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   03-AUG-2022, entry version 108.
DE   RecName: Full=Flavastacin;
DE            EC=3.4.24.76;
DE   Flags: Precursor;
OS   Elizabethkingia meningoseptica (Chryseobacterium meningosepticum).
OC   Bacteria; Bacteroidetes; 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}.
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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; 3.40.390.10; -; 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   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; SSF50370; SSF50370; 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