CH601_MYCTU
ID CH601_MYCTU Reviewed; 539 AA.
AC P9WPE9; L0TCP9; P0A518; Q59573; Q59581;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Chaperonin GroEL 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL1 {ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000303|PubMed:19717599};
GN Synonyms=cpn60.1 {ECO:0000303|PubMed:15327959},
GN groL1 {ECO:0000255|HAMAP-Rule:MF_00600}; OrderedLocusNames=Rv3417c;
GN ORFNames=MTCY78.12;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=7681982; DOI=10.1073/pnas.90.7.2608;
RA Kong T.H., Coates A.R.M., Butcher P.D., Hickman C.J., Shinnick T.M.;
RT "Mycobacterium tuberculosis expresses two chaperonin-60 homologs.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2608-2612(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP FUNCTION AS A CHAPERONE, ATPASE ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND LACK OF ACTIVITY IN E.COLI.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15327959; DOI=10.1016/j.jmb.2004.07.066;
RA Qamra R., Srinivas V., Mande S.C.;
RT "Mycobacterium tuberculosis GroEL homologues unusually exist as lower
RT oligomers and retain the ability to suppress aggregation of substrate
RT proteins.";
RL J. Mol. Biol. 342:605-617(2004).
RN [4]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18227175; DOI=10.1128/iai.01078-07;
RA Hu Y., Henderson B., Lund P.A., Tormay P., Ahmed M.T., Gurcha S.S.,
RA Besra G.S., Coates A.R.;
RT "A Mycobacterium tuberculosis mutant lacking the groEL homologue cpn60.1 is
RT viable but fails to induce an inflammatory response in animal models of
RT infection.";
RL Infect. Immun. 76:1535-1546(2008).
RN [5]
RP PHOSPHORYLATION AT THR-25 AND THR-54, AND MUTAGENESIS OF THR-25 AND THR-54.
RX PubMed=19201798; DOI=10.1128/jb.01569-08;
RA Canova M.J., Kremer L., Molle V.;
RT "The Mycobacterium tuberculosis GroEL1 chaperone is a substrate of Ser/Thr
RT protein kinases.";
RL J. Bacteriol. 191:2876-2883(2009).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, PHOSPHORYLATION AT SER-393, AND
RP LACK OF ACTIVITY IN E.COLI.
RX PubMed=19717599; DOI=10.1128/jb.00652-09;
RA Kumar C.M., Khare G., Srikanth C.V., Tyagi A.K., Sardesai A.A., Mande S.C.;
RT "Facilitated oligomerization of mycobacterial GroEL: evidence for
RT phosphorylation-mediated oligomerization.";
RL J. Bacteriol. 191:6525-6538(2009).
RN [7]
RP ERRATUM OF PUBMED:19717599.
RX PubMed=32900867; DOI=10.1128/jb.00441-20;
RA Kumar C.M.S., Khare G., Srikanth C.V., Tyagi A.K., Sardesai A.A.,
RA Mande S.C.;
RL J. Bacteriol. 202:0-0(2020).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [9]
RP LACK OF ACTIVITY IN E.COLI.
RX PubMed=22834700; DOI=10.1111/j.1365-2958.2012.08150.x;
RA Fan M., Rao T., Zacco E., Ahmed M.T., Shukla A., Ojha A., Freeke J.,
RA Robinson C.V., Benesch J.L., Lund P.A.;
RT "The unusual mycobacterial chaperonins: evidence for in vivo
RT oligomerization and specialization of function.";
RL Mol. Microbiol. 85:934-944(2012).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=26822628; DOI=10.1016/j.tube.2015.11.003;
RA Sharma A., Rustad T., Mahajan G., Kumar A., Rao K.V., Banerjee S.,
RA Sherman D.R., Mande S.C.;
RT "Towards understanding the biological function of the unusual chaperonin
RT Cpn60.1 (GroEL1) of Mycobacterium tuberculosis.";
RL Tuberculosis 97:137-146(2016).
