TUBZ_BACTI
ID TUBZ_BACTI Reviewed; 484 AA.
AC Q8KNP3;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Tubulin-like protein TubZ {ECO:0000303|PubMed:17510284};
DE EC=3.6.5.- {ECO:0000269|PubMed:17873046, ECO:0000269|PubMed:18198178};
DE AltName: Full=FtsZ-like protein TubZ-Bt {ECO:0000303|PubMed:18198178};
GN Name=tubZ {ECO:0000303|PubMed:17510284}; ORFNames=ATN07_33550, pBt156;
OS Bacillus thuringiensis subsp. israelensis.
OG Plasmid pAM65-52-4-128K {ECO:0000303|PubMed:27810477},
OG Plasmid pBtoxis {ECO:0000303|PubMed:12324359}, and
OG Plasmid pT0124-4 {ECO:0000303|Ref.3}.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1430;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=4Q2-72 / 4Q5; PLASMID=pBtoxis;
RX PubMed=12324359; DOI=10.1128/aem.68.10.5082-5095.2002;
RA Berry C., O'Niel S., Ben-Dov E., Jones A.F., Murphy L., Quail M.A.,
RA Harris D., Zaritsky A., Parkhill J.;
RT "Complete sequence and organization of pBtoxis, the toxin-coding plasmid of
RT Bacillus thuringiensis subsp. israelensis.";
RL Appl. Environ. Microbiol. 68:5082-5095(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AM65-52; PLASMID=pAM65-52-4-128K;
RX PubMed=27810477; DOI=10.1016/j.resmic.2016.10.008;
RA Bolotin A., Gillis A., Sanchis V., Nielsen-LeRoux C., Mahillon J.,
RA Lereclus D., Sorokin A.;
RT "Comparative genomics of extrachromosomal elements in Bacillus
RT thuringiensis subsp. israelensis.";
RL Res. Microbiol. 168:331-344(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1.24; PLASMID=pT0124-4;
RA Alves G.B., Melo F.L., Campos F.S., Correa R.F.T., Ribeiro B.M.,
RA Aguiar R.W.S.;
RT "Bacillus turingiensis from Tocantins.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, PROBABLE OPERON, DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
RC STRAIN=4Q5; PLASMID=pBtoxis;
RX PubMed=16936050; DOI=10.1128/aem.00976-06;
RA Tang M., Bideshi D.K., Park H.W., Federici B.A.;
RT "Minireplicon from pBtoxis of Bacillus thuringiensis subsp. israelensis.";
RL Appl. Environ. Microbiol. 72:6948-6954(2006).
RN [5]
RP SUBUNIT, FILAMENT FORMATION, SUBCELLULAR LOCATION, PROBABLE OPERON, AND
RP MUTAGENESIS OF ASP-269.
RC STRAIN=ATCC 35646 / USDA HD522; PLASMID=pBtoxis;
RX PubMed=17510284; DOI=10.1101/gad.1546107;
RA Larsen R.A., Cusumano C., Fujioka A., Lim-Fong G., Patterson P.,
RA Pogliano J.;
RT "Treadmilling of a prokaryotic tubulin-like protein, TubZ, required for
RT plasmid stability in Bacillus thuringiensis.";
RL Genes Dev. 21:1340-1352(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TUBR, SUBUNIT, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=4Q5; PLASMID=pBtoxis;
RX PubMed=17873046; DOI=10.1128/jb.00908-07;
RA Tang M., Bideshi D.K., Park H.W., Federici B.A.;
RT "Iteron-binding ORF157 and FtsZ-like ORF156 proteins encoded by pBtoxis
RT play a role in its replication in Bacillus thuringiensis subsp.
RT israelensis.";
RL J. Bacteriol. 189:8053-8058(2007).
RN [7]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, FILAMENT FORMATION, AND SUBUNIT.
RC STRAIN=Mosquito Dunks; PLASMID=pBtoxis;
RX PubMed=18198178; DOI=10.1074/jbc.m709163200;
RA Chen Y., Erickson H.P.;
RT "In vitro assembly studies of FtsZ/tubulin-like proteins (TubZ) from
RT Bacillus plasmids: evidence for a capping mechanism.";
RL J. Biol. Chem. 283:8102-8109(2008).
RN [8]
RP FILAMENT STABILITY.
RC STRAIN=ATCC 35646 / USDA HD522; PLASMID=pBtoxis;
RX PubMed=23010931; DOI=10.1073/pnas.1210899109;
RA Aylett C.H., Lowe J.;
RT "Superstructure of the centromeric complex of TubZRC plasmid partitioning
RT systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:16522-16527(2012).
RN [9]
RP FUNCTION, AND SUBUNIT.
RC PLASMID=pBtoxis;
RX PubMed=25825718; DOI=10.1073/pnas.1423746112;
RA Fink G., Loewe J.;
RT "Reconstitution of a prokaryotic minus end-tracking system using TubRC
RT centromeric complexes and tubulin-like protein TubZ filaments.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1845-E1850(2015).
RN [10] {ECO:0007744|PDB:3M89, ECO:0007744|PDB:3M8K}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-407 IN COMPLEX WITH GTP, X-RAY
RP CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-428, FUNCTION, SUBUNIT, DOMAIN, AND
RP MUTAGENESIS OF 408-ARG--ARG-484.
RC PLASMID=pBtoxis;
RX PubMed=20534443; DOI=10.1073/pnas.1003817107;
RA Ni L., Xu W., Kumaraswami M., Schumacher M.A.;
RT "Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits
RT the prokaryotic tubulin homolog TubZ to effect DNA partition.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11763-11768(2010).
RN [11] {ECO:0007744|PDB:2XKA, ECO:0007744|PDB:2XKB}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-421 IN COMPLEX WITH GDP AND
RP GTP-GAMMA-S, COFACTOR, SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC 35646 / USDA HD522; PLASMID=pBtoxis;
RX PubMed=20974911; DOI=10.1073/pnas.1010176107;
RA Aylett C.H., Wang Q., Michie K.A., Amos L.A., Lowe J.;
RT "Filament structure of bacterial tubulin homologue TubZ.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19766-19771(2010).
RN [12] {ECO:0007744|PDB:3J4S, ECO:0007744|PDB:3J4T}
RP STRUCTURE BY ELECTRON MICROSCOPY (6.80 ANGSTROMS), FILAMENT FORMATION,
RP DOMAIN, AND MUTAGENESIS OF 224-LYS--LYS-230; ASP-269 AND 471-ILE--ARG-484.
RC STRAIN=ATCC 35646 / USDA HD522; PLASMID=pBtoxis;
RX PubMed=24550513; DOI=10.1073/pnas.1318339111;
RA Montabana E.A., Agard D.A.;
RT "Bacterial tubulin TubZ-Bt transitions between a two-stranded intermediate
RT and a four-stranded filament upon GTP hydrolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:3407-3412(2014).
CC -!- FUNCTION: A tubulin-like, filament forming GTPase; the motor component
CC of the type III plasmid partition system which ensures correct
CC segregation of the pBtoxis plasmid. Filaments may seed from the
CC centromere-like site (tubC) when bound by DNA-binding protein TubR; the
CC tubC-TubR complex stabilizes the TubZ filament. Filaments grow at the
CC plus end and depolymerize at the minus end, a process called
CC treadmilling. TubR-tubC complexes track the depolymerizing minus end of
CC the filament, probably pulling plasmid within the cell
CC (PubMed:20534443, PubMed:23010931, PubMed:25825718). Required for
CC pBtoxis plasmid replication/partition (PubMed:16936050,
CC PubMed:17873046). Binds the TubR-tubC complex; GTP is not required for
CC binding to TubR-tubC. TubZ alone does not bind DNA (PubMed:17873046,
CC PubMed:20534443, PubMed:25825718). Has a high GTPase activity in the
CC presence of Mg(2+); in the presence of GTP assembles into dynamic
CC filaments which upon polymerization bind almost exclusively GDP.
CC Filament formation is cooperative, requiring a critical concentration.
CC Formation occurs very quickly and is followed by disassembly as GTP is
CC consumed (PubMed:18198178). {ECO:0000269|PubMed:16936050,
CC ECO:0000269|PubMed:17873046, ECO:0000269|PubMed:18198178,
CC ECO:0000269|PubMed:20534443, ECO:0000269|PubMed:23010931,
CC ECO:0000269|PubMed:25825718}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:17873046, ECO:0000269|PubMed:18198178};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20974911, ECO:0007744|PDB:2XKB};
CC Note=In the GTP-gamma-S-bound filament structure all subunits bind
CC Mg(2+), in the GDP-bound filament less than half the subunits bind
CC Mg(2+). {ECO:0000269|PubMed:20974911, ECO:0007744|PDB:2XKA,
CC ECO:0007744|PDB:2XKB};
CC -!- ACTIVITY REGULATION: GTPase is inhibited by GTP-gamma-S, which also
CC stabilizes filaments. {ECO:0000269|PubMed:18198178}.
CC -!- SUBUNIT: Forms filaments; a 2-stranded filament forms with the non-
CC hydrolyzable GTP-gamma-S which is probably a precursor to the 4-
CC stranded filament that forms in the presence of GTP. The 4-stranded
CC form binds GDP (PubMed:18198178, PubMed:20974911, PubMed:24550513). In
CC vivo polymerizes to form dynamic filaments that often extend from one
CC cell pole to the other, moving in a unidirectional manner. Filaments
CC polymerize at the plus end and depolymerize at the minus end, a process
CC called treadmilling. Polymerization only occurs above a critical
CC concentration, it does not require upstream tubR (PubMed:17510284,
CC PubMed:25825718). The tubC DNA-TubR complex binds to TubZ
CC (PubMed:17873046, PubMed:20534443). {ECO:0000269|PubMed:17510284,
CC ECO:0000269|PubMed:17873046, ECO:0000269|PubMed:18198178,
CC ECO:0000269|PubMed:20534443, ECO:0000269|PubMed:20974911,
CC ECO:0000269|PubMed:24550513, ECO:0000269|PubMed:25825718}.
CC -!- INTERACTION:
CC Q8KNP3; Q8KNP3: tubZ; NbExp=3; IntAct=EBI-15857919, EBI-15857919;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17510284}.
CC Note=Forms long, dynamic filaments. {ECO:0000269|PubMed:17510284,
CC ECO:0000269|PubMed:18198178, ECO:0000269|PubMed:20974911}.
CC -!- INDUCTION: Probably part of the tubR-tubZ operon.
CC {ECO:0000305|PubMed:16936050, ECO:0000305|PubMed:17510284}.
CC -!- DOMAIN: Consists of two domains: a nucleotide-binding N-terminus that
CC hydrolyzes GTP and a C-terminus domain necessary for polymerization.
CC The domains are bridged by a long, central helix (PubMed:20534443,
CC PubMed:20974911, PubMed:24550513). The C-terminus is required for
CC binding to the TubR-iteron DNA complex; its gradual deletion leads to
CC decreasing binding to TubR-DNA (PubMed:20534443). Interactions between
CC the C-terminus and the following monomer drive polymerization (By
CC similarity). The C-terminus is required for filament formation
CC (PubMed:24550513). In the absence of GTP's gamma phosphate the
CC intersubunit interface is weakened, linking GTP hydrolysis to
CC treadmilling (PubMed:20974911). {ECO:0000250|UniProtKB:B3FK34,
CC ECO:0000269|PubMed:20534443, ECO:0000269|PubMed:20974911,
CC ECO:0000269|PubMed:24550513}.
CC -!- DISRUPTION PHENOTYPE: Loss of plasmid replication.
CC {ECO:0000269|PubMed:16936050, ECO:0000269|PubMed:17873046}.
CC -!- BIOTECHNOLOGY: A miniplasmid containing this and upstream gene tubR is
CC able to replicate in B.thuringiensis subsp. israelensis and express
CC insect toxin proteins. The miniplasmid could be used to make plasmids
CC for insect toxin overexpression. {ECO:0000269|PubMed:16936050}.
CC -!- MISCELLANEOUS: N-terminally tagged protein does not form filaments, C-
CC terminally tagged protein does so, but not as well as untagged protein.
CC {ECO:0000269|PubMed:24550513}.
CC -!- MISCELLANEOUS: The pBtoxis plasmid encodes all the major endotoxin
CC proteins (Cyt1Aa, Cry4Aa, Cry4Ba, and Cry11Aa) responsible for the
CC mosquito larvicidal activity of strain 4Q2.
CC {ECO:0000305|PubMed:12324359}.
CC -!- SIMILARITY: Belongs to the FtsZ family. TubZ subfamily.
CC {ECO:0000305|PubMed:20534443}.
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DR EMBL; AL731825; CAD30186.1; -; Genomic_DNA.
DR EMBL; CP013279; AND28646.1; -; Genomic_DNA.
DR EMBL; KY352353; ASO64580.1; -; Genomic_DNA.
DR RefSeq; WP_000926085.1; NZ_VEIF01000064.1.
DR RefSeq; YP_001573870.1; NC_010076.1.
DR PDB; 2XKA; X-ray; 3.00 A; A/B/C/D/E/F/G=1-421.
DR PDB; 2XKB; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-421.
DR PDB; 3J4S; EM; 6.80 A; A=1-484.
DR PDB; 3J4T; EM; 10.80 A; F=1-484.
DR PDB; 3M89; X-ray; 2.00 A; A=1-407.
DR PDB; 3M8K; X-ray; 2.30 A; A=1-428.
DR PDBsum; 2XKA; -.
DR PDBsum; 2XKB; -.
DR PDBsum; 3J4S; -.
DR PDBsum; 3J4T; -.
DR PDBsum; 3M89; -.
DR PDBsum; 3M8K; -.
DR AlphaFoldDB; Q8KNP3; -.
DR SMR; Q8KNP3; -.
DR DIP; DIP-59348N; -.
DR IntAct; Q8KNP3; 1.
DR EvolutionaryTrace; Q8KNP3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030541; P:plasmid partitioning; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR SUPFAM; SSF52490; SSF52490; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Plasmid; Plasmid partition.
FT CHAIN 1..484
FT /note="Tubulin-like protein TubZ"
FT /id="PRO_0000448563"
FT REGION 408..484
FT /note="Required to bind TubR-DNA complex"
FT /evidence="ECO:0000269|PubMed:20534443"
FT REGION 428..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20534443,
FT ECO:0000269|PubMed:20974911, ECO:0007744|PDB:2XKA,
FT ECO:0007744|PDB:2XKB, ECO:0007744|PDB:3M89"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20974911,
FT ECO:0007744|PDB:2XKB"
FT BINDING 140..142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20534443,
FT ECO:0000269|PubMed:20974911, ECO:0007744|PDB:2XKA,
FT ECO:0007744|PDB:2XKB, ECO:0007744|PDB:3M89"
FT BINDING 213
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20534443,
FT ECO:0000269|PubMed:20974911, ECO:0007744|PDB:2XKA,
FT ECO:0007744|PDB:2XKB, ECO:0007744|PDB:3M89"
FT BINDING 237
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20534443,
FT ECO:0007744|PDB:3M89"
FT BINDING 241
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:20534443,
FT ECO:0000269|PubMed:20974911, ECO:0007744|PDB:2XKA,
FT ECO:0007744|PDB:2XKB, ECO:0007744|PDB:3M89"
FT MUTAGEN 224..230
FT /note="KGTKDLK->AGTADLA: No polymerization in the presence
FT of GTP, forms 2-stranded filaments in the presence of GTP-
FT gamma-S; destabilizes the 4-stranded filament but should
FT not affect GTP hydrolysis."
FT /evidence="ECO:0000269|PubMed:24550513"
FT MUTAGEN 269
FT /note="D->A: Lower critical concentration value, filaments
FT are deficient in disassembly, pBtoxis is very unstable,
FT assembles with wild-type TubZ subunits; probably has no
FT GTPase activity. Only forms thin, 2 stranded filaments."
FT /evidence="ECO:0000269|PubMed:17510284,
FT ECO:0000269|PubMed:24550513"
FT MUTAGEN 408..484
FT /note="Missing: No longer binds TubR-DNA complex, protein
FT still forms filaments in vitro."
FT /evidence="ECO:0000269|PubMed:20534443"
FT MUTAGEN 471..484
FT /note="Missing: Very poor polymerization in the presence of
FT GTP or GTP-gamma-S."
FT /evidence="ECO:0000269|PubMed:24550513"
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:3M8K"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2XKA"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 104..118
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2XKA"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 140..154
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 173..196
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:2XKA"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 236..257
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 267..275
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 279..288
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 320..330
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 337..347
FT /evidence="ECO:0007829|PDB:3M89"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 364..379
FT /evidence="ECO:0007829|PDB:3M89"
FT HELIX 384..400
FT /evidence="ECO:0007829|PDB:3M89"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:2XKB"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:2XKA"
SQ SEQUENCE 484 AA; 54373 MW; A7969E2625171D0D CRC64;
MLLNSNELEH IHSTNHSVND ISIRWGVIGA GQKGNKEADL FAGYKFSNGT TCYPTLAVNF
AESDMMHLQN IIKEDRIHFD GLKGAARTPS VVTDLFDPET NPNANGYLDK LAQELGRKFT
NEEGEVIVDQ FLICLGAGGG VGTGWGSLVL QLIREQFFPC PVSMLISLPS GDPDEINNAL
VLLSEIDEFM REQDRLFGNS DIKPLANVIV NDNTQMQRII ESQKGTKDLK NRYVNWKEVA
NDNVVSTLHE INIIPENYGS DNVTYDPSDL IKLLSIPGRF LTIGKARIAK FDLHSLENSI
KRSLDEGFFS AEHQFETATM YGGFVLRPSN ADFFKDVNTE NRIRNTLGEY KRLDEIAGKF
GDPIWDNEYA VCYTIFAGMT MPKRYISLAR EGKELAEKQE QLRAEAQRKQ DEEKVDISFA
TNRVQKNTFN PYNKNQGFGG ASRFSGGKNS AFKRQTSEAT STQNQQEEEN IISTLKTSNP
FKKR
