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Protein

Ulilysin

Gene

MA_3214

Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Metalloprotease which in vitro specifically cleaves IGFBP-2 to -6, insulin, and extracellular matrix proteins but not IGFBP-1 or IGF-II. Shows a preference for substrates with an arginine in the P1' position, the first position downstream of the scissile bond.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Ca2+1 PublicationNote: Binds 2 calcium ions per subunit.1 Publication
  • Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Enzyme regulationi

Inhibited by EDTA, excess zinc, and also significantly by batimastat in vitro. Is not inhibited by other metalloprotease inhibitors like phosphoramidon, captopril and galardine or those targeting other classes of proteases.2 Publications

pH dependencei

Optimum pH is 7.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei225 – 2251Substrate1 Publication
Metal bindingi228 – 2281Zinc; catalyticPROSITE-ProRule annotation2 Publications
Active sitei229 – 2291Proton acceptor2 Publications
Metal bindingi232 – 2321Zinc; catalyticPROSITE-ProRule annotation2 Publications
Metal bindingi238 – 2381Zinc; catalyticPROSITE-ProRule annotation2 Publications
Metal bindingi240 – 2401Calcium 1; via carbonyl oxygen2 Publications
Metal bindingi243 – 2431Calcium 12 Publications
Metal bindingi249 – 2491Calcium 1; via carbonyl oxygen2 Publications
Metal bindingi254 – 2541Calcium 22 Publications
Metal bindingi256 – 2561Calcium 2; via carbonyl oxygen2 Publications
Metal bindingi259 – 2591Calcium 22 Publications
Metal bindingi262 – 2621Calcium 1; via carbonyl oxygen2 Publications
Metal bindingi263 – 2631Calcium 1; via carbonyl oxygen2 Publications
Binding sitei295 – 2951Substrate1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMACE188937:GI2O-3249-MONOMER.

Protein family/group databases

MEROPSiM43.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Ulilysin (EC:3.4.24.-)
Gene namesi
Ordered Locus Names:MA_3214
OrganismiMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifieri188937 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
Proteomesi
  • UP000002487 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 60Removed in mature formPRO_0000280823
Signal peptidei1 – ?Sequence analysis
Chaini61 – 322262UlilysinPRO_0000280824Add
BLAST
Propeptidei323 – 34220Removed in mature formPRO_0000280825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi250 ↔ 2772 Publications
Disulfide bondi269 ↔ 297Curated

Post-translational modificationi

The inactive zymogen pro-ulilysin undergoes calcium-mediated autolytic activation to the mature ulilysin. Autoproteolytic activation entails removal of the first 60 residues and of a highly charged 20-residue C-terminal tail.

Keywords - PTMi

Disulfide bond, Zymogen

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi188937.MA3214.

Structurei

Secondary structure

1
342
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi65 – 7713Combined sources
Helixi78 – 803Combined sources
Helixi84 – 9714Combined sources
Turni98 – 1003Combined sources
Helixi103 – 1075Combined sources
Helixi110 – 1156Combined sources
Beta strandi121 – 1255Combined sources
Beta strandi137 – 1426Combined sources
Helixi153 – 1553Combined sources
Helixi157 – 1593Combined sources
Turni167 – 1693Combined sources
Beta strandi171 – 1777Combined sources
Beta strandi188 – 1914Combined sources
Helixi198 – 2003Combined sources
Beta strandi202 – 2065Combined sources
Helixi207 – 2093Combined sources
Beta strandi210 – 2134Combined sources
Helixi224 – 23310Combined sources
Turni280 – 2823Combined sources
Turni295 – 2973Combined sources
Helixi303 – 31412Combined sources
Turni315 – 3173Combined sources
Helixi318 – 3203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CKIX-ray1.70A/B61-322[»]
2J83X-ray2.00A/B61-322[»]
3LUMX-ray1.70A/B/C/D61-322[»]
3LUNX-ray1.80A/B61-322[»]
ProteinModelPortaliQ8TL28.
SMRiQ8TL28. Positions 61-322.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TL28.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni188 – 1892Substrate binding

Domaini

Consists of two subdomains separated by an active site cleft containing the catalytic zinc ion.

