FIBER_BPK1F
ID FIBER_BPK1F Reviewed; 1064 AA.
AC Q04830; Q2WC71; Q858B1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 4.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Tail spike protein {ECO:0000305};
DE Short=TSP;
DE AltName: Full=Endo-N-acetylneuraminidase;
DE Short=Endo-N;
DE EC=3.2.1.129 {ECO:0000269|PubMed:12556457, ECO:0000269|PubMed:19189967, ECO:0000269|PubMed:3546309};
DE AltName: Full=Endo-alpha-sialidase {ECO:0000305};
DE AltName: Full=EndoNF;
DE AltName: Full=G102;
DE Contains:
DE RecName: Full=C-terminal chaperone protein;
OS Escherichia phage K1F (Bacteriophage K1F).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Kayfunavirus;
OC Escherichia virus K1F.
OX NCBI_TaxID=344021;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 2-31 AND 917-920, AND SUBCELLULAR
RP LOCATION.
RX PubMed=8331067; DOI=10.1128/jb.175.14.4354-4363.1993;
RA Petter J.G., Vimr E.R.;
RT "Complete nucleotide sequence of the bacteriophage K1F tail gene encoding
RT endo-N-acylneuraminidase (endo-N) and comparison to an endo-N homolog in
RT bacteriophage PK1E.";
RL J. Bacteriol. 175:4354-4363(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 913-922,
RP IDENTIFICATION, PROTEOLYTIC CLEAVAGE, AND CATALYTIC ACTIVITY.
RX PubMed=12556457; DOI=10.1074/jbc.m212048200;
RA Muehlenhoff M., Stummeyer K., Grove M., Sauerborn M., Gerardy-Schahn R.;
RT "Proteolytic processing and oligomerization of bacteriophage-derived
RT endosialidases.";
RL J. Biol. Chem. 278:12634-12644(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16321955; DOI=10.1128/jb.187.24.8499-8503.2005;
RA Scholl D., Merril C.;
RT "The genome of bacteriophage K1F, a T7-like phage that has acquired the
RT ability to replicate on K1 strains of Escherichia coli.";
RL J. Bacteriol. 187:8499-8503(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16689790; DOI=10.1111/j.1365-2958.2006.05173.x;
RA Stummeyer K., Schwarzer D., Claus H., Vogel U., Gerardy-Schahn R.,
RA Muhlenhoff M.;
RT "Evolution of bacteriophages infecting encapsulated bacteria: lessons from
RT Escherichia coli K1-specific phages.";
RL Mol. Microbiol. 60:1123-1135(2006).
RN [5]
RP CHARACTERIZATION, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3546309; DOI=10.1016/s0021-9258(18)61387-0;
RA Hallenbeck P.C., Vimr E.R., Yu F., Bassler B., Troy F.A.;
RT "Purification and properties of a bacteriophage-induced endo-N-
RT acetylneuraminidase specific for poly-alpha-2,8-sialosyl carbohydrate
RT units.";
RL J. Biol. Chem. 262:3553-3561(1987).
RN [6]
RP PROTEOLYTIC CLEAVAGE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-911.
RX PubMed=19189967; DOI=10.1074/jbc.m808475200;
RA Schwarzer D., Stummeyer K., Haselhorst T., Freiberger F., Rode B.,
RA Grove M., Scheper T., von Itzstein M., Muehlenhoff M., Gerardy-Schahn R.;
RT "Proteolytic release of the intramolecular chaperone domain confers
RT processivity to endosialidase F.";
RL J. Biol. Chem. 284:9465-9474(2009).
RN [7] {ECO:0007744|PDB:1V0E, ECO:0007744|PDB:1V0F}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 246-910, INTERACTION WITH SIALIC
RP ACID, SUBUNIT, MUTAGENESIS OF GLU-581; ARG-596 AND ARG-647, AND ACTIVE
RP SITE.
RX PubMed=15608653; DOI=10.1038/nsmb874;
RA Stummeyer K., Dickmanns A., Muhlenhoff M., Gerardy-Schahn R., Ficner R.;
RT "Crystal structure of the polysialic acid-degrading endosialidase of
RT bacteriophage K1F.";
RL Nat. Struct. Mol. Biol. 12:90-96(2005).
