Descriptions

Mosquitocidal toxin (MTX) from Bacillus sphaericus is a protein produced during the vegetative growth phase of the bacterium. It exhibits strong toxicity against mosquito larvae, and its ADP-ribosyltransferase activity is essential for its cytotoxicity. The autoinhibition of MTX is mediated by the putative binding and autoinhibiting domain that consists of four ricin-like domains (domain I-IV). Cleavages by trypsin occur after Lys262 and by chymotrypsin after Phe264 increase the enzymatic activity of MTX, thereby relieving the autoinhibition of MTX.

Autoinhibitory domains (AIDs)

Target domain

30-264 (Enzyme domain)

Relief mechanism

Cleavage

Assay

Structural analysis, Split protein assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q75UG7

Entry ID Method Resolution Chain Position Source
AF-Q75UG7-F1 Predicted AlphaFoldDB

No variants for Q75UG7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q75UG7

No associated diseases with Q75UG7

3 regional properties for Q75UG7

Type Name Position InterPro Accession
domain Ricin B, lectin domain 298 - 579 IPR000772-1
domain Ricin B, lectin domain 591 - 720 IPR000772-2
domain Ricin B, lectin domain 729 - 862 IPR000772-3

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAIKKVLKII LAIIIIISCQ LPLNQKTVYA SPNSPKDNTW IQAASLTWLM DMSSLLYQLI
70 80 90 100 110 120
STRIPSFASP NGLYMREQTI DSNTGQIQID NEHRLLRWDR RPPNDIFLNG FIPRVTNQNL
130 140 150 160 170 180
SPVEDTHLLN YLRTNSPSIF VSTTRARYNN LGLEITPWTP HSANNNIIYR YEIFAPGGID
190 200 210 220 230 240
INASLSRNHN PFPNEDEITF PGGIRPEFIR STYEYHNGEI VRIWINPNFI NPSTLNDVSG
250 260 270 280 290 300
PSNISKVFWH ENHSEGNNMD SKGFILDLDY NQDFDMFAPN GEIPNNNLLN NNSLNVIQNS
310 320 330 340 350 360
EYQIKNKKDR NIVVTLDSDY GGSPVESYKN FGFENQKWNI KYDSKKNAYK IYNRETPTLL
370 380 390 400 410 420
LSWNSNSSNG EQVIRGYTES GSNNQYWTIE KNVNGFYKFR NLSDPSKILD LKDGNTLNKT
430 440 450 460 470 480
PLVVSSENSS SSQEWLIEKT NYQTVKDGTY QVSSKLNENK VIEQISTNKI HIFSNSDKEN
490 500 510 520 530 540
QVWNLIYNPI LKAYKIKSLK YPNYSLAWDS NNTRTIVAAT GDYNDQYWLI ERNEDNTYII
550 560 570 580 590 600
RNYENRKIVL DLSNGSTTDG NGLLGFEFHG GINQRWIIKP FSFNSIQDGI YQFMTVINQD
610 620 630 640 650 660
LIADLTTNNY TIATKTNNYS SNQKWTVTYN DKKRAYKIRN LQHAHLSLAW DSNHSDKIFG
670 680 690 700 710 720
ATGDYDDQYW IPILQTDGSF IFRNYKNPNK IFGTNGQPIN DIPLKAQDVT GQNNQKWYLR
730 740 750 760 770 780
HLNSSNNFTG YFNISSKKNF NKIITMNSNK TQAVIFDNIG INNQSWKLKY NDNKNAYQIH
790 800 810 820 830 840
ILDNFLYFQG GHNIVATMQN VTNDDLRSYW YVEYNFNKDG FIIRNAFDTS YVLDVFQGNF
850 860
ANNTPIITYQ NYLNDNQLWN FIPSLGVEPR