Sequence similaritiesi

Belongs to the peptidase M43B family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410XPH7. LUCA.
InParanoidiQ8TL28.
OMAiRNSFAQP.
PhylomeDBiQ8TL28.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR008754. Peptidase_M43.
[Graphical view]
PfamiPF05572. Peptidase_M43. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8TL28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEKFESRGI EEASSEVPTQ RRCGAMEVHH RLLRSASYVR ERDQIENLAL
60 70 80 90 100
KYKQGFRAIS RMEIVKIPVV VHVVWNEEEE NISDAQIQSQ IDILNKDFRK
110 120 130 140 150
LNSDVSQVPS VWSNLIADLG IEFFLATKDP NGNQTTGITR TQTSVTFFTT
160 170 180 190 200
SDEVKFASSG GEDAWPADRY LNIWVCHVLK SEIGQDILGY AQFPGGPAET
210 220 230 240 250
DGVVIVDAAF GTTGTALPPF DKGRTATHEI GHWLNLYHIW GDELRFEDPC
260 270 280 290 300
SRSDEVDDTP NQADPNFGCP SYPHVSCSNG PNGDMFMNYM DYVDDKCMVM
310 320 330 340
FTQGQATRVN ACLDGPRSSF LARVEETEKK EAPSKREMPM PR
Length:342
Mass (Da):38,371
Last modified:June 1, 2002 - v1
Checksum:iB2480CD7BB2B9574
GO

Mass spectrometryi

Molecular mass is 28885±50 Da from positions 61 - 322. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM06585.1.
RefSeqiWP_011023149.1. NC_003552.1.

Genome annotation databases

EnsemblBacteriaiAAM06585; AAM06585; MA_3214.
GeneIDi1475107.
KEGGimac:MA3214.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM06585.1.
RefSeqiWP_011023149.1. NC_003552.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CKIX-ray1.70A/B61-322[»]
2J83X-ray2.00A/B61-322[»]
3LUMX-ray1.70A/B/C/D61-322[»]
3LUNX-ray1.80A/B61-322[»]
ProteinModelPortaliQ8TL28.
SMRiQ8TL28. Positions 61-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi188937.MA3214.

Protein family/group databases

MEROPSiM43.007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM06585; AAM06585; MA_3214.
GeneIDi1475107.
KEGGimac:MA3214.

Phylogenomic databases

eggNOGiENOG410XPH7. LUCA.
InParanoidiQ8TL28.
OMAiRNSFAQP.
PhylomeDBiQ8TL28.

Enzyme and pathway databases

BioCyciMACE188937:GI2O-3249-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8TL28.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR008754. Peptidase_M43.
[Graphical view]
PfamiPF05572. Peptidase_M43. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity."
    Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.
    , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.
    Genome Res. 12:532-542(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.
  2. "Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases."
    Tallant C., Garcia-Castellanos R., Seco J., Baumann U., Gomis-Rueth F.X.
    J. Biol. Chem. 281:17920-17928(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, CHARACTERIZATION, AUTOCATALYTIC CLEAVAGES, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, MASS SPECTROMETRY, ENZYME REGULATION, DISULFIDE BONDS, X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 61-322 OF MUTANT ALA-269 IN COMPLEX WITH DIPEPTIDE PRODUCT AND ZINC.
    Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.
  3. Gomis-Rueth F.X.
    Unpublished observations (FEB-2007)
    Cited for: PH DEPENDENCE.
  4. "Substrate specificity of a metalloprotease of the pappalysin family revealed by an inhibitor and a product complex."
    Garcia-Castellanos R., Tallant C., Marrero A., Sola M., Baumann U., Gomis-Rueth F.X.
    Arch. Biochem. Biophys. 457:57-72(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 61-322 OF MUTANT ALA-269 IN COMPLEX WITH INHIBITOR AND ZINC, DISULFIDE BONDS, ENZYME REGULATION.
    Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

Entry informationi

Entry nameiULIL_METAC
AccessioniPrimary (citable) accession number: Q8TL28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: June 1, 2002
Last modified: January 20, 2016
This is version 75 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.