YENB_YERET
ID YENB_YERET Reviewed; 1487 AA.
AC B6A880;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Toxin subunit YenB {ECO:0000303|PubMed:21278295};
GN Name=yenB {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], PROTEIN SEQUENCE OF 1-9, IDENTIFICATION
RP BY MASS SPECTROMETRY, FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND 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) IN COMPLEX WITH YENC2, AND DOMAIN.
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).
RN [4] {ECO:0007744|PDB:5KIS}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RA Busby J.N., Hurst M.R.H., Lott J.S.;
RT "Structure of a new BC complex from Yersinia entomophaga.";
RL Submitted (JUN-2016) to the PDB data bank.
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, PubMed:22158901). The TC has an endochitinase
CC activity (PubMed:21278295) (Probable). {ECO:0000269|PubMed:21278295,
CC ECO:0000269|PubMed:22158901, 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 Yen-TC:K9 subcomplex is about
CC 26 nm tall and 22 nm in diameter with 5-fold symmetry and 5 copies of
CC YenA1, YenA2, Chi1 and Chi2; the chitinase subunits may be solvent
CC accessible on the exterior the complex (PubMed:22158901). The Yen-TC:K9
CC subcomplex has no insecticidal activity (PubMed:22158901). The native
CC complex with additional YenB, YenC1 and YenC2 subunits is 16 nm taller
CC and is insecticidal; the toxicity-conferring subunits are present at
CC about 1 copy each (PubMed:22158901). {ECO:0000269|PubMed:21278295,
CC ECO:0000269|PubMed:22158901, ECO:0000269|PubMed:23913273}.
CC -!- INTERACTION:
CC B6A880; B6A882: yenC2; NbExp=3; IntAct=EBI-16067250, EBI-16067263;
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 389-698 form a 5-bladed beta-propeller domain which
CC closes one end of the shell; the other end of the shell is closed by
CC the RHS repeat-associated core domain in YenC2.
CC {ECO:0000269|PubMed:23913273}.
CC -!- DISRUPTION PHENOTYPE: Cells with a disrupted yenA1-yenA2-chi2-yenB-
CC yenC1-yenC2 locus are no longer pathogenic in C.zealandica larvae.
CC {ECO:0000269|PubMed:21278295}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the SpvB family.
CC {ECO:0000305}.
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DR EMBL; DQ400808; ABG33866.1; -; Genomic_DNA.
DR RefSeq; WP_064513231.1; NZ_MWTM01000006.1.
DR PDB; 4IGL; X-ray; 2.49 A; A/C=1-1487.
DR PDB; 5KIS; X-ray; 2.40 A; A=1-1487.
DR PDBsum; 4IGL; -.
DR PDBsum; 5KIS; -.
DR AlphaFoldDB; B6A880; -.
DR SMR; B6A880; -.
DR DIP; DIP-60597N; -.
DR IntAct; B6A880; 1.
DR STRING; 935293.PL78_03760; -.
DR PATRIC; fig|935293.3.peg.809; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR003284; Sal_SpvB.
DR InterPro; IPR022044; TcdB_toxin_mid/C.
DR InterPro; IPR022045; TcdB_toxin_mid/N.
DR Pfam; PF03534; SpvB; 1.
DR Pfam; PF12255; TcdB_toxin_midC; 1.
DR Pfam; PF12256; TcdB_toxin_midN; 1.
DR PRINTS; PR01341; SALSPVBPROT.
DR SUPFAM; SSF69318; SSF69318; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Secreted; Virulence.
FT CHAIN 1..1487
FT /note="Toxin subunit YenB"
FT /id="PRO_0000445773"
FT REGION 27..378
FT /note="SpvB-like domain"
FT /evidence="ECO:0000269|PubMed:23913273"
FT REGION 389..698
FT /note="5-bladed beta-propeller domain"
FT /evidence="ECO:0000269|PubMed:23913273"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 125..140
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 190..200
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 234..245
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 336..346
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 353..362
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:4IGL"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 416..422
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 426..433
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 442..449
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 510..516
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 521..527
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 563..569
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 571..576
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 578..583
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 586..590
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 592..594
FT /evidence="ECO:0007829|PDB:5KIS"
FT TURN 611..613
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 616..618
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 619..622
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 624..629
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 631..635
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 637..643
FT /evidence="ECO:0007829|PDB:5KIS"
FT TURN 647..649
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 655..658
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 670..674
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 678..681
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 683..687
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 689..693
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 708..712
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 714..725
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 726..739
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 753..762
FT /evidence="ECO:0007829|PDB:5KIS"
FT TURN 763..765
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 768..781
FT /evidence="ECO:0007829|PDB:5KIS"
FT TURN 782..785
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 786..800
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 805..808
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 813..819
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 824..827
