PHLC_CLOP1
ID PHLC_CLOP1 Reviewed; 398 AA.
AC Q0TV31; P15310; P94658; Q46246; Q46279; Q46280; Q46281; Q46282; Q57317;
AC Q59303; Q59304; Q59305; Q59313; Q60121;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phospholipase C;
DE Short=PLC;
DE EC=3.1.4.3;
DE AltName: Full=Alpha-toxin;
DE AltName: Full=Hemolysin;
DE AltName: Full=Lecithinase;
DE AltName: Full=Phosphatidylcholine cholinephosphohydrolase;
DE Flags: Precursor;
GN Name=plc; Synonyms=cpa; OrderedLocusNames=CPF_0042;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 29-39.
RX PubMed=2540749; DOI=10.1016/0006-291x(89)91616-1;
RA Okabe A., Shimizu T., Hayashi H.;
RT "Cloning and sequencing of a phospholipase C gene of Clostridium
RT perfringens.";
RL Biochem. Biophys. Res. Commun. 160:33-39(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 29-53.
RX PubMed=2536355; DOI=10.1128/iai.57.2.367-376.1989;
RA Titball R.W., Hunter S.E.C., Martin K.L., Morris B.C., Shuttleworth A.D.,
RA Rubidge T., Anderson D.W., Kelly D.C.;
RT "Molecular cloning and nucleotide sequence of the alpha-toxin
RT (phospholipase C) of Clostridium perfringens.";
RL Infect. Immun. 57:367-376(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 /
RC Type A;
RX PubMed=2536356; DOI=10.1128/iai.57.2.468-476.1989;
RA Tso J.Y., Siebel C.;
RT "Cloning and expression of the phospholipase C gene from Clostridium
RT perfringens and Clostridium bifermentans.";
RL Infect. Immun. 57:468-476(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2546005; DOI=10.1111/j.1365-2958.1989.tb00183.x;
RA Leslie D., Fairweather N., Pickard D., Dougan G., Kehoe M.;
RT "Phospholipase C and haemolytic activities of Clostridium perfringens
RT alpha-toxin cloned in Escherichia coli: sequence and homology with a
RT Bacillus cereus phospholipase C.";
RL Mol. Microbiol. 3:383-392(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
RN [6]
RP MUTAGENESIS OF HISTIDINE RESIDUES.
RX PubMed=7868589; DOI=10.1128/jb.177.5.1179-1185.1995;
RA Nagahama M., Okagawa Y., Nakayama T., Nishioka E., Sakurai J.;
RT "Site-directed mutagenesis of histidine residues in Clostridium perfringens
RT alpha-toxin.";
RL J. Bacteriol. 177:1179-1185(1995).
RN [7]
RP ACTIVITY AGAINST MOUSE ERYTHROCYTES, AND USE AS A VACCINE.
RX PubMed=8581165; DOI=10.1099/13500872-142-1-191;
RA Ginter A., Williamson E.D., Dessy F., Coppe P., Bullifent H., Howells A.M.,
RA Titball R.W.;
RT "Molecular variation between the alpha-toxins from the type strain (NCTC
RT 8237) and clinical isolates of Clostridium perfringens associated with
RT disease in man and animals.";
RL Microbiology 142:191-198(1996).
RN [8]
RP MUTAGENESIS OF ASP-297; TYR-303; TYR-335; TYR-359 AND ASP-364.
RX PubMed=10931204; DOI=10.1046/j.1432-1327.2000.01588.x;
RA Alape-Giron A., Flores-Diaz M., Guillouard I., Naylor C.E., Titball R.W.,
RA Rucavado A., Lomonte B., Basak A.K., Gutierrez J.M., Cole S.T.,
RA Thelestam M.;
RT "Identification of residues critical for toxicity in Clostridium
RT perfringens phospholipase C, the key toxin in gas gangrene.";
RL Eur. J. Biochem. 267:5191-5197(2000).
RN [9]
RP MUTAGENESIS OF ASP-321; ASP-333 AND LYS-358.
