YENC2_YERET
ID YENC2_YERET Reviewed; 970 AA.
AC B6A882;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Toxin subunit YenC2 {ECO:0000303|PubMed:21278295};
GN Name=yenC2 {ECO:0000303|PubMed:21278295};
OS Yersinia entomophaga.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=935293;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-1678 / DSM 22339 / MH96;
RX PubMed=21278295; DOI=10.1128/jb.01044-10;
RA Hurst M.R., Jones S.A., Binglin T., Harper L.A., Jackson T.A., Glare T.R.;
RT "The main virulence determinant of Yersinia entomophaga MH96 is a broad-
RT host-range toxin complex active against insects.";
RL J. Bacteriol. 193:1966-1980(2011).
RN [2]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC BAA-1678 / DSM 22339 / MH96;
RX PubMed=22158901; DOI=10.1073/pnas.1111155108;
RA Landsberg M.J., Jones S.A., Rothnagel R., Busby J.N., Marshall S.D.,
RA Simpson R.M., Lott J.S., Hankamer B., Hurst M.R.;
RT "3D structure of the Yersinia entomophaga toxin complex and implications
RT for insecticidal activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20544-20549(2011).
RN [3] {ECO:0007744|PDB:4IGL}
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1-690 IN COMPLEX WITH YENB,
RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ARG-650; ASP-663 AND ASP-686.
RC STRAIN=ATCC BAA-1678 / DSM 22339 / MH96;
RX PubMed=23913273; DOI=10.1038/nature12465;
RA Busby J.N., Panjikar S., Landsberg M.J., Hurst M.R., Lott J.S.;
RT "The BC component of ABC toxins is an RHS-repeat-containing protein
RT encapsulation device.";
RL Nature 501:547-550(2013).
CC -!- FUNCTION: Part of an orally active toxin complex (TC) with strong
CC insecticidal effects on larvae of the Coleoptera Costelytra zealandica,
CC Acrossidius tasmania and Adoryphorus couloni and some Lepidoptera
CC larvae (PubMed:21278295). The TC has an endochitinase activity
CC (PubMed:21278295) (Probable). {ECO:0000269|PubMed:21278295,
CC ECO:0000305|PubMed:22158901}.
CC -!- ACTIVITY REGULATION: Toxin complex is secreted when grown at 25 degrees
CC Celsius or less; at higher temperatures the proteins are present
CC intracellularly but not secreted. {ECO:0000269|PubMed:21278295}.
CC -!- SUBUNIT: Semipurified toxin complex consists of at least YenA1-YenA2-
CC YenB-YenC1-YenC2-Chi1-Chi2 (PubMed:21278295). YenB and the N-terminus
CC of YenC2 form a large hollow shell of beta-strands (PubMed:23913273).
CC The shell is closed at both ends, within which the C-terminus of YenC2
CC is probably found (PubMed:23913273). The C-terminal region dissociates
CC from the YenB-YenC2 complex at pH 4.5 but not 7.5 (PubMed:23913273).
CC The Yen-TC:K9 subcomplex is about 26 nm tall and 22 nm in diameter with
CC 5-fold symmetry and 5 copies of YenA1, YenA2, Chi1 and Chi2; the
CC chitinase subunits may be solvent accessible on the exterior the
CC complex (PubMed:22158901). The Yen-TC:K9 subcomplex has no insecticidal
CC activity (PubMed:22158901). The native complex with additional YenB,
CC YenC1 and YenC2 subunits is 16 nm taller and is insecticidal; the
CC toxicity-conferring subunits are present at about 1 copy each
CC (PubMed:22158901). {ECO:0000269|PubMed:21278295,
CC ECO:0000269|PubMed:22158901, ECO:0000269|PubMed:23913273}.
CC -!- INTERACTION:
CC B6A882; B6A880: yenB; NbExp=3; IntAct=EBI-16067263, EBI-16067250;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21278295}.
CC Note=Secreted when grown at 25 degrees Celsius or less, but not when
CC grown at 30 or 37 degrees Celsius. {ECO:0000269|PubMed:21278295}.
CC -!- DOMAIN: Residues 610-690 form a beta-strand plug which closes one end
CC of the shell; the other end of the shell is closed by the 5-bladed
CC beta-propeller domain in YenB. {ECO:0000269|PubMed:23913273}.
CC -!- DISRUPTION PHENOTYPE: A double yenC1-yenC2 deletion is no longer
CC pathogenic in C.zealandica larvae. {ECO:0000269|PubMed:21278295}.
CC -!- SIMILARITY: Belongs to the RHS family. {ECO:0000305|PubMed:23913273}.
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DR EMBL; DQ400808; ABG33864.1; -; Genomic_DNA.
DR PDB; 4IGL; X-ray; 2.49 A; B/D=1-690.
DR PDBsum; 4IGL; -.
DR AlphaFoldDB; B6A882; -.
DR SMR; B6A882; -.
DR DIP; DIP-60598N; -.
DR IntAct; B6A882; 1.
DR PATRIC; fig|935293.3.peg.811; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR022385; Rhs_assc_core.
DR InterPro; IPR041508; TcC-like_repeat.
DR InterPro; IPR025968; YwqJ_deaminase.
DR Pfam; PF18807; TTc_toxin_rep; 1.
DR Pfam; PF14431; YwqJ-deaminase; 1.
DR TIGRFAMs; TIGR03696; Rhs_assc_core; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Repeat; Secreted; Virulence.