RN [8] {ECO:0007744|PDB:3JU4}
RP X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) OF 246-910, AND SUBUNIT.
RX PubMed=20124697; DOI=10.1107/s0907444909048720;
RA Schulz E.C., Neumann P., Gerardy-Schahn R., Sheldrick G.M., Ficner R.;
RT "Structure analysis of endosialidase NF at 0.98 A resolution.";
RL Acta Crystallogr. D 66:176-180(2010).
RN [9] {ECO:0007744|PDB:3GVJ, ECO:0007744|PDB:3GVK, ECO:0007744|PDB:3GVL}
RP X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 246-910 IN COMPLEX WITH
RP OLIGOMERIC SIALIC ACID, ACTIVE SITE, MUTAGENESIS OF TRP-328; HIS-350;
RP LYS-410; HIS-542; ARG-549; GLU-581 AND ARG-647, INTERACTION WITH SIALIC
RP ACID, AND FUNCTION.
RX PubMed=20096705; DOI=10.1016/j.jmb.2010.01.028;
RA Schulz E.C., Schwarzer D., Frank M., Stummeyer K., Muhlenhoff M.,
RA Dickmanns A., Gerardy-Schahn R., Ficner R.;
RT "Structural basis for the recognition and cleavage of polysialic acid by
RT the bacteriophage K1F tailspike protein EndoNF.";
RL J. Mol. Biol. 397:341-351(2010).
CC -!- FUNCTION: [Tail spike protein]: Responsible for initial absorption of
CC the phage to the host bacterium. Degrades the alpha-2,8-linked
CC polysialic acid K1 capsule by cleaving within the polymer chain of
CC polysialic acid. {ECO:0000269|PubMed:20096705,
CC ECO:0000269|PubMed:3546309}.
CC -!- FUNCTION: [C-terminal chaperone protein]: The C-terminal chaperone
CC protein mediates homotrimerization and proper folding of the catalytic
CC endo-N trimer. {ECO:0000269|PubMed:12556457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or
CC poly(sialic) acids.; EC=3.2.1.129;
CC Evidence={ECO:0000269|PubMed:12556457, ECO:0000269|PubMed:19189967,
CC ECO:0000269|PubMed:3546309};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=71 uM for poly-alpha-2,8-sialosyl carbohydrates
CC {ECO:0000269|PubMed:3546309};
CC KM=1.2 mM for oligo-alpha-2,8-sialosyl carbohydrates
CC {ECO:0000269|PubMed:3546309};
CC KM=7.1 uM for poly-alpha-2,8-alpha-2,9-sialosyl carbohydrates
CC {ECO:0000269|PubMed:3546309};
CC Vmax=19 umol/min/mg enzyme for poly-alpha-2,8-sialosyl carbohydrates
CC cleavage {ECO:0000269|PubMed:3546309};
CC Vmax=18 umol/min/mg enzyme for oligo-alpha-2,8-sialosyl carbohydrates
CC cleavage {ECO:0000269|PubMed:3546309};
CC Vmax=13 umol/min/mg enzyme for poly-alpha-2,8-alpha-2,9-sialosyl
CC carbohydrates {ECO:0000269|PubMed:3546309};
CC -!- SUBUNIT: [Tail spike protein]: Homotrimer (PubMed:3546309,
CC PubMed:20124697). Interacts with sialic acid (PubMed:15608653,
CC PubMed:20096705). {ECO:0000269|PubMed:15608653,
CC ECO:0000269|PubMed:20096705, ECO:0000269|PubMed:20124697,
CC ECO:0000269|PubMed:3546309}.
CC -!- INTERACTION:
CC Q04830; Q04830: -; NbExp=2; IntAct=EBI-15829658, EBI-15829658;
CC -!- SUBCELLULAR LOCATION: [Tail spike protein]: Virion. Note=Tail spike.
CC {ECO:0000269|PubMed:8331067}.
CC -!- PTM: Proteolytic cleavage and release of the chaperone stabilizes the
CC folded protein. {ECO:0000269|PubMed:12556457,
CC ECO:0000269|PubMed:19189967}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 58 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC37340.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M63657; AAC37340.1; ALT_FRAME; Unassigned_DNA.
