Reviewed, UniProtKB/Swiss-Prot P30995 (BXE_CLOBU)

Names and origin

Protein names	Recommended name:     Botulinum neurotoxin type E       Short name=BoNT/E     EC=3.4.24.69 Alternative name(s):     Bontoxilysin-E Cleaved into the following 2 chains:     1- Recommended name:             Botulinum neurotoxin E light chain     2- Recommended name:             Botulinum neurotoxin E heavy chain
Organism	Clostridium butyricum
Taxonomic identifier	1492 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	1251 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Botulinum toxin acts by inhibiting neurotransmitter release. It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase.
Catalytic activity	Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Disulfide-linked heterodimer of a light chain (L) and a heavy chain (H). The light chain has the pharmacological activity, while the N- and C-terminal of the heavy chain mediate channel formation and toxin binding, respectively.
Subcellular location	Botulinum neurotoxin E light chain: Secreted. Host cytoplasm › host cytosol. Botulinum neurotoxin E heavy chain: Secreted. Host cell junction › host synapse › host presynaptic cell membrane Potential.
Miscellaneous	There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C1, D, E, F, and G.
Sequence similarities	Belongs to the peptidase M27 family.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cytoplasm Membrane Secreted Synapse
Domain	Transmembrane
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Neurotoxin Protease Toxin
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	inhibition of neurotransmitter uptake Inferred from electronic annotation. Source: InterPro pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW synapse Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro toxin receptor binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 422	421	Botulinum neurotoxin E light chain		PRO_0000029223
	Chain	423 – 1251	829	Botulinum neurotoxin E heavy chain		PRO_0000029224
Sites
	Active site	213	1	By similarity
	Metal binding	212	1	Zinc; catalytic By similarity
	Metal binding	216	1	Zinc; catalytic By similarity
Amino acid modifications
	Disulfide bond	412 ↔ 426		Interchain (between light and heavy chains) Probable
Experimental info
	Sequence conflict	230	1	K → M in CAA37321. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P30995-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E8D7F180E9863581	FASTA	1,251	143,397
	10 20 30 40 50 60 MPTINSFNYN DPVNNRTILY IKPGGCQQFY KSFNIMKNIW IIPERNVIGT IPQDFLPPTS 70 80 90 100 110 120 LKNGDSSYYD PNYLQSDQEK DKFLKIVTKI FNRINDNLSG RILLEELSKA NPYLGNDNTP 130 140 150 160 170 180 DGDFIINDAS AVPIQFSNGS QSILLPNVII MGAEPDLFET NSSNISLRNN YMPSNHGFGS 190 200 210 220 230 240 IAIVTFSPEY SFRFKDNSMN EFIQDPALTL MHELIHSLHG LYGAKGITTK YTITQKQNPL 250 260 270 280 290 300 ITNIRGTNIE EFLTFGGTDL NIITSAQSND IYTNLLADYK KIASKLSKVQ VSNPLLNPYK 310 320 330 340 350 360 DVFEAKYGLD KDASGIYSVN INKFNDIFKK LYSFTEFDLA TKFQVKCRQT YIGQYKYFKL 370 380 390 400 410 420 SNLLNDSIYN ISEGYNINNL KVNFRGQNAN LNPRIITPIT GRGLVKKIIR FCKNIVSVKG 430 440 450 460 470 480 IRKSICIEIN NGELFFVASE NSYNDDNINT PKEIDDTVTS NNNYENDLDQ VILNFNSESA 490 500 510 520 530 540 PGLSDEKLNL TIQNDAYIPK YDSNGTSDIE QHDVNELNVF FYLDAQKVPE GENNVNLTSS 550 560 570 580 590 600 IDTALLEQPK IYTFFSSEFI NNVNKPVQAA LFVGWIQQVL VDFTTEANQK STVDKIADIS 610 620 630 640 650 660 IVVPYIGLAL NIGNEAQKGN FKDALELLGA GILLEFEPEL LIPTILVFTI KSFLGSSDNK 670 680 690 700 710 720 NKVIKAINNA LKERDEKWKE VYSFIVSNWM TKINTQFNKR KEQMYQALQN QVNALKAIIE 730 740 750 760 770 780 SKYNSYTLEE KNELTNKYDI EQIENELNQK VSIAMNNIDR FLTESSISYL MKLINEVKIN 790 800 810 820 830 840 KLREYDENVK TYLLDYIIKH GSILGESQQE LNSMVIDTLN NSIPFKLSSY TDDKILISYF 850 860 870 880 890 900 NKFFKRIKSS SVLNMRYKND KYVDTSGYDS NININGDVYK YPTNKNQFGI YNDKLSEVNI 910 920 930 940 950 960 SQNDYIIYDN KYKNFSISFW VRIPNYDNKI VNVNNEYTII NCMRDNNSGW KVSLNHNEII 970 980 990 1000 1010 1020 WTLQDNSGIN QKLAFNYGNA NGISDYINKW IFVTITNDRL GDSKLYINGN LIDKKSILNL 1030 1040 1050 1060 1070 1080 GNIHVSDNIL FKIVNCSYTR YIGIRYFNIF DKELDETEIQ TLYNNEPNAN ILKDFWGNYL 1090 1100 1110 1120 1130 1140 LYDKEYYLLN VLKPNNFINR RTDSTLSINN IRSTILLANR LYSGIKVKIQ RVNNSSTNDN 1150 1160 1170 1180 1190 1200 LVRKNDQVYI NFVASKTHLL PLYADTATTN KEKTIKISSS GNRFNQVVVM NSVGNCTMNF 1210 1220 1230 1240 1250 KNNNGNNIGL LGFKADTVVA STWYYTHMRD NTNSNGFFWN FISEEHGWQE K

