ID   FLVS_FLAME              Reviewed;         443 AA.
AC   Q47899;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 65.
DE   RecName: Full=Flavastacin;
DE            EC=3.4.24.76;
DE   Flags: Precursor;
OS   Flavobacterium meningosepticum (Chryseobacterium meningosepticum)
OS   (Elizabethkingia meningoseptica).
OC   Bacteria; Bacteroidetes; Flavobacteria; Flavobacteriales;
OC   Flavobacteriaceae; Elizabethkingia.
OX   NCBI_TaxID=238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=95289734; PubMed=7771796; DOI=10.1006/abbi.1995.1293;
RA   Tarentino A.L., Quinones G., Grimwood B.G., Hauer C.R.,
RA   Plummer T.H. Jr.;
RT   "Molecular cloning and sequence analysis of flavastacin: an O-
RT   glycosylated prokaryotic zinc metalloendopeptidase.";
RL   Arch. Biochem. Biophys. 319:281-285(1995).
RN   [2]
RP   GLYCOSYLATION AT SER-355.
RX   MEDLINE=95286606; 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
RT   from the prokaryote Flavobacterium meningosepticum.";
RL   J. Biol. Chem. 270:13197-13203(1995).
CC   -!- FUNCTION: Zinc metallendopeptidase that cleaves preferentially on
CC       amino-terminal side of aspartate-containing substrates.
CC   -!- CATALYTIC ACTIVITY: Hydrolyzes polypeptides on the amino-side of
CC       Asp in -Xaa-|-Asp-. Acts very slowly on -Xaa-|-Glu.
CC   -!- COFACTOR: Zinc.
CC   -!- PTM: O-linked glycan consists of the Man, GlcNAc, GlcU, Glc, GlcU,
CC       Rha, Man heptasaccharide.
CC   -!- SIMILARITY: Belongs to the peptidase M12A family.
CC   -!- SIMILARITY: Contains 1 ricin B-type lectin domain.
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DR   EMBL; L37784; AAC41455.1; -; Genomic_DNA.
DR   PIR; S65963; S65963.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   MEROPS; M12.066; -.
DR   BRENDA; 3.4.24.76; 39124.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR006025; Pept_M_Zn_BS.
DR   InterPro; IPR006026; Peptidase_M.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00458; RICIN; 1.
DR   SMART; SM00235; ZnMc; 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;
KW   Metal-binding; Metalloprotease; Protease; Signal; Zinc; Zymogen.
FT   SIGNAL        1     15       Potential.
FT   PROPEP       16     91       Activation peptide.
FT                                /FTId=PRO_0000028875.
FT   CHAIN        92    443       Flavastacin.
FT                                /FTId=PRO_0000028876.
FT   DOMAIN      297    440       Ricin B-type lectin.
FT   ACT_SITE    190    190       By similarity.
FT   METAL       189    189       Zinc; catalytic (By similarity).
FT   METAL       193    193       Zinc; catalytic (By similarity).
FT   METAL       199    199       Zinc; catalytic (By similarity).
FT   CARBOHYD    355    355       O-linked (Man...).
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
//