ELAS_PSEAE
ID ELAS_PSEAE Reviewed; 498 AA.
AC P14756;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Elastase;
DE EC=3.4.24.26;
DE AltName: Full=Neutral metalloproteinase;
DE AltName: Full=PAE {ECO:0000303|PubMed:1899664};
DE AltName: Full=Pseudolysin;
DE Contains:
DE RecName: Full=Pro-elastase;
DE Flags: Precursor;
GN Name=lasB; OrderedLocusNames=PA3724;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAO;
RX PubMed=2842313; DOI=10.1128/jb.170.9.4309-4314.1988;
RA Bever R.A., Iglewski B.H.;
RT "Molecular characterization and nucleotide sequence of the Pseudomonas
RT aeruginosa elastase structural gene.";
RL J. Bacteriol. 170:4309-4314(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 13130 / JCM 20134;
RX PubMed=2493453; DOI=10.1128/jb.171.3.1698-1704.1989;
RA Fukushima J., Yamamoto S., Morihara K., Atsumi Y., Takeuchi H.,
RA Kawamoto S., Okuda K.;
RT "Structural gene and complete amino acid sequence of Pseudomonas aeruginosa
RT IFO 3455 elastase.";
RL J. Bacteriol. 171:1698-1704(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29260 / PA103, and N-10;
RX PubMed=1917848; DOI=10.1128/jb.173.19.6153-6158.1991;
RA Tanaka E., Kawamoto S., Fukushima J., Hamajima K., Onishi H., Miyagi Y.,
RA Inami S., Morihara K., Okuda K.;
RT "Detection of elastase production in Escherichia coli with the elastase
RT structural gene from several non-elastase-producing strains of Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 173:6153-6158(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PST-01;
RX PubMed=10828420; DOI=10.1016/s1369-703x(00)00060-7;
RA Ogino H., Yokoo J., Watanabe F., Ishikawa H.;
RT "Cloning and sequencing of a gene of organic solvent-stable protease
RT secreted from Pseudomonas aeruginosa PST-01 and its expression in
RT Escherichia coli.";
RL Biochem. Eng. J. 5:191-200(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [6]
RP PROTEIN SEQUENCE OF 24-28 AND 198-212.
RX PubMed=1544509; DOI=10.1016/0014-5793(92)80134-3;
RA Kessler E., Safrin M., Peretz M., Burstein Y.;
RT "Identification of cleavage sites involved in proteolytic processing of
RT Pseudomonas aeruginosa preproelastase.";
RL FEBS Lett. 299:291-293(1992).
RN [7]
RP PROTEIN SEQUENCE OF 24-28, FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC
RP CLEAVAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=PAO1 / PAO25;
RX PubMed=9642203; DOI=10.1128/jb.180.13.3467-3469.1998;
RA Braun P., de Groot A., Bitter W., Tommassen J.;
RT "Secretion of elastinolytic enzymes and their propeptides by Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 180:3467-3469(1998).
RN [8]
RP PROTEIN SEQUENCE OF 198-237.
RC STRAIN=PAO;
RX PubMed=3034864; DOI=10.1128/jb.169.6.2691-2696.1987;
RA Schad P.A., Bever R.A., Nicas T.I., Leduc F., Hanne L.F., Iglewski B.H.;
RT "Cloning and characterization of elastase genes from Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 169:2691-2696(1987).
RN [9]
RP PROTEIN SEQUENCE OF 198-217.
RC STRAIN=569B;
RX PubMed=2123831; DOI=10.1128/iai.58.12.4011-4015.1990;
RA Haese C.C., Finkelstein R.A.;
RT "Comparison of the Vibrio cholerae hemagglutinin/protease and the
RT Pseudomonas aeruginosa elastase.";
RL Infect. Immun. 58:4011-4015(1990).
RN [10]
RP PROTEIN SEQUENCE OF 198-212, FUNCTION, EXPRESSION IN E.COLI, AND
RP MUTAGENESIS OF HIS-420.
RC STRAIN=FRD1;
RX PubMed=1744034; DOI=10.1128/jb.173.24.7781-7789.1991;
RA McIver K., Kessler E., Ohman D.E.;
RT "Substitution of active-site His-223 in Pseudomonas aeruginosa elastase and
RT expression of the mutated lasB alleles in Escherichia coli show evidence
RT for autoproteolytic processing of proelastase.";
RL J. Bacteriol. 173:7781-7789(1991).
RN [11]
RP PROTEIN SEQUENCE OF 212-226; 354-376 AND 429-442.
