Reviewed, UniProtKB/Swiss-Prot Q47899 (FLVS_FLAME)

Names and origin

Protein names	Recommended name:     Flavastacin     EC=3.4.24.76
Organism	Flavobacterium meningosepticum (Chryseobacterium meningosepticum) (Elizabethkingia meningoseptica)
Taxonomic identifier	238 [NCBI]
Taxonomic lineage	Bacteria › Bacteroidetes › Flavobacteria › Flavobacteriales › Flavobacteriaceae › Elizabethkingia

Protein attributes

Sequence length	443 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	Zinc metallendopeptidase that cleaves preferentially on amino-terminal side of aspartate-containing substrates.
Catalytic activity	Hydrolyzes polypeptides on the amino-side of Asp in -Xaa-|-Asp-. Acts very slowly on -Xaa-|-Glu.
Cofactor	Zinc.
Post-translational modification	O-linked glycan consists of the Man, GlcNAc, GlcU, Glc, GlcU, Rha, Man heptasaccharide.
Sequence similarities	Belongs to the peptidase M12A family. Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
Domain	Signal
Ligand	Lectin Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro sugar binding Inferred from electronic annotation. Source: UniProtKB-KW 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
	Signal peptide	1 – 15	15	Potential
	Propeptide	16 – 91	76	Activation peptide		PRO_0000028875
	Chain	92 – 443	352	Flavastacin		PRO_0000028876
Regions
	Domain	297 – 440	144	Ricin B-type lectin
Sites
	Active site	190	1	By similarity
	Metal binding	189	1	Zinc; catalytic By similarity
	Metal binding	193	1	Zinc; catalytic By similarity
	Metal binding	199	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	355	1	O-linked (Man...) Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q47899-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 690C6031363EFA09	FASTA	443	48,957
	10 20 30 40 50 60 MTRKLLILSG CLILALNSCK SDMETTPASS VDHTTTQLNG TTIHKLLING AYTYVNEVNG 70 80 90 100 110 120 EYFYADDITI TAEQFNQLKR MANPDISTVE RSTIVSSFIK TWPNATVYYT LPSQGSLSTQ 130 140 150 160 170 180 AYNTFLTNIN KAFDMISSKT SVKFVQRTNQ TEYITFTYST GNSSPLGWVK NRVNGIKIYN 190 200 210 220 230 240 TTYPAIIAHE IMHSMGIMHE QCRPDRDQYI IVDTNRAQDG TRHNFNLYND YAGHGEFDFG 250 260 270 280 290 300 SVMMYKSTDF AIDPNLPVMT KLDGSTFGKQ RDGLSAGDYA GINHLYGPVN STSATNGTYT 310 320 330 340 350 360 LTTSLAGDKN IDITGSSTAD GTDVILYSAT TGNNQKFIFR KSEHGYFTIK SILDSTKVLT 370 380 390 400 410 420 VRNNGTANGT AVELRTNADT DAQKWLLFNL GNEGFGFAPK NAPSLRLEVK DGLTTNLTPI 430 440 VIGSTDQTLQ PYTKQRFTLT KVN

References

[1]	"Molecular cloning and sequence analysis of flavastacin: an O-glycosylated prokaryotic zinc metalloendopeptidase." Tarentino A.L., Quinones G., Grimwood B.G., Hauer C.R., Plummer T.H. Jr. Arch. Biochem. Biophys. 319:281-285(1995) [PubMed: 7771796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Detailed structural analysis of a novel, specific O-linked glycan from the prokaryote Flavobacterium meningosepticum." Reinhold B.B., Hauer C.R., Plummer T.H. Jr., Reinhold V.N. J. Biol. Chem. 270:13197-13203(1995) [PubMed: 7768917] [Abstract] Cited for: GLYCOSYLATION AT SER-355.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L37784 Genomic DNA. Translation: AAC41455.1.
PIR	S65963.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13.
MEROPS	M12.066.
Enzyme and pathway databases
BRENDA	3.4.24.76. 39124.
Family and domain databases
InterPro	IPR006025. Pept_M_Zn_BS. IPR006026. Peptidase_M. IPR001506. Peptidase_M12A. IPR000772. Ricin_B_lectin. [Graphical view]
Pfam	PF01400. Astacin. 1 hit. PF00652. Ricin_B_lectin. 1 hit. [Graphical view]
PRINTS	PR00480. ASTACIN.
SMART	SM00458. RICIN. 1 hit. SM00235. ZnMc. 1 hit. [Graphical view]
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FLVS_FLAME

Accession

Primary (citable) accession number: Q47899

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2001
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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