RX PubMed=11147832; DOI=10.1006/abbi.2000.2065;
RA Walker N., Holley J., Naylor C.E., Flores-Diaz M., Alape-Giron A.,
RA Carter G., Carr F.J., Thelestam M., Keyte M., Moss D.S., Basak A.K.,
RA Miller J., Titball R.W.;
RT "Identification of residues in the carboxy-terminal domain of Clostridium
RT perfringens alpha-toxin (phospholipase C) which are required for its
RT biological activities.";
RL Arch. Biochem. Biophys. 384:24-30(2000).
RN [10]
RP MUTAGENESIS OF ASP-297; TYR-359 AND PHE-362.
RX PubMed=11334886; DOI=10.1016/s0014-5793(01)02385-7;
RA Jepson M., Bullifent H.L., Crane D.T., Flores-Diaz M., Alape-Giron A.,
RA Jayasekera P., Lingard B., Moss D.S., Titball R.W.;
RT "Tyrosine 331 and phenylalanine 334 in Clostridium perfringens alpha-toxin
RT are essential for cytotoxic activity.";
RL FEBS Lett. 495:172-177(2001).
RN [11]
RP CHARACTERIZATION.
RX PubMed=2497921; DOI=10.1111/j.1476-5381.1989.tb11931.x;
RA Fujii Y., Sakurai J.;
RT "Contraction of the rat isolated aorta caused by Clostridium perfringens
RT alpha toxin (phospholipase C): evidence for the involvement of arachidonic
RT acid metabolism.";
RL Br. J. Pharmacol. 97:119-124(1989).
RN [12]
RP IMPORTANCE OF ZINC.
RX PubMed=2111259; DOI=10.1111/j.1574-6968.1988.tb03188.x;
RA Titball R.W., Rubidge T.;
RT "The role of histidine residues in the alpha toxin of Clostridium
RT perfringens.";
RL FEMS Microbiol. Lett. 56:261-265(1990).
RN [13]
RP SIMILARITY OF C-TERMINAL DOMAIN TO LIPOXYGENASES AND C-TERMINAL TRUNCATION.
RX PubMed=1902199; DOI=10.1128/iai.59.5.1872-1874.1991;
RA Titball R.W., Leslie D.L., Harvey S., Kelly D.C.;
RT "Hemolytic and sphingomyelinase activities of Clostridium perfringens
RT alpha-toxin are dependent on a domain homologous to that of an enzyme from
RT the human arachidonic acid pathway.";
RL Infect. Immun. 59:1872-1874(1991).
RN [14]
RP REVIEW.
RX PubMed=16887662; DOI=10.1006/anae.1999.0191;
RA Titball R.W., Naylor C.E., Basak A.K.;
RT "The Clostridium perfringens alpha-toxin.";
RL Anaerobe 5:51-64(1999).
RN [15]
RP REVIEW.
RX PubMed=11008117; DOI=10.1016/s1286-4579(00)01281-8;
RA Jepson M., Titball R.W.;
RT "Structure and function of clostridial phospholipases C.";
RL Microbes Infect. 2:1277-1284(2000).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 29-398 OF THE CALCIUM-BOUND CLOSED
RP FORM.
RX PubMed=10610794; DOI=10.1006/jmbi.1999.3279;
RA Naylor C.E., Jepson M., Crane D.T., Titball R.W., Miller J., Basak A.K.,
RA Bolgiano B.;
RT "Characterisation of the calcium-binding C-terminal domain of Clostridium
RT perfringens alpha-toxin.";
RL J. Mol. Biol. 294:757-770(1999).
CC -!- FUNCTION: Bacterial hemolysins are exotoxins that attack blood cell
CC membranes and cause cell rupture. Constitutes an essential virulence
CC factor in gas gangrene. Binds to eukaryotic membranes where it
CC hydrolyzes both phosphatidylcholine and sphingomyelin. The
CC diacylglycerol produced can activate both the arachidonic acid pathway,
CC leading to modulation of the inflammatory response cascade and
CC thrombosis, and protein kinase C, leading to activation of eukaryotic
CC phospholipases and further membrane damage. Acts on human and mouse
CC erythrocytes, but not on rabbit or horse erythrocytes.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 3 Ca(2+) ions per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 3 Zn(2+) ions per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: The protein is composed of 2 domains; the N-terminal domain
CC contains the phospholipase C active site (PLC), in a cleft which is
CC also occupied by the 3 zinc ions. The C-terminal domain is a putative
CC phospholipid-recognition domain, which shows structural homology with
CC phospholipid-binding C2-like domains from a range of eukaryotic
CC proteins. The ability to bind membrane phospholipids in a Ca(2+)
CC dependent manner and toxicity is conferred by this C-terminal domain,
CC which also contributes to the sphingomyelinase activity.