RC STRAIN=ATCC 33467 / type 1 smooth, and ATCC 33468 / type 2 mucoid;
RA Liddor M.;
RT "Biofouling in water treatment systems: effect of membrane properties on
RT biofilm formation.";
RL Thesis (2005), Ben-Gurion University, Israel.
RN [12]
RP SUBCELLULAR LOCATION, INDUCTION, AND PROTEOLYTIC CLEAVAGE.
RC STRAIN=Habs serotype I;
RX PubMed=3141383; DOI=10.1128/jb.170.11.5241-5247.1988;
RA Kessler E., Safrin M.;
RT "Synthesis, processing, and transport of Pseudomonas aeruginosa elastase.";
RL J. Bacteriol. 170:5241-5247(1988).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1, DG1, and FRD1 / FRD2;
RX PubMed=1597429; DOI=10.1128/jb.174.12.4140-4147.1992;
RA Olson J.C., Ohman D.E.;
RT "Efficient production and processing of elastase and LasA by Pseudomonas
RT aeruginosa require zinc and calcium ions.";
RL J. Bacteriol. 174:4140-4147(1992).
RN [14]
RP FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1, FRD1, and Habs serotype 1;
RX PubMed=11533066; DOI=10.1074/jbc.m106950200;
RA Cahan R., Axelrad I., Safrin M., Ohman D.E., Kessler E.;
RT "A secreted aminopeptidase of Pseudomonas aeruginosa. Identification,
RT primary structure, and relationship to other aminopeptidases.";
RL J. Biol. Chem. 276:43645-43652(2001).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 198-498 IN COMPLEX WITH CALCIUM
RP AND ZINC, COFACTOR, SUBUNIT, DISULFIDE BOND, AND ACTIVE SITE.
RX PubMed=1899664; DOI=10.2210/pdb1ezm/pdb;
RA Thayer M.M., Flaherty K.M., McKay D.B.;
RT "Three-dimensional structure of the elastase of Pseudomonas aeruginosa at
RT 1.5-A resolution.";
RL J. Biol. Chem. 266:2864-2871(1991).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 198-498 IN COMPLEX WITH CALCIUM
RP AND ZINC AND AN INHIBITOR, COFACTOR, AND DISULFIDE BOND.
RA Bitto E., McKay D.B.;
RT "Elastase of Pseudomonas aeruginosa with an inhibitor.";
RL Submitted (JUL-2004) to the PDB data bank.
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 198-498 IN COMPLEX WITH CALCIUM
RP AND ZINC AND AN INHIBITOR, COFACTOR, AND DISULFIDE BOND.
RA Overgaard M.T., McKay D.B.;
RT "Structure of the elastase of Pseudomonas aeruginosa complexed with
RT phosphoramidon.";
RL Submitted (JUN-2008) to the PDB data bank.
CC -!- FUNCTION: Cleaves host elastin, collagen, IgG, and several complement
CC components as well as endogenous pro-aminopeptidase (PubMed:11533066).
CC Autocatalyses processing of its pro-peptide (PubMed:9642203,
CC PubMed:1744034). Processes the pro-peptide of pro-chitin-binding
CC protein (cbpD) (PubMed:9642203). Involved in the pathogenesis of
CC P.aeruginosa infections. {ECO:0000269|PubMed:11533066,
CC ECO:0000269|PubMed:1597429, ECO:0000269|PubMed:1744034,
CC ECO:0000269|PubMed:9642203}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins including elastin, collagen types III
CC and IV, fibronectin and immunoglobulin A, generally with bulky
CC hydrophobic group at P1'. Insulin B chain cleavage pattern identical
CC to that of thermolysin, but specificity differs in other respects.;
CC EC=3.4.24.26;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16,
CC ECO:0000269|Ref.17};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:1899664,
CC ECO:0000269|Ref.16, ECO:0000269|Ref.17};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16,
CC ECO:0000269|Ref.17};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000269|PubMed:1899664,
CC ECO:0000269|Ref.16, ECO:0000269|Ref.17};
CC -!- ACTIVITY REGULATION: Inhibited by phosphoramidon.
CC {ECO:0000269|PubMed:11533066}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1899664}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1597429,
CC ECO:0000269|PubMed:3141383, ECO:0000269|PubMed:9642203}. Note=Secreted
CC in an Xcp-dependent fashion (a type II secretion pathway).
CC {ECO:0000269|PubMed:9642203}.