RN [11]
RP ACETYLATION AT SER-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=27353550; DOI=10.1038/srep28892;
RA Pathak D., Bhat A.H., Sapehia V., Rai J., Rao A.;
RT "Biochemical evidence for relaxed substrate specificity of Nalpha-
RT acetyltransferase (Rv3420c/rimI) of Mycobacterium tuberculosis.";
RL Sci. Rep. 6:28892-28892(2016).
RN [12]
RP FUNCTION IN COPPER HOMEOSTASIS, SUBUNIT, DOMAIN, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 522-VAL--HIS-539.
RX PubMed=32808291; DOI=10.1002/1873-3468.13906;
RA Ansari M.Y., Batra S.D., Ojha H., Dhiman K., Ganguly A., Tyagi J.S.,
RA Mande S.C.;
RT "A novel function of Mycobacterium tuberculosis chaperonin paralog GroEL1
RT in copper homeostasis.";
RL FEBS Lett. 594:3305-3323(2020).
RN [13]
RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=32812602; DOI=10.1039/d0mt00101e;
RA Yang D., Klebl D.P., Zeng S., Sobott F., Prevost M., Soumillion P.,
RA Vandenbussche G., Fontaine V.;
RT "Interplays between copper and Mycobacterium tuberculosis GroEL1.";
RL Metallomics 12:1267-1277(2020).
RN [14] {ECO:0007744|PDB:3M6C}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 184-377, FUNCTION, AND DOMAIN.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21094166; DOI=10.1016/j.jmb.2010.11.021;
RA Sielaff B., Lee K.S., Tsai F.T.;
RT "Structural and functional conservation of Mycobacterium tuberculosis GroEL
RT paralogs suggests that GroEL1 is a chaperonin.";
RL J. Mol. Biol. 405:831-839(2011).
CC -!- FUNCTION: Prevents aggregation of substrate proteins and promotes their
CC refolding (PubMed:15327959, PubMed:19717599, PubMed:21094166). In
CC vitro, activity may be independent of the presence or absence of the
CC GroES co-chaperonin or ATP (PubMed:15327959). Shows weak ATPase
CC activity (PubMed:15327959, PubMed:32812602).
CC {ECO:0000269|PubMed:15327959, ECO:0000269|PubMed:19717599,
CC ECO:0000269|PubMed:21094166, ECO:0000269|PubMed:32812602}.
CC -!- FUNCTION: Involved in copper homeostasis (PubMed:32808291,
CC PubMed:32812602). Binds copper and may help maintaining copper
CC homeostasis when copper is present in excess, notably in the macrophage
CC phagosome, by acting as a metal storage protein (PubMed:32808291,
CC PubMed:32812602). Could be involved in copper resistance during
CC mycobacterial biofilm formation (PubMed:32812602). Protects from copper
CC stress in vitro (PubMed:32808291). Can also bind other metals, but
CC binds copper with relatively higher affinity compared to nickel and
CC cobalt (PubMed:32808291). May play an important role in survival under
CC low aeration by affecting the expression of genes known for hypoxia
CC response (PubMed:26822628). {ECO:0000269|PubMed:26822628,
CC ECO:0000269|PubMed:32808291, ECO:0000269|PubMed:32812602}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00600};
CC -!- ACTIVITY REGULATION: Oligomerization, which is mediated by
CC phosphorylation, is required for chaperone activity. Lower oligomeric
CC GroELs possess substrate binding activity but are inefficient in
CC promoting refolding (PubMed:19717599). The binding of copper protects
CC GroEL1 from destabilization and increases its ATPase activity
CC (PubMed:32812602). {ECO:0000269|PubMed:19717599,
CC ECO:0000269|PubMed:32812602}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat for ATPase activity is 0.16 min(-1).
