZVD; -.
DR PDBsum; 4ZVE; -.
DR PDBsum; 4ZVF; -.
DR PDBsum; 4ZVG; -.
DR PDBsum; 4ZVH; -.
DR AlphaFoldDB; P0AA89; -.
DR SMR; P0AA89; -.
DR BioGRID; 4262162; 6.
DR ComplexPortal; CPX-3982; dosPC diguanylate cyclase/c-di-GMP phosphodiesterase complex.
DR STRING; 511145.b1490; -.
DR jPOST; P0AA89; -.
DR PaxDb; P0AA89; -.
DR PRIDE; P0AA89; -.
DR DNASU; 945835; -.
DR EnsemblBacteria; AAC74563; AAC74563; b1490.
DR EnsemblBacteria; BAA15155; BAA15155; BAA15155.
DR GeneID; 945835; -.
DR KEGG; ecj:JW5241; -.
DR KEGG; eco:b1490; -.
DR PATRIC; fig|1411691.4.peg.777; -.
DR EchoBASE; EB3554; -.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_000445_11_5_6; -.
DR InParanoid; P0AA89; -.
DR OMA; DGHPDYE; -.
DR BioCyc; EcoCyc:G6784-MON; -.
DR BioCyc; MetaCyc:G6784-MON; -.
DR BRENDA; 2.7.7.65; 2026.
DR UniPathway; UPA00599; -.
DR PRO; PR:P0AA89; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0070025; F:carbon monoxide binding; IDA:EcoCyc.
DR GO; GO:0052621; F:diguanylate cyclase activity; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IDA:EcoCyc.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IBA:GO_Central.
DR GO; GO:1902201; P:negative regulation of bacterial-type flagellum-dependent cell motility; IBA:GO_Central.
DR GO; GO:0070482; P:response to oxygen levels; IDA:ComplexPortal.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd14757; GS_EcDosC-like_GGDEF; 1.
DR Gene3D; 1.10.490.10; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR039435; DosC_GS.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR044398; Globin-sensor_dom.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF11563; Protoglobin; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR TIGRFAMs; TIGR00254; GGDEF; 1.
DR PROSITE; PS50887; GGDEF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Heme; Iron; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..460
FT /note="Diguanylate cyclase DosC"
FT /id="PRO_0000201321"
FT DOMAIN 325..458
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 98
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 43
FT /note="Involved in oxygen binding and important for the
FT stability of the Fe(II)-O(2) complex"
FT SITE 60
FT /note="Important for oxygen binding and stability of the
FT Fe(II)-O(2) complex"
FT SITE 65
FT /note="Critical for restricting water access to the heme
FT distal side to avoid rapid autoxidation"
FT SITE 338
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT MUTAGEN 43
FT /note="Y->A,L: Same biofilm formation activity as wild-
FT type. Large decrease in O(2) affinity."
FT /evidence="ECO:0000269|PubMed:21067162"
FT MUTAGEN 43
FT /note="Y->F,W: Same biofilm formation activity as wild-
FT type. Markedly enhanced O(2) dissociation but not
FT association rate constants. Highly enhanced autoxidation
FT rate constant."
FT /evidence="ECO:0000269|PubMed:21067162"
FT MUTAGEN 60
FT /note="Q->A,E: Same biofilm formation activity as wild-
FT type. Enhanced O(2) dissociation but not association rate
FT constants. Enhanced autoxidation rate constant."
FT /evidence="ECO:0000269|PubMed:21067162"
FT MUTAGEN 60
FT /note="Q->L: Same biofilm formation activity as wild-type.
FT 5-fold reduction in O(2) dissociation rate constant.
FT Significant decrease in the autoxidation rate constant."
FT /evidence="ECO:0000269|PubMed:21067162"
FT MUTAGEN 65
FT /note="L->G,T: Enhanced autoxidation rate constant.
FT Markedly enhanced O(2) association rate constant."
FT /evidence="ECO:0000269|PubMed:22005448"
FT MUTAGEN 65
FT /note="L->M,Q: Enhanced autoxidation rate constant.
FT Decrease in O(2) association rate constant."
FT /evidence="ECO:0000269|PubMed:22005448"
FT MUTAGEN 98
FT /note="H->A: Same biofilm formation activity as wild-type.
