BXWO_WEIOS
ID BXWO_WEIOS Reviewed; 1336 AA.
AC A0A069CUU9;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Putative botulinum-like toxin Wo {ECO:0000303|PubMed:27443638};
DE Short=BoNT/Wo {ECO:0000303|PubMed:27443638};
DE EC=3.4.24.69 {ECO:0000269|PubMed:27443638};
GN ORFNames=WOSG25_110680;
OS Weissella oryzae (strain DSM 25784 / JCM 18191 / LMG 30913 / SG25).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Weissella.
OX NCBI_TaxID=1329250;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25784 / JCM 18191 / LMG 30913 / SG25;
RX PubMed=25013139; DOI=10.1128/genomea.00667-14;
RA Tanizawa Y., Fujisawa T., Mochizuki T., Kaminuma E., Suzuki Y.,
RA Nakamura Y., Tohno M.;
RT "Draft genome sequence of Weissella oryzae SG25T, isolated from fermented
RT rice grains.";
RL Genome Announc. 2:0-0(2014).
RN [2]
RP DISCUSSION OF SEQUENCE.
RX PubMed=25541486; DOI=10.1016/j.febslet.2014.12.018;
RA Mansfield M.J., Adams J.B., Doxey A.C.;
RT "Botulinum neurotoxin homologs in non-Clostridium species.";
RL FEBS Lett. 589:342-348(2015).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=27443638; DOI=10.1038/srep30257;
RA Zornetta I., Azarnia Tehran D., Arrigoni G., Anniballi F., Bano L.,
RA Leka O., Zanotti G., Binz T., Montecucco C.;
RT "The first non Clostridial botulinum-like toxin cleaves VAMP within the
RT juxtamembrane domain.";
RL Sci. Rep. 6:30257-30257(2016).
CC -!- FUNCTION: When overexpressed the N-terminus (residues 1-476) cleaves
CC rat synaptobrevin-2/VAMP2 between '89-Trp-|-Trp-90' in vitro. This
CC releases the cytoplasmic domain of VAMP2 from the synaptic vesicle
CC membrane, which would prevent the assembly of the trans-SNARE complex
CC on the membrane and thus prevent vesicle-target membrane fusion and
CC neurotransmitter release (PubMed:27443638).
CC {ECO:0000269|PubMed:27443638}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Limited hydrolysis of proteins of the neuroexocytosis
CC apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on
CC small molecule substrates.; EC=3.4.24.69;
CC Evidence={ECO:0000269|PubMed:27443638};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0DPI0, ECO:0000305|PubMed:27443638};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and 1,10-phenanthroline
CC (PubMed:27443638). {ECO:0000269|PubMed:27443638}.
CC -!- MISCELLANEOUS: There are seven antigenically distinct forms of
CC botulinum neurotoxin: Types A, B, C, D, E, F, and G, but serologically
CC this does not belong to any of them. {ECO:0000269|PubMed:27443638}.
CC -!- SIMILARITY: Belongs to the peptidase M27 family. {ECO:0000305}.
CC -!- CAUTION: This bacteria is missing genes associated with the botulinum
CC neurotoxin cluster in Clostridia (botR, hemagglutinin genes and ORF-X
CC proteins), so it is not clear if it is actually a toxin. The in situ
CC target might not be animal as this bacteria was isolated from fermented
CC rice grains. {ECO:0000303|PubMed:25541486}.
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DR EMBL; DF820494; GAK31590.1; -; Genomic_DNA.
DR RefSeq; WP_027699549.1; NZ_DF820494.1.
DR PDB; 6RIM; X-ray; 1.60 A; A/B/C/D/E/F/G/H=2-476.
DR PDBsum; 6RIM; -.
DR AlphaFoldDB; A0A069CUU9; -.
DR SMR; A0A069CUU9; -.
DR EnsemblBacteria; GAK31590; GAK31590; WOSG25_110680.
DR OrthoDB; 50987at2; -.
DR Proteomes; UP000030643; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..1336
FT /note="Putative botulinum-like toxin Wo"
FT /id="PRO_0000444914"
FT REGION 1..476
FT /note="Has protease activity"
FT /evidence="ECO:0000269|PubMed:27443638"
FT ACT_SITE 251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0DPI0"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 31..41
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 47..60
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:6RIM"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 101..125
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:6RIM"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:6RIM"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 244..259
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 309..325
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 339..348
FT /evidence="ECO:0007829|PDB:6RIM"
FT TURN 349..352
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 357..367
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:6RIM"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 382..391
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 397..404
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:6RIM"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:6RIM"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:6RIM"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:6RIM"
SQ SEQUENCE 1336 AA; 153025 MW; 173CAE78C0DD2205 CRC64;
MDVLEMFDVN YESPILESFD STTQSLNDVH VFMSRIQMSA YDADGEGRIE YRNLKLYEIS
SGIFISTDRL DTGASGVEDD HEMVDYYSSA RLTREFLGES LDSQKSDYFE GIKKVFSFYK
NKCNESRYIK EFFEEIQFRN ICGFPKQAGT SSTDIFDQFN SVDVLLQDPV TSVWNKKVGS
KKANIVIIPP ATNLPITEAC ATAGFQPEGF PKLGSGSFFT VQFDPFFSTR FKAHETDDVA
LLDPTLTLLH EMTHGLHFQK GIANPVNRSG ETPAWATTWG RVTGDNDAFK ETPMEELLTF
NKHTIDDDIE ISDHLKSTYI GFLYNGRNED DPTESVDGVY QNVSSFLNQY RGFEISSDFQ
HFIESCYGVK YNQESKKFIV NPRNIKRYVQ DGFFIDEAKF ARILNIKTRS YYTLMPDNLG
VWSYRVDILN RLRETFDEDR GLLSQELDFH TALTPVVSEN PALELEVAGM QRMVSLPKIK
ASYLPSDIKI KNFTGQKISH DTILDTNISG IIISKIKYKS DFVVDESMPR SSLNTTNYNL
SPIKGTKFET DIRDKTSVKV TVSEITAPMI NHVMKLDNSK VLTERPSLNE DLEETFKNTK
DVYIPKTTAM MKLKEGADQT LGAVGFAVWS GQILEDLYNL AQKKEVSIDQ IKDDLMSILP
FYCAYKNLSA EKYEQAFANA TLDAFLIFAT DGGGFAGLGI TVGAIAINSM YAKAETMEAY
DSMFGKYVDQ YQNDIKNFTL NAYVQWENNI LSRLWNESRL AITGFRNMLK TVKTVMEFDA
TNQAYSEEDR KIIKAKCEEI FSEFPMLMQT FAKNSMTANL ENASKIFNDI VWQKIKEELD
QYVIDSKKYF LDSLEEAYNN GSISAESYYK YQTEAREKFV SPREVIDLYI AAHDTVVKRK
RYIRRYSRKY DLATDFKGNT VHLNGLGEGT QDIQDLYGNY SVYADKKTVS TQEGHFDQTI
KIAKDTNTIN KVVLAVSSNN GKEYALNKDE QYTISFWLRM PVPSSSEERR IFSYSAVSGV
NKEVEELILQ VKNNEFVLAT ANLLRNSEFV IEPRIALNRW VKITIVNENT RIKVYQNDNL
LGLIKDSSRK KPIAQRGTFK FYNYNVDYQL DDISYYNGTI SQRDIKYTFK EDHGQFVYDH
WGERLQYNKA YYLLSDDNKS AFETVYETKR LKLKSVPGVD IKYLGMNDRV YGYYGGLQFK
LVPLDSKNMN NYVRWGDKFT MQSIETTNLS LAIIQDNAYF APTQLKLISN EGKSEEEIFT
FDRNIKLQNA AILVGTGNSK QGPISAYKRG YSGDLWINGA RLDGYVTVVN KSNYSNDEIQ
EKFKWIFVPK DANWVE
