ID FLVS_ELIME Reviewed; 443 AA.
AC Q47899;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Flavastacin;
DE EC=3.4.24.76;
DE Flags: Precursor;
OS Elizabethkingia meningoseptica (Chryseobacterium meningosepticum).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7771796; DOI=10.1006/abbi.1995.1293;
RA Tarentino A.L., Quinones G., Grimwood B.G., Hauer C.R., Plummer T.H. Jr.;
RT "Molecular cloning and sequence analysis of flavastacin: an O-glycosylated
RT prokaryotic zinc metalloendopeptidase.";
RL Arch. Biochem. Biophys. 319:281-285(1995).
RN [2]
RP GLYCOSYLATION AT SER-355.
RX PubMed=7768917; DOI=10.1074/jbc.270.22.13197;
RA Reinhold B.B., Hauer C.R., Plummer T.H. Jr., Reinhold V.N.;
RT "Detailed structural analysis of a novel, specific O-linked glycan from the
RT prokaryote Flavobacterium meningosepticum.";
RL J. Biol. Chem. 270:13197-13203(1995).
CC -!- FUNCTION: Zinc metallendopeptidase that cleaves preferentially on N-
CC terminal side of aspartate-containing substrates.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes polypeptides on the amino-side of Asp in -Xaa-|-
CC Asp-. Acts very slowly on -Xaa-|-Glu.; EC=3.4.24.76;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU01211};
CC -!- PTM: O-linked glycan consists of the Man, GlcNAc, GlcU, Glc, GlcU, Rha,
CC Man heptasaccharide. {ECO:0000269|PubMed:7768917}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L37784; AAC41455.1; -; Genomic_DNA.
DR PIR; S65963; S65963.
DR AlphaFoldDB; Q47899; -.
DR SMR; Q47899; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR MEROPS; M12.066; -.
DR iPTMnet; Q47899; -.
DR KEGG; ag:AAC41455; -.
DR BRENDA; 3.4.24.76; 1374.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 2.80.10.50; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF850; METALLOENDOPEPTIDASE; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF14200; RicinB_lectin_2; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00458; RICIN; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Lectin; Metal-binding;
KW Metalloprotease; Protease; Signal; Zinc; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..91
FT /note="Activation peptide"
FT /id="PRO_0000028875"
FT CHAIN 92..443
FT /note="Flavastacin"
FT /id="PRO_0000028876"
FT DOMAIN 92..289
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 297..440
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT ACT_SITE 190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 355
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:7768917"
SQ SEQUENCE 443 AA; 48957 MW; 690C6031363EFA09 CRC64;
MTRKLLILSG CLILALNSCK SDMETTPASS VDHTTTQLNG TTIHKLLING AYTYVNEVNG
EYFYADDITI TAEQFNQLKR MANPDISTVE RSTIVSSFIK TWPNATVYYT LPSQGSLSTQ
AYNTFLTNIN KAFDMISSKT SVKFVQRTNQ TEYITFTYST GNSSPLGWVK NRVNGIKIYN
TTYPAIIAHE IMHSMGIMHE QCRPDRDQYI IVDTNRAQDG TRHNFNLYND YAGHGEFDFG
SVMMYKSTDF AIDPNLPVMT KLDGSTFGKQ RDGLSAGDYA GINHLYGPVN STSATNGTYT
LTTSLAGDKN IDITGSSTAD GTDVILYSAT TGNNQKFIFR KSEHGYFTIK SILDSTKVLT
VRNNGTANGT AVELRTNADT DAQKWLLFNL GNEGFGFAPK NAPSLRLEVK DGLTTNLTPI
VIGSTDQTLQ PYTKQRFTLT KVN
//
