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Protein

Glycyl-glycine endopeptidase ALE-1

Gene
N/A
Organism
Staphylococcus capitis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan.

Catalytic activityi

Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

pH dependencei

Optimum pH is 7-9.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi150 – 1501ZincCurated
Metal bindingi154 – 1541ZincCurated
Active sitei231 – 2311By similarity
Metal bindingi233 – 2331ZincCurated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell wall biogenesis/degradation

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM23.012.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycyl-glycine endopeptidase ALE-1 (EC:3.4.24.75)
Alternative name(s):
Staphylolytic enzyme ALE-1
OrganismiStaphylococcus capitis
Taxonomic identifieri29388 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Add
BLAST
Chaini36 – 362327Glycyl-glycine endopeptidase ALE-1PRO_0000026814Add
BLAST

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi279 – 29113Combined sources
Beta strandi293 – 3008Combined sources
Beta strandi306 – 3105Combined sources
Beta strandi