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 831..833
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 848..853
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 860..863
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 868..876
FT /evidence="ECO:0007829|PDB:5KIS"
FT TURN 877..880
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 882..889
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 891..893
FT /evidence="ECO:0007829|PDB:5KIS"
FT TURN 894..897
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 900..912
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 917..919
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 921..933
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 938..940
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 942..951
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 957..964
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 984..987
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 991..994
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 996..1008
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1015..1029
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 1031..1033
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 1041..1045
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1058..1071
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1080..1089
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 1093..1097
FT /evidence="ECO:0007829|PDB:5KIS"
FT TURN 1098..1100
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 1103..1112
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1116..1118
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1130..1135
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1137..1140
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 1143..1145
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1149..1154
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1161..1165
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1169..1176
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1182..1187
FT /evidence="ECO:0007829|PDB:5KIS"
FT TURN 1189..1191
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1194..1198
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1204..1209
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1215..1224
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1227..1231
FT /evidence="ECO:0007829|PDB:5KIS"
FT TURN 1234..1236
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 1245..1249
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1258..1264
FT /evidence="ECO:0007829|PDB:5KIS"
FT TURN 1265..1268
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 1274..1281
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 1286..1293
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1301..1303
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 1305..1315
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 1319..1327
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1334..1342
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1351..1358
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1364..1370
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1373..1377
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1383..1385
FT /evidence="ECO:0007829|PDB:4IGL"
FT STRAND 1391..1393
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1396..1400
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1402..1405
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1408..1410
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1416..1420
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1423..1426
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 1433..1439
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1442..1447
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1453..1457
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1463..1468
FT /evidence="ECO:0007829|PDB:5KIS"
FT STRAND 1470..1476
FT /evidence="ECO:0007829|PDB:5KIS"
FT HELIX 1478..1482
FT /evidence="ECO:0007829|PDB:5KIS"
SQ SEQUENCE 1487 AA; 166998 MW; B5B723F6B8C777F1 CRC64;
MQNSQEMAIT TLSLPKGGGA INGMGESVGQ AGPDGMVTFS IPLPFSAGRG VAPALSLSYS
SGAGNGPFGM GWQCSAMSIS RRTQKGVPQY NEDDEFLSPS GEVMAIALND SGFEDVRTAN
RLQGIPLPFS YKVTRYQPRL IQDFIKIEYW QPVKQTDGTP FWIIYSPDGQ THILGKNSHS
RVANAENPSQ IASWLLEETV TPTGEHIYYQ YSGENQVNCT DAEIALHPQD SAQRYLARID
YGNISPQASL FVLDEELPNL TQWLFHLVFD YGERDISINK IPTFEGGTTG WLARPDMFSR
YDFGIEIRNR RLCHQVLGFH RLEALNDRDV TDEIPVLVNR LTLDYDLNNS VSTLVAVRQV
AYETDGSPIT QPPLEFDYQR FDTGSIPGWQ EMPQLEAFNG YQPYQMIDLY GEGTPGILYQ
ETPGAWWYKS PQRQIGGDSN AVTYGAMKAL PKIPRLQEGA TLMDINGDGR LDWVITSAGV
RGFHSIHSTG EWTHFTPLNT LPTEYFHPKA QLADLVGAGL SDLVLIGPKS VRLYANQQGN
WAPAQDVTQA ENVSLPVIGI DSRQLVAFAD MLGSGQQHLV EITADSVKCW PNMGHGRFGQ
PLTLEGFSQP QTSFNPDRVF LADIDGSGTN DIIYAHSECL EIYLNESGNR FSKPISLLLP
DGVNFDNTCQ LQAADIQGLG IASLVMTVPH MSPTHWRCDL ALNKPWLLNV MNNNRGAETC
LFYRSSAQFW LDEKQLVEAA GQQPECHLPF PMHLHWRSEI FDEITGNRLT QEQEYAHGSW
DGQEREFRGF GRLIQRDTDG FAQGTVDIPT HPSRTVSWFA TGIPEIDTTL SAEFWRGDDQ
AFSPFSPRFT RWENDSEAGS DVAFIPSEHD AFWLNRAMKG QLLRSELYGD DGTPEAEIPY
SVTEMRHQVR ALPTTDATVP SAWCSTIETR SYQYQRVAAD PQCSQQVVIK ADRYGSPLLS
VAINYPRRKK PEKSPYPDDL PETLFDSSYD TQQQQLHLTK QQQNYFHLTN DDNWLLGLPK
EQRNDGYQYD QERAPANGFT LETLIASNSL IGSNQPFTYL GQSRVAYQGG VDEQPSLQAL
VAYGETAILD EKTLQAFVGV LDSKTRDELL FSAGYQLAPR LFRVESEPDV WVARQGYSEF
GDYSQFWRPL SQRSTLLTGK TTLKWDKHYC VVIETQDAAQ LVTQARYDYR FLTPYSLTDA
NDNQHYVVLN PFGEVIASRF WGTEAGKDAG YSTPQAKPFV VPATIEAALA LSPGIPVAHC
AIFEPESWMQ KLTQHDVSER MADNGTLWNA LLQARFVTED GYVCALGRRR WMARHGLSVL
MLTLLAEIPR TPPHSLTITT DRYDSDDQQQ LRQRILFSDG FGRLLQSAQR VEAGESWQRS
EDSSLVVNVS GTPALVVTDN RWAVSGRTEY DGKGQGIRVY QPYFLDDWRY LSDDSARTDL
FADTHIYDPL GREYQVITAK GYRRERQYTP WFVVNQDEND TAANLAI