FT CHAIN 1..970
FT /note="Toxin subunit YenC2"
FT /id="PRO_0000445775"
FT REPEAT 168..182
FT /note="RHS 1"
FT /evidence="ECO:0000305|PubMed:23913273"
FT REPEAT 297..311
FT /note="RHS 2"
FT /evidence="ECO:0000305|PubMed:23913273"
FT REPEAT 329..343
FT /note="RHS 3"
FT /evidence="ECO:0000305|PubMed:23913273"
FT REPEAT 361..375
FT /note="RHS 4"
FT /evidence="ECO:0000305|PubMed:23913273"
FT REPEAT 408..422
FT /note="RHS 5"
FT /evidence="ECO:0000305|PubMed:23913273"
FT REPEAT 500..514
FT /note="RHS 6"
FT /evidence="ECO:0000305|PubMed:23913273"
FT REPEAT 580..594
FT /note="RHS 7"
FT /evidence="ECO:0000305|PubMed:23913273"
FT REPEAT 606..620
FT /note="RHS 8"
FT /evidence="ECO:0000305|PubMed:23913273"
FT REPEAT 640..654
FT /note="RHS 9"
FT /evidence="ECO:0000305|PubMed:23913273"
FT REGION 610..690
FT /note="RHS-repeat associated core domain"
FT /evidence="ECO:0000305"
FT REGION 849..950
FT /note="Deaminase domain"
FT /evidence="ECO:0000305"
FT SITE 690..691
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000305|PubMed:23913273"
FT MUTAGEN 650
FT /note="R->A: Loss of auto-proteolytic activity."
FT /evidence="ECO:0000269|PubMed:23913273"
FT MUTAGEN 663
FT /note="D->N: Loss of auto-proteolytic activity."
FT /evidence="ECO:0000269|PubMed:23913273"
FT MUTAGEN 686
FT /note="D->N: Loss of auto-proteolytic activity."
FT /evidence="ECO:0000269|PubMed:23913273"
FT TURN 5..8
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:4IGL"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:4IGL"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:4IGL"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:4IGL"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 177..186
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:4IGL"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:4IGL"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:4IGL"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 327..336
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 374..381
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 407..415
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 421..427
FT /evidence="ECO:0007829|PDB:4IGL"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 435..441
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:4IGL"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:4IGL"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:4IGL"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:4IGL"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 513..520
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 527..534
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 537..543
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 550..557
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 564..572
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 580..587
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 604..610
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 616..622
FT /evidence="ECO:0007829|PDB:4IGL"
FT HELIX 625..629
FT /evidence="ECO:0007829|PDB:4IGL"
FT HELIX 634..636
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 648..652
FT /evidence="ECO:0007829|PDB:4IGL"
FT TURN 654..656
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 657..661
FT /evidence="ECO:0007829|PDB:4IGL"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 673..675
FT /evidence="ECO:0007829|PDB:4IGL"
FT HELIX 677..679
FT /evidence="ECO:0007829|PDB:4IGL"
FT TURN 681..683
FT /evidence="ECO:0007829|PDB:4IGL"
SQ SEQUENCE 970 AA; 107447 MW; 37FBE004CB1F7C7C CRC64;
MDIQLFSKTP SVTVFDNRGL SVRDIAYRRH PDTPKVTEEC ITYHQFDFRG FLAQSLDPRL
NHKEVTNFSY LTDLNGNIIY TQSVDAGNTL VLNDTEGRSV IAMTNISRGE NGKDDLSLAV
TRTFQYENAP LPGRPLSVTE QVNGENARIT EHFVYAGNTP QEKNLNLAGQ CVSYYDAAGL
IQTDSVSLTG KPLSVSRKLL KNLDDTNILA DWQGNDTSAW NSLLATEIYT TVTRTDAAGA
VLTTIDAVGN QQRVAFDIAG QLSASWLTLK GGQEQVIIKV LTYSAAGQKL REEGGNGVVT
TYTYEAETQR LIGIKTERPN GHAAGAKVLQ DLRYEYDPVG NVLSITNDAE ETRFWRNQKV
VPENAYRYDS LYQLVSASGR EVAGAGQQGS DLPSPLVPLP SDSSVYTNYT RTYTYDSAGN
LMRIRHSAPA TNNNYTLNIT VSERSNRGVM SSLTENPADV DALFTASGSQ KCLQQGQSLI
WTPRGELRTV LLVARGETAD DSESYRYDGS SQRILKISSQ QTNHSARVQR ALYLPGLEWR
TMTGGVAEAE NLQVICIGEA GRAQVRVLHW ESGKPDGIIN DQIRWSYDNL TCSSGLEVDG
DGLVISMEEY YPYGGTAVWA ARSHIETAYK TVRYSGKERD ATGLYYYGFR YYQPWAGRWL
SADPAGTVDG LNLYRMVRNN PLRLTDPDGM APLDWLDLDT TNASRDIVKA IYQLNQIDGP
HRGVRDTYQR MTESTGMILQ ETLNNEAVLK GIKQKDKEKK SRGMKFTNSK LKTYAAHAGV
LNTLQPDPVY KDGFLNLPGS LGNKNTFPGV ELIEDKVKPS LSQYHPDKLG KSQRWKPESS
LGYYRVADTE AFITGIRSQY KSSGTDLHAV VEGRIRDHLL ANNNVLPKMA GIAGLHAEVQ
ALNYIISNPD IEGGNAERLN GSYIFTQRLV GDVNQDFPAC YNCSGIISGL ENVMTGRVNN
DVRLKRRKSF