CC {ECO:0000269|PubMed:15327959};
CC -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric
CC rings stacked back-to-back (Probable). Also exists as lower oligomers,
CC including monomeric, dimeric and heptameric forms (PubMed:15327959,
CC PubMed:19717599, PubMed:32808291, PubMed:32812602). The switch between
CC the single-ring (heptameric) and double-ring (tetradecameric) forms is
CC mediated by phosphorylation on Ser-393 (PubMed:19717599). Interacts
CC with the co-chaperonin GroES (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_00600, ECO:0000269|PubMed:15327959,
CC ECO:0000269|PubMed:19717599, ECO:0000269|PubMed:32808291,
CC ECO:0000269|PubMed:32812602, ECO:0000305|PubMed:19717599}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- INDUCTION: In response to heat shock (45 degrees Celsius) and
CC hyperosmolarity. {ECO:0000269|PubMed:18227175}.
CC -!- DOMAIN: Each subunit is composed of an apical domain, an intermediate
CC domain and an equatorial domain (PubMed:32808291). The apical domain is
CC sufficient for substrate recognition (PubMed:21094166). Contains a
CC characteristic histidine-rich C terminus which is essential for copper
CC binding (PubMed:32808291). Copper binding causes conformational
CC rearrangement (PubMed:32808291). {ECO:0000269|PubMed:21094166,
CC ECO:0000269|PubMed:32808291}.
CC -!- PTM: Phosphorylated on Thr-25 and Thr-54 by PknF (PubMed:19201798).
CC Phosphorylated on Ser-393 by an unknown kinase (PubMed:19717599).
CC {ECO:0000269|PubMed:19201798, ECO:0000269|PubMed:19717599}.
CC -!- PTM: N-terminus is acetylated by RimI. {ECO:0000269|PubMed:27353550}.
CC -!- DISRUPTION PHENOTYPE: Not essential (PubMed:18227175, PubMed:26822628).
CC Increased heat sensitivity (at 55 degrees Celsius) (PubMed:18227175).
CC Inactivation of the gene does not affect cell wall lipids, or growth
CC and survival in macrophages, but mutant shows slower growth in the
CC mouse lung and spleen in early infection and fails to produce
CC granulomatous inflammation in either mice or guinea pigs
CC (PubMed:18227175). This is associated with reduced cytokine expression
CC in infected animals and macrophages (PubMed:18227175). Knockout of the
CC gene leads to differential gene expression under low aeration stress,
CC including down regulation of genes in copper response and genes
CC encoding members of folate synthesis super pathway (PubMed:26822628).
CC Survival under low aeration is significantly compromised in this
CC knockout mutant (PubMed:26822628). Knockout mutant shows increased
CC sensitivity to Cu(2+) (PubMed:32808291). {ECO:0000269|PubMed:18227175,
CC ECO:0000269|PubMed:26822628, ECO:0000269|PubMed:32808291}.
CC -!- MISCELLANEOUS: M.tuberculosis contains two copies of the groEL gene,
CC groEL1 and groEL2. GroEL2 is probably the housekeeping chaperonin, with
CC the GroEL1 proteins having evolved, following an ancestral gene
CC duplication event, to take on a more specialized role or roles.
CC {ECO:0000305|PubMed:22834700}.
CC -!- MISCELLANEOUS: Recombinant GroEL of M.tuberculosis is unable to act as
CC effective molecular chaperone when expressed in Escherichia coli
CC (PubMed:18227175, PubMed:19717599, PubMed:22834700). Although
CC M.tuberculosis GroEL1 is capable of oligomerization in its native
CC environment, it cannot do the same in E.coli, which probably explains
CC its lack of chaperone activity in E.coli (PubMed:19717599). Can
CC complement M.smegmatis mutants (PubMed:22834700).
CC {ECO:0000269|PubMed:18227175, ECO:0000269|PubMed:19717599,
CC ECO:0000269|PubMed:22834700}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; X60350; CAA42909.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46239.1; -; Genomic_DNA.
DR PIR; F70737; F70737.
DR RefSeq; NP_217934.1; NC_000962.3.
DR RefSeq; WP_003418021.1; NZ_NVQJ01000027.1.
DR PDB; 3M6C; X-ray; 2.20 A; A=184-377.
DR PDBsum; 3M6C; -.
DR AlphaFoldDB; P9WPE9; -.
DR SMR; P9WPE9; -.
DR STRING; 83332.Rv3417c; -.
DR MoonProt; P9WPE9; -.
DR iPTMnet; P9WPE9; -.
DR PaxDb; P9WPE9; -.
DR DNASU; 887877; -.
DR GeneID; 45427413; -.
DR GeneID; 887877; -.
DR KEGG; mtu:Rv3417c; -.
DR TubercuList; Rv3417c; -.
DR eggNOG; COG0459; Bacteria.
DR OMA; YWIASNA; -.
DR PhylomeDB; P9WPE9; -.
DR PRO; PR:P9WPE9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0043590; C:bacterial nucleoid; IDA:MTBBASE.
DR GO; GO:1990220; C:GroEL-GroES complex; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:MTBBASE.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042262; P:DNA protection; IDA:MTBBASE.
DR GO; GO:0090143; P:nucleoid organization; IDA:MTBBASE.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:CAFA.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IDA:CAFA.
DR GO; GO:0009408; P:response to heat; IEP:MTBBASE.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Chaperone; Copper; Cytoplasm;
KW Isomerase; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:27353550"
FT CHAIN 2..539
FT /note="Chaperonin GroEL 1"
FT /id="PRO_0000063451"
FT BINDING 29..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 86..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:27353550"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19201798"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19201798"
FT MOD_RES 393
FT /note="Phosphoserine; in tetradecamer"
FT /evidence="ECO:0000269|PubMed:19717599"
FT VARIANT 467
FT /note="N -> K (in strain: Erdman)"
FT MUTAGEN 25
FT /note="T->A: Lack of phosphorylation by PknF; when
FT associated with A-54."
FT /evidence="ECO:0000269|PubMed:19201798"
FT MUTAGEN 54
FT /note="T->A: Lack of phosphorylation by PknF; when
FT associated with A-25."
FT /evidence="ECO:0000269|PubMed:19201798"
FT MUTAGEN 522..539
FT /note="Missing: Cannot bind nickel, cobalt or copper."
FT /evidence="ECO:0000269|PubMed:32808291"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:3M6C"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:3M6C"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:3M6C"
FT STRAND 210..225
FT /evidence="ECO:0007829|PDB:3M6C"
FT HELIX 228..241
FT /evidence="ECO:0007829|PDB:3M6C"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:3M6C"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:3M6C"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:3M6C"
FT HELIX 280..294
FT /evidence="ECO:0007829|PDB:3M6C"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:3M6C"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:3M6C"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:3M6C"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:3M6C"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:3M6C"
FT HELIX 337..352
FT /evidence="ECO:0007829|PDB:3M6C"
FT HELIX 357..373
FT /evidence="ECO:0007829|PDB:3M6C"
SQ SEQUENCE 539 AA; 55877 MW; 3E0B93164C091B63 CRC64;
MSKLIEYDET ARRAMEVGMD KLADTVRVTL GPRGRHVVLA KAFGGPTVTN DGVTVAREIE
LEDPFEDLGA QLVKSVATKT NDVAGDGTTT ATILAQALIK GGLRLVAAGV NPIALGVGIG
KAADAVSEAL LASATPVSGK TGIAQVATVS SRDEQIGDLV GEAMSKVGHD GVVSVEESST
LGTELEFTEG IGFDKGFLSA YFVTDFDNQQ AVLEDALILL HQDKISSLPD LLPLLEKVAG
TGKPLLIVAE DVEGEALATL VVNAIRKTLK AVAVKGPYFG DRRKAFLEDL AVVTGGQVVN
PDAGMVLREV GLEVLGSARR VVVSKDDTVI VDGGGTAEAV ANRAKHLRAE IDKSDSDWDR
EKLGERLAKL AGGVAVIKVG AATETALKER KESVEDAVAA AKAAVEEGIV PGGGASLIHQ
ARKALTELRA SLTGDEVLGV DVFSEALAAP LFWIAANAGL DGSVVVNKVS ELPAGHGLNV
NTLSYGDLAA DGVIDPVKVT RSAVLNASSV ARMVLTTETV VVDKPAKAED HDHHHGHAH