CC -!- INDUCTION: Optimal protein expression in vivo requires both Zn(2+) and
CC Ca(2+) during growth (at protein level). {ECO:0000269|PubMed:1597429,
CC ECO:0000269|PubMed:3141383}.
CC -!- PTM: Made as a membrane-associated pre-pro-protein, which is exported
CC to the periplasm (yielding pro-elastase) with removal of the signal
CC peptide. Under certain conditions pro-elastase can accumulate. The pro-
CC peptide is removed in the periplasm yielding a (mature length) 33 kDa
CC protein, probably by autocatalysis (PubMed:1744034). The pro-peptide
CC probably remains associated with elastase and can be secreted
CC (PubMed:9642203). Further alterations (perhaps processing) seems to be
CC required before secretion into the extracellular space
CC (PubMed:1744034). {ECO:0000269|PubMed:11533066,
CC ECO:0000269|PubMed:1744034, ECO:0000269|PubMed:3141383,
CC ECO:0000269|PubMed:9642203}.
CC -!- DISRUPTION PHENOTYPE: Loss of processing of its own pro-peptide and
CC pro-chitin-binding protein CbpD (PubMed:9642203). Loss of processing of
CC pro-aminopeptidase to mature aminopeptidase (PubMed:11533066).
CC {ECO:0000269|PubMed:11533066, ECO:0000269|PubMed:9642203}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR EMBL; M19472; AAB36615.1; -; Genomic_DNA.
DR EMBL; M24531; AAA25811.1; -; Genomic_DNA.
DR EMBL; AB029328; BAB79621.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07111.1; -; Genomic_DNA.
DR PIR; A32359; HYBSPA.
DR RefSeq; NP_252413.1; NC_002516.2.
DR RefSeq; WP_003113835.1; NZ_QZGE01000001.1.
DR PDB; 1EZM; X-ray; 1.50 A; A=198-498.
DR PDB; 1U4G; X-ray; 1.40 A; A=198-498.
DR PDB; 3DBK; X-ray; 1.40 A; A=198-498.
DR PDB; 6F8B; X-ray; 1.30 A; A=198-498.
DR PDB; 6FZX; X-ray; 2.10 A; A=198-498.
DR PDBsum; 1EZM; -.
DR PDBsum; 1U4G; -.
DR PDBsum; 3DBK; -.
DR PDBsum; 6F8B; -.
DR PDBsum; 6FZX; -.
DR AlphaFoldDB; P14756; -.
DR SMR; P14756; -.
DR STRING; 287.DR97_4154; -.
DR BindingDB; P14756; -.
DR ChEMBL; CHEMBL1075146; -.
DR DrugBank; DB02307; N-(1-carboxy-3-phenylpropyl)phenylalanyl-alpha-asparagine.
DR MEROPS; M04.005; -.
DR PaxDb; P14756; -.
DR PRIDE; P14756; -.
DR EnsemblBacteria; AAG07111; AAG07111; PA3724.
DR GeneID; 880368; -.
DR KEGG; pae:PA3724; -.
DR PATRIC; fig|208964.12.peg.3895; -.
DR PseudoCAP; PA3724; -.
DR HOGENOM; CLU_008590_4_2_6; -.
DR InParanoid; P14756; -.
DR OMA; QLYWTAN; -.
DR PhylomeDB; P14756; -.
DR BioCyc; MetaCyc:MON-14569; -.
DR BioCyc; PAER208964:G1FZ6-3794-MON; -.
DR BRENDA; 3.4.24.26; 5087.
DR EvolutionaryTrace; P14756; -.
DR PHI-base; PHI:7892; -.
DR PRO; PR:P14756; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004175; F:endopeptidase activity; IDA:CACAO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IMP:PseudoCAP.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
DR GO; GO:0043952; P:protein transport by the Sec complex; IDA:PseudoCAP.
DR GO; GO:0006508; P:proteolysis; IDA:PseudoCAP.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:PseudoCAP.
