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Protein

Flavastacin

Gene
N/A
Organism
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Zinc metallendopeptidase that cleaves preferentially on N-terminal side of aspartate-containing substrates.

Catalytic activityi

Hydrolyzes polypeptides on the amino-side of Asp in -Xaa-|-Asp-. Acts very slowly on -Xaa-|-Glu.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi189 – 1891Zinc; catalyticPROSITE-ProRule annotation
Active sitei190 – 1901PROSITE-ProRule annotation
Metal bindingi193 – 1931Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi199 – 1991Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Lectin, Metal-binding, Zinc

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
MEROPSiM12.066.

Names & Taxonomyi

Protein namesi
Recommended name:
Flavastacin (EC:3.4.24.76)
OrganismiElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifieri238 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence analysisAdd
BLAST
Propeptidei16 – 9176Activation peptidePRO_0000028875Add
BLAST
Chaini92 – 443352FlavastacinPRO_0000028876Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi355 – 3551O-linked (Man...)1 Publication

Post-translational modificationi

O-linked glycan consists of the Man, GlcNAc, GlcU, Glc, GlcU, Rha, Man heptasaccharide.1 Publication

Keywords - PTMi

Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ47899.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini297 – 440144Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M12A family.Curated
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

KOiK20138.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF01400. Astacin. 1 hit.
PF14200. RicinB_lectin_2. 1 hit.
[Graphical view]
PRINTSiPR00480. ASTACIN.
SMARTiSM00458. RICIN. 1 hit.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q47899-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRKLLILSG CLILALNSCK SDMETTPASS VDHTTTQLNG TTIHKLLING
60 70 80 90 100
AYTYVNEVNG EYFYADDITI TAEQFNQLKR MANPDISTVE RSTIVSSFIK
110 120 130 140 150
TWPNATVYYT LPSQGSLSTQ AYNTFLTNIN KAFDMISSKT SVKFVQRTNQ
160 170 180 190 200
TEYITFTYST GNSSPLGWVK NRVNGIKIYN TTYPAIIAHE IMHSMGIMHE
210 220 230 240 250
QCRPDRDQYI IVDTNRAQDG TRHNFNLYND YAGHGEFDFG SVMMYKSTDF
260 270 280 290 300
AIDPNLPVMT KLDGSTFGKQ RDGLSAGDYA GINHLYGPVN STSATNGTYT
310 320 330 340 350
LTTSLAGDKN IDITGSSTAD GTDVILYSAT TGNNQKFIFR KSEHGYFTIK
360 370 380 390 400
SILDSTKVLT VRNNGTANGT AVELRTNADT DAQKWLLFNL GNEGFGFAPK
410 420 430 440
NAPSLRLEVK DGLTTNLTPI VIGSTDQTLQ PYTKQRFTLT KVN
Length:443
Mass (Da):48,957
Last modified:November 1, 1996 - v1
Checksum:i690C6031363EFA09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37784 Genomic DNA. Translation: AAC41455.1.
PIRiS65963.

Genome annotation databases

KEGGiag:AAC41455.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37784 Genomic DNA. Translation: AAC41455.1.
PIRiS65963.

3D structure databases

ProteinModelPortaliQ47899.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
MEROPSiM12.066.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC41455.

Phylogenomic databases

KOiK20138.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF01400. Astacin. 1 hit.
PF14200. RicinB_lectin_2. 1 hit.
[Graphical view]
PRINTSiPR00480. ASTACIN.
SMARTiSM00458. RICIN. 1 hit.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-355.

Entry informationi

Entry nameiFLVS_ELIME
AccessioniPrimary (citable) accession number: Q47899
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.