CC -!- BIOTECHNOLOGY: Vaccination of mice with a fragment (residues 275-398)
CC protects them against a subsequent challenge with purified alpha-toxin.
CC -!- MISCELLANEOUS: Two main forms of alpha-toxin can be purified from
CC C.perfringens; a major form with a pI of 5.48, and a minor form with a
CC pI of 5.6. Both are equally active. Variations seen in PLC activity
CC between different strains may be due to transcriptional regulation.
CC -!- MISCELLANEOUS: Mutating residues 303 or 359 of the C.perfringens toxin
CC to match those found in C.bifermentans (301 and 358 respectively)
CC reduces toxicity considerably.
CC -!- SIMILARITY: Belongs to the bacterial zinc-metallophospholipase C
CC family. {ECO:0000255|PROSITE-ProRule:PRU00678}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/PLC/";
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DR EMBL; M24904; AAA23272.1; -; Genomic_DNA.
DR EMBL; X13608; CAA31943.1; -; Genomic_DNA.
DR EMBL; CP000246; ABG84486.1; -; Genomic_DNA.
DR PIR; A30565; A30565.
DR RefSeq; WP_011590041.1; NC_008261.1.
DR PDB; 1QM6; X-ray; 2.50 A; A/B=29-398.
DR PDB; 1QMD; X-ray; 2.20 A; A/B=29-398.
DR PDB; 2WXT; X-ray; 2.00 A; A=29-398.
DR PDB; 2WXU; X-ray; 1.80 A; A=29-398.
DR PDB; 2WY6; X-ray; 3.20 A; A/B/C=29-398.
DR PDBsum; 1QM6; -.
DR PDBsum; 1QMD; -.
DR PDBsum; 2WXT; -.
DR PDBsum; 2WXU; -.
DR PDBsum; 2WY6; -.
DR AlphaFoldDB; Q0TV31; -.
DR SMR; Q0TV31; -.
DR STRING; 195103.CPF_0042; -.
DR PRIDE; Q0TV31; -.
DR EnsemblBacteria; ABG84486; ABG84486; CPF_0042.
DR GeneID; 29569865; -.
DR KEGG; cpf:CPF_0042; -.
DR eggNOG; ENOG5033QPJ; Bacteria.
DR HOGENOM; CLU_690198_0_0_9; -.
DR OMA; DHFWDPD; -.
DR OrthoDB; 753730at2; -.
DR EvolutionaryTrace; Q0TV31; -.
DR Proteomes; UP000001823; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IDA:CACAO.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044179; P:hemolysis in another organism; IDA:CACAO.
DR Gene3D; 1.10.575.10; -; 1.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
DR InterPro; IPR029002; PLPC/GPLD1.
DR InterPro; IPR001531; Zn_PLipaseC.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF00882; Zn_dep_PLPC; 1.
DR PRINTS; PR00479; PRPHPHLPASEC.
DR SMART; SM00770; Zn_dep_PLPC; 1.
DR SUPFAM; SSF48537; SSF48537; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS00384; PROKAR_ZN_DEPEND_PLPC_1; 1.
DR PROSITE; PS51346; PROKAR_ZN_DEPEND_PLPC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytolysis; Direct protein sequencing; Hemolysis;
KW Hydrolase; Metal-binding; Secreted; Signal; Toxin; Virulence; Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:2536355,
FT ECO:0000269|PubMed:2540749"
FT CHAIN 29..398
FT /note="Phospholipase C"
FT /id="PRO_0000259456"
FT DOMAIN 29..278
FT /note="Zn-dependent PLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT DOMAIN 284..398
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 275..283
FT /note="Linker"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT MUTAGEN 278..398
FT /note="Missing: Loss of sphingomyelinase, hemolytic
FT activity and lethality."
FT /evidence="ECO:0000269|PubMed:7868589"
FT MUTAGEN 297
FT /note="D->Y: Binds less Ca(2+), small decrease in PLC,
FT sphingomyelinase and myotoxicity, increased hemolytic and
FT cytotoxic activities."
FT /evidence="ECO:0000269|PubMed:10931204,
FT ECO:0000269|PubMed:11334886"
FT MUTAGEN 303
FT /note="Y->F,N: Increased dependence of PLC on Ca(2+).
FT Dramatically decreases hemolytic, cytotoxic and myotoxic
FT activities."
FT /evidence="ECO:0000269|PubMed:10931204"
FT MUTAGEN 321
FT /note="D->S: Reduces affinity for Ca(2+), decreases toxin
FT activity."
FT /evidence="ECO:0000269|PubMed:11147832"
FT MUTAGEN 333
FT /note="D->G: Decreases toxin activity in vivo and against
FT aggregated substrates in vitro. May destabilize
FT interactions between the N and C-terminal domains."
FT /evidence="ECO:0000269|PubMed:11147832"
FT MUTAGEN 335
FT /note="Y->F: Dramatically decreases hemolytic and cytotoxic
FT activities."
FT /evidence="ECO:0000269|PubMed:10931204"
FT MUTAGEN 358
FT /note="K->E: Decreases toxin activity in vivo and against
FT aggregated substrates in vitro."
FT /evidence="ECO:0000269|PubMed:11147832"
FT MUTAGEN 359
FT /note="Y->F,L: Dramatically decreases hemolytic and
FT cytotoxic activities."
FT /evidence="ECO:0000269|PubMed:10931204,
FT ECO:0000269|PubMed:11334886"
FT MUTAGEN 362
FT /note="F->I: Dramatically decreases sphingomyelinase,
FT cytotoxicity and hemolytic and myotoxic activities."
FT /evidence="ECO:0000269|PubMed:11334886"
FT MUTAGEN 364
FT /note="D->N: Increased dependence of PLC on Ca(2+).
FT Dramatically decreases hemolytic, cytotoxic and myotoxic
FT activities."
FT /evidence="ECO:0000269|PubMed:10931204"
FT CONFLICT 17
FT /note="S -> T (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2WXU"
FT HELIX 38..53
FT /evidence="ECO:0007829|PDB:2WXU"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:2WXU"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:2WXU"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2WXU"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:2WXU"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:1QMD"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:1QMD"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2WXU"
FT HELIX 122..138
FT /evidence="ECO:0007829|PDB:2WXU"
FT HELIX 142..159
FT /evidence="ECO:0007829|PDB:2WXU"
FT TURN 163..167
FT /evidence="ECO:0007829|PDB:2WXU"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:2WXU"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:2WXU"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:2WXU"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:2WXU"
FT HELIX 213..234
FT /evidence="ECO:0007829|PDB:2WXU"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:2WY6"
FT HELIX 242..273
FT /evidence="ECO:0007829|PDB:2WXU"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:2WXT"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:2WXU"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:2WXU"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:2WXU"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:2WXU"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:2WXU"
FT STRAND 349..357
FT /evidence="ECO:0007829|PDB:2WXU"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:2WXU"
FT STRAND 368..375
FT /evidence="ECO:0007829|PDB:2WXU"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:2WXU"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:2WXU"
SQ SEQUENCE 398 AA; 45476 MW; 4A36E7E2A7139724 CRC64;
MKRKICKALI CAALATSLWA GASTKVYAWD GKIDGTGTHA MIVTQGVSIL ENDLSKNEPE
SVRKNLEILK ENMHELQLGS TYPDYDKNAY DLYQDHFWDP DTDNNFSKDN SWYLAYSIPD
TGESQIRKFS ALARYEWQRG NYKQATFYLG EAMHYFGDID TPYHPANVTA VDSAGHVKFE
TFAEERKEQY KINTAGCKTN EAFYTDILKN KDFNAWSKEY ARGFAKTGKS IYYSHASMSH
SWDDWDYAAK VTLANSQKGT AGYIYRFLHD VSEGNDPSVG KNVKELVAYI STSGEKDAGT
DDYMYFGIKT KDGKTQEWEM DNPGNDFMTG SKDTYTFKLK DENLKIDDIQ NMWIRKRKYT
AFSDAYKPEN IKIIANGKVV VDKDINEWIS GNSTYNIK