FT Loss of heme-binding ability."
FT /evidence="ECO:0000269|PubMed:21067162"
FT MUTAGEN 223
FT /note="H->A: Same biofilm formation activity as wild-type."
FT /evidence="ECO:0000269|PubMed:21067162"
FT MUTAGEN 365
FT /note="R->A: Same biofilm formation activity as wild-type."
FT /evidence="ECO:0000269|PubMed:21067162"
FT MUTAGEN 368
FT /note="D->A: Lacks biofilm formation activity, and thus is
FT probably devoid of diguanylate cyclase activity."
FT /evidence="ECO:0000269|PubMed:21067162"
FT MUTAGEN 376..377
FT /note="DE->AA: Loss of DGC activity. Stimulation of PNAG
FT production and activation of pgaABCD expression are
FT abolished."
FT /evidence="ECO:0000269|PubMed:20576684"
FT MUTAGEN 376
FT /note="D->A: Lacks biofilm formation activity, and thus is
FT probably devoid of diguanylate cyclase activity."
FT /evidence="ECO:0000269|PubMed:21067162"
FT MUTAGEN 377
FT /note="E->A: Lacks biofilm formation activity, and thus is
FT probably devoid of diguanylate cyclase activity."
FT /evidence="ECO:0000269|PubMed:21067162"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:4ZVA"
FT HELIX 21..48
FT /evidence="ECO:0007829|PDB:4ZVA"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:4ZVA"
FT HELIX 59..77
FT /evidence="ECO:0007829|PDB:4ZVA"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4ZVA"
FT HELIX 84..101
FT /evidence="ECO:0007829|PDB:4ZVA"
FT HELIX 105..124
FT /evidence="ECO:0007829|PDB:4ZVA"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:4ZVA"
FT HELIX 130..152
FT /evidence="ECO:0007829|PDB:4ZVA"
FT HELIX 178..203
FT /evidence="ECO:0007829|PDB:4ZVC"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:4ZVC"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:4ZVC"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:4ZVC"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:4ZVC"
FT HELIX 233..254
FT /evidence="ECO:0007829|PDB:4ZVC"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:4ZVC"
FT HELIX 262..291
FT /evidence="ECO:0007829|PDB:4ZVC"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:4ZVF"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:4ZVF"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4ZVF"
FT HELIX 309..323
FT /evidence="ECO:0007829|PDB:4ZVF"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:4ZVF"
FT HELIX 337..344
FT /evidence="ECO:0007829|PDB:4ZVF"
FT HELIX 346..363
FT /evidence="ECO:0007829|PDB:4ZVF"
FT STRAND 368..374
FT /evidence="ECO:0007829|PDB:4ZVF"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:4ZVF"
FT HELIX 387..402
FT /evidence="ECO:0007829|PDB:4ZVF"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:4ZVH"
FT STRAND 418..424
FT /evidence="ECO:0007829|PDB:4ZVF"
FT HELIX 431..447
FT /evidence="ECO:0007829|PDB:4ZVF"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:4ZVF"
SQ SEQUENCE 460 AA; 53178 MW; 79168311553E61C3 CRC64;
MEMYFKRMKD EWTGLVEQAD PPIRAKAAEI AVAHAHYLSI EFYRIVRIDP HAEEFLSNEQ
VERQLKSAME RWIINVLSAQ VDDVERLIQI QHTVAEVHAR IGIPVEIVEM GFRVLKKILY
PVIFSSDYSA AEKLQVYHFS INSIDIAMEV MTRAFTFSDS SASKEDENYR IFSLLENAEE
EKERQIASIL SWEIDIIYKI LLDSDLGSSL PLSQADFGLW FNHKGRHYFS GIAEVGHISR
LIQDFDGIFN QTMRNTRNLN NRSLRVKFLL QIRNTVSQII TLLRELFEEV SRHEVGMDVL
TKLLNRRFLP TIFKREIAHA NRTGTPLSVL IIDVDKFKEI NDTWGHNTGD EILRKVSQAF
YDNVRSSDYV FRYGGDEFII VLTEASENET LRTAERIRSR VEKTKLKAAN GEDIALSLSI
GAAMFNGHPD YERLIQIADE ALYIAKRRGR NRVELWKASL