References

[1]	"Sequences of the botulinal neurotoxin E derived from Clostridium botulinum type E (strain Beluga) and Clostridium butyricum (strains ATCC 43181 and ATCC 43755)." Poulet S., Hauser D., Quanz M., Niemann H., Popoff M.R. Biochem. Biophys. Res. Commun. 183:107-113(1992) [PubMed: 1543481] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43181 and ATCC 43755.
[2]	"Cloning of a DNA fragment encoding the 5'-terminus of the botulinum type E toxin gene from Clostridium butyricum strain BL6340." Fujii N., Kimura K., Murakami T., Indoh T., Tsuzuki K., Yokosawa N., Yashiki T., Oguma K. J. Gen. Microbiol. 137:519-525(1991) [PubMed: 2033376] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252. Strain: BL6340.
[3]	"Neurotoxin type E from Clostridium botulinum and C. butyricum; partial sequence and comparison." Gimenez J., Foley J., Dasgupta B.R. FASEB J. 2:A1750-A1750(1988) Cited for: PROTEIN SEQUENCE OF 2-49. Strain: 5262.

Web resources

BotDB - A Database Resource for Clostridial Neurotoxins

Cross-references

Sequence databases
EMBLGenBankDDBJ	X62088 Genomic DNA. Translation: CAA43998.1. X53180 Genomic DNA. Translation: CAA37321.1.
PIR	JH0256.
3D structure databases
HSSP	HSSP built from PDB template 1E1H based on UniProtKB Q45894.
SMR	P30995. Positions 2-412.
ModBase	Search...
Protein family/group databases
MEROPS	M27.002.
Enzyme and pathway databases
BRENDA	3.4.24.69. 1230.
Family and domain databases
InterPro	IPR013320. ConA-like_subgrp. IPR006025. Pept_M_Zn_BS. IPR000395. Peptidase_M27. IPR013104. Toxin_rcpt_bd_C. IPR012928. Toxin_rcpt_bd_N. IPR012500. Toxin_trans. [Graphical view]
Gene3D	G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit. G3DSA:3.90.1240.10. Peptidase_M27. 1 hit.
Pfam	PF01742. Peptidase_M27. 1 hit. PF07951. Toxin_R_bind_C. 1 hit. PF07953. Toxin_R_bind_N. 1 hit. PF07952. Toxin_trans. 1 hit. [Graphical view]
PRINTS	PR00760. BONTOXILYSIN.
ProDom	PD001963. Botulinum. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BXE_CLOBU

Accession

Primary (citable) accession number: P30995

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)