DR Gene3D; 1.10.390.10; -; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR025711; PepSY.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF03413; PepSY; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Calcium; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Virulence; Zinc; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:1544509"
FT CHAIN 24..498
FT /note="Pro-elastase"
FT /id="PRO_0000431322"
FT PROPEP 24..197
FT /evidence="ECO:0000269|PubMed:1544509,
FT ECO:0000269|PubMed:2123831, ECO:0000269|PubMed:3034864,
FT ECO:0000269|PubMed:9642203"
FT /id="PRO_0000028616"
FT CHAIN 198..498
FT /note="Elastase"
FT /evidence="ECO:0000269|PubMed:1544509,
FT ECO:0000269|PubMed:1744034, ECO:0000269|PubMed:2123831,
FT ECO:0000269|PubMed:3034864"
FT /id="PRO_0000028617"
FT ACT_SITE 338
FT /evidence="ECO:0000305|PubMed:1899664"
FT ACT_SITE 420
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:1899664"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16,
FT ECO:0000269|Ref.17"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16,
FT ECO:0000269|Ref.17"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16,
FT ECO:0000269|Ref.17"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16,
FT ECO:0000269|Ref.17"
FT BINDING 369
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16,
FT ECO:0000269|Ref.17"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16,
FT ECO:0000269|Ref.17"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16,
FT ECO:0000269|Ref.17"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16,
FT ECO:0000269|Ref.17"
FT SITE 197..198
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:1744034"
FT DISULFID 227..255
FT /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16,
FT ECO:0000269|Ref.17"
FT DISULFID 467..494
FT /evidence="ECO:0000269|PubMed:1899664, ECO:0000269|Ref.17"
FT VARIANT 75
FT /note="Y -> T (in strain: PA103 and N-10)"
FT VARIANT 102
FT /note="Q -> R (in strain: PA103 and N-10)"
FT VARIANT 185
FT /note="T -> Y (in strain: PA103 and N-10)"
FT VARIANT 211
FT /note="K -> I (in strain: 569B)"
FT VARIANT 241
FT /note="S -> G (in strain: PA103 and N-10)"
FT VARIANT 282
FT /note="K -> D (in strain: PA103 and N-10)"
FT VARIANT 325
FT /note="M -> V (in strain: IFO 3455)"
FT VARIANT 471
FT /note="R -> S (in strain: PA103)"
FT MUTAGEN 420
FT /note="H->D,Y: Loss of proteolytic and elastolytic
FT activity; significantly decreased processing of
FT proelastase, proelastase accumulates in the periplasm (in
FT E.coli)."
FT /evidence="ECO:0000269|PubMed:1744034"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:6F8B"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:6F8B"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:6F8B"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1EZM"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:6F8B"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:6F8B"
FT HELIX 269..288
FT /evidence="ECO:0007829|PDB:6F8B"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1U4G"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:6F8B"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:6F8B"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:6F8B"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:6F8B"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:6F8B"
FT HELIX 332..346
FT /evidence="ECO:0007829|PDB:6F8B"
FT HELIX 354..376
FT /evidence="ECO:0007829|PDB:6F8B"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:6F8B"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:6F8B"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:6F8B"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:6F8B"
FT HELIX 400..403
FT /evidence="ECO:0007829|PDB:6F8B"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:6F8B"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:6F8B"
FT HELIX 419..422
FT /evidence="ECO:0007829|PDB:6F8B"
FT HELIX 424..434
FT /evidence="ECO:0007829|PDB:6F8B"
FT HELIX 441..454
FT /evidence="ECO:0007829|PDB:6F8B"
FT HELIX 462..475
FT /evidence="ECO:0007829|PDB:6F8B"
FT HELIX 480..489
FT /evidence="ECO:0007829|PDB:6F8B"
SQ SEQUENCE 498 AA; 53687 MW; 4B6AA96A569D9615 CRC64;
MKKVSTLDLL FVAIMGVSPA AFAADLIDVS KLPSKAAQGA PGPVTLQAAV GAGGADELKA
IRSTTLPNGK QVTRYEQFHN GVRVVGEAIT EVKGPGKSVA AQRSGHFVAN IAADLPGSTT
AAVSAEQVLA QAKSLKAQGR KTENDKVELV IRLGENNIAQ LVYNVSYLIP GEGLSRPHFV
IDAKTGEVLD QWEGLAHAEA GGPGGNQKIG KYTYGSDYGP LIVNDRCEMD DGNVITVDMN
SSTDDSKTTP FRFACPTNTY KQVNGAYSPL NDAHFFGGVV FKLYRDWFGT SPLTHKLYMK
VHYGRSVENA YWDGTAMLFG DGATMFYPLV SLDVAAHEVS HGFTEQNSGL IYRGQSGGMN
EAFSDMAGEA AEFYMRGKND FLIGYDIKKG SGALRYMDQP SRDGRSIDNA SQYYNGIDVH
HSSGVYNRAF YLLANSPGWD TRKAFEVFVD ANRYYWTATS NYNSGACGVI RSAQNRNYSA
ADVTRAFSTV GVTCPSAL