DR EMBL; AJ505988; CAD44528.2; -; Genomic_DNA.
DR EMBL; DQ111067; AAZ73001.1; -; Genomic_DNA.
DR EMBL; AM084414; CAJ29390.1; -; Genomic_DNA.
DR PIR; A36887; A36887.
DR RefSeq; YP_338127.1; NC_007456.1.
DR PDB; 1V0E; X-ray; 1.90 A; A/B/C/D/E/F=246-910.
DR PDB; 1V0F; X-ray; 2.55 A; A/B/C/D/E/F=246-910.
DR PDB; 3GVJ; X-ray; 1.48 A; A=246-910.
DR PDB; 3GVK; X-ray; 1.84 A; A/B/C=246-910.
DR PDB; 3GVL; X-ray; 1.41 A; A=246-910.
DR PDB; 3GW6; X-ray; 2.60 A; A/B/C/D/E/F=790-1064.
DR PDB; 3JU4; X-ray; 0.98 A; A=246-910.
DR PDBsum; 1V0E; -.
DR PDBsum; 1V0F; -.
DR PDBsum; 3GVJ; -.
DR PDBsum; 3GVK; -.
DR PDBsum; 3GVL; -.
DR PDBsum; 3GW6; -.
DR PDBsum; 3JU4; -.
DR SMR; Q04830; -.
DR DIP; DIP-48774N; -.
DR DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR DrugBank; DB04265; N-acetyl-beta-neuraminic acid.
DR CAZy; GH58; Glycoside Hydrolase Family 58.
DR MEROPS; S74.001; -.
DR GeneID; 3707741; -.
DR KEGG; vg:3707741; -.
DR BRENDA; 3.2.1.129; 716.
DR SABIO-RK; Q04830; -.
DR EvolutionaryTrace; Q04830; -.
DR Proteomes; UP000001530; Genome.
DR Proteomes; UP000001722; Genome.
DR GO; GO:0098024; C:virus tail, fiber; IDA:UniProtKB.
DR GO; GO:0016996; F:endo-alpha-(2,8)-sialidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0098996; P:disruption of host cell glycocalyx during viral entry; IEA:UniProtKB-KW.
DR GO; GO:0044409; P:entry into host; IDA:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IDA:UniProtKB.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 4.10.1090.10; -; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR024427; Endosialidase_beta_barrel.
DR InterPro; IPR024428; Endosialidase_beta_prop.
DR InterPro; IPR024430; Endosialidase_C_dom.
DR InterPro; IPR044914; Endosialidase_C_dom_sf.
DR InterPro; IPR024429; Endosialidase_N-extension.
DR InterPro; IPR001724; Glycl_Hydrolase_58.
DR InterPro; IPR005604; Phage_T7_tail_fibre.
DR InterPro; IPR030392; S74_ICA.
DR InterPro; IPR036278; Sialidase_sf.
DR InterPro; IPR040775; Tail_spike_N.
DR Pfam; PF12195; End_beta_barrel; 1.
DR Pfam; PF12217; End_beta_propel; 1.
DR Pfam; PF12218; End_N_terminal; 1.
DR Pfam; PF12219; End_tail_spike; 1.
DR Pfam; PF13884; Peptidase_S74; 1.
DR Pfam; PF03906; Phage_T7_tail; 1.
DR Pfam; PF18668; Tail_spike_N; 1.
DR PRINTS; PR00849; GLHYDRLASE58.
DR SUPFAM; SSF50939; SSF50939; 1.
DR PROSITE; PS51688; ICA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Degradation of host capsule during virus entry;
KW Degradation of host cell envelope components during virus entry;
KW Direct protein sequencing; Glycosidase; Host-virus interaction; Hydrolase;
KW Reference proteome; Repeat; Viral attachment to host adhesion receptor;
KW Viral attachment to host cell; Viral tail fiber protein;
KW Viral tail protein; Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|PubMed:8331067"
FT CHAIN 2..1064
FT /note="Tail spike protein"
FT /id="PRO_0000057709"
FT CHAIN 912..1064
FT /note="C-terminal chaperone protein"
FT /evidence="ECO:0000305|PubMed:12556457"
FT /id="PRO_0000438182"
FT REPEAT 360..371
FT /note="BNR 1"
FT REPEAT 496..503
FT /note="BNR 2"
FT REPEAT 608..619
FT /note="BNR 3"
FT DOMAIN 911..1064
FT /note="Peptidase S74"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01025"
FT ACT_SITE 581
FT /evidence="ECO:0000269|PubMed:15608653,
FT ECO:0000269|PubMed:20096705"
FT ACT_SITE 596
FT /evidence="ECO:0000269|PubMed:15608653"
FT ACT_SITE 647
FT /evidence="ECO:0000269|PubMed:15608653,
FT ECO:0000269|PubMed:20096705"
FT SITE 542
FT /note="Binding to sialic acid"
FT /evidence="ECO:0000269|PubMed:20096705"
FT SITE 545
FT /note="Binding to sialic acid"
FT /evidence="ECO:0000269|PubMed:20096705"
FT SITE 549
FT /note="Binding to sialic acid"
FT /evidence="ECO:0000269|PubMed:20096705"
FT SITE 578
FT /note="Binding to sialic acid"
FT /evidence="ECO:0000269|PubMed:20096705"
FT SITE 598
FT /note="Binding to sialic acid"
FT /evidence="ECO:0000269|PubMed:20096705"
FT SITE 599
FT /note="Binding to sialic acid"
FT /evidence="ECO:0000269|PubMed:20096705"
FT MUTAGEN 328
FT /note="W->R: Almost complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:20096705"
FT MUTAGEN 350
FT /note="H->A,N,Q: Almost complete loss of enzymatic
FT activity."
FT /evidence="ECO:0000269|PubMed:20096705"
FT MUTAGEN 410
FT /note="K->A: 80% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:20096705"
FT MUTAGEN 542
FT /note="H->A: 60% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:20096705"
FT MUTAGEN 549
FT /note="R->A: Almost complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:20096705"
FT MUTAGEN 581
FT /note="E->A: Almost complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15608653,
FT ECO:0000269|PubMed:20096705"
FT MUTAGEN 596
FT /note="R->A: Complete loss of enzymatic activity; when
FT associated with A-581. Complete loss of enzymatic activity;
FT when associated with A-647."
FT /evidence="ECO:0000269|PubMed:15608653"
FT MUTAGEN 647
FT /note="R->A: Almost complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15608653,
FT ECO:0000269|PubMed:20096705"
FT MUTAGEN 911
FT /note="S->A: Complete loss of proteolytic processing. 190-
FT fold reduced enzymatic activity."
FT /evidence="ECO:0000269|PubMed:19189967"
FT CONFLICT 628
FT /note="H -> R (in Ref. 1; AAC37340)"
FT /evidence="ECO:0000305"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:3JU4"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:3JU4"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 339..352
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 356..364
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:3GVK"
FT TURN 380..384
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 398..407
FT /evidence="ECO:0007829|PDB:3JU4"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 413..422
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 426..431
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 524..531
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 537..543
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 550..556
FT /evidence="ECO:0007829|PDB:3JU4"
FT TURN 557..561
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 567..570
FT /evidence="ECO:0007829|PDB:3JU4"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 579..587
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 590..598
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 606..612
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 639..645
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 667..674
FT /evidence="ECO:0007829|PDB:3JU4"
FT TURN 675..677
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 686..690
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 696..698
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 702..710
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 713..721
FT /evidence="ECO:0007829|PDB:3JU4"
FT TURN 728..734
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 746..753
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 784..786
FT /evidence="ECO:0007829|PDB:3GVK"
FT STRAND 790..792
FT /evidence="ECO:0007829|PDB:3GVK"
FT STRAND 796..803
FT /evidence="ECO:0007829|PDB:3GVK"
FT TURN 808..811
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 812..817
FT /evidence="ECO:0007829|PDB:3GVK"
FT STRAND 819..826
FT /evidence="ECO:0007829|PDB:3GVK"
FT HELIX 833..835
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 837..847
FT /evidence="ECO:0007829|PDB:3JU4"
FT HELIX 848..850
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 853..857
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 861..863
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 867..870
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 872..879
FT /evidence="ECO:0007829|PDB:3GVK"
FT STRAND 884..889
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 891..893
FT /evidence="ECO:0007829|PDB:3JU4"
FT STRAND 901..905
FT /evidence="ECO:0007829|PDB:3GVK"
FT HELIX 924..930
FT /evidence="ECO:0007829|PDB:3GW6"
FT STRAND 936..938
FT /evidence="ECO:0007829|PDB:3GW6"
FT HELIX 941..947
FT /evidence="ECO:0007829|PDB:3GW6"
FT HELIX 948..950
FT /evidence="ECO:0007829|PDB:3GW6"
FT STRAND 953..956
FT /evidence="ECO:0007829|PDB:3GW6"
FT HELIX 959..968
FT /evidence="ECO:0007829|PDB:3GW6"
FT STRAND 984..989
FT /evidence="ECO:0007829|PDB:3GW6"
FT STRAND 992..1006
FT /evidence="ECO:0007829|PDB:3GW6"
FT STRAND 1008..1010
FT /evidence="ECO:0007829|PDB:3GW6"
FT STRAND 1012..1026
FT /evidence="ECO:0007829|PDB:3GW6"
FT STRAND 1029..1034
FT /evidence="ECO:0007829|PDB:3GW6"
FT HELIX 1036..1059
FT /evidence="ECO:0007829|PDB:3GW6"
SQ SEQUENCE 1064 AA; 118905 MW; 82FAB75EDC68DAB6 CRC64;
MSTITQFPSG NTQYRIEFDY LARTFVVVTL VNSSNPTLNR VLEVGRDYRF LNPTMIEMLV
DQSGFDIVRI HRQTGTDLVV DFRNGSVLTA SDLTTAELQA IHIAEEGRDQ TVDLAKEYAD
AAGSSAGNAK DSEDEARRIA ESIRAAGLIG YMTRRSFEKG YNVTTWSEVL LWEEDGDYYR
WDGTLPKNVP AGSTPETSGG IGLGAWVSVG DAALRSQISN PEGAILYPEL HRARWLDEKD
ARGWGAKGDG VTDDTAALTS ALNDTPVGQK INGNGKTYKV TSLPDISRFI NTRFVYERIP
GQPLYYASEE FVQGELFKIT DTPYYNAWPQ DKAFVYENVI YAPYMGSDRH GVSRLHVSWV
KSGDDGQTWS TPEWLTDLHP DYPTVNYHCM SMGVCRNRLF AMIETRTLAK NALTNCALWD
RPMSRSLHLT GGITKAANQR YATIHVPDHG LFVGDFVNFS NSAVTGVSGD MTVATVIDKD
NFTVLTPNQQ TSDLNNAGKN WHMGTSFHKS PWRKTDLGLI PSVTEVHSFA TIDNNGFAMG
YHQGDVAPRE VGLFYFPDAF NSPSNYVRRQ IPSEYEPDAS EPCIKYYDGV LYLITRGTRG
DRLGSSLHRS RDIGQTWESL RFPHNVHHTT LPFAKVGDDL IMFGSERAEN EWEAGAPDDR
YKASYPRTFY ARLNVNNWNA DDIEWVNITD QIYQGGIVNS GVGVGSVVVK DNYIYYMFGG
EDHFNPWTYG DNSAKDPFKS DGHPSDLYCY KMKIGPDNRV SRDFRYGAVP NRAVPVFFDT
NGVRTVPAPM EFTGDLGLGH VTIRASTSSN IRSEVLMEGE YGFIGKSIPT DNPAGQRIIF
CGGEGTSSTT GAQITLYGAN NTDSRRIVYN GDEHLFQSAD VKPYNDNVTA LGGPSNRFTT
AYLGSNPIVT SNGERKTEPV VFDDAFLDAW GDVHYIMYQW LDAVQLKGND ARIHFGVIAQ
QIRDVFIAHG LMDENSTNCR YAVLCYDKYP RMTDTVFSHN EIVEHTDEEG NVTTTEEPVY
TEVVIHEEGE EWGVRPDGIF FAEAAYQRRK LERIEARLSA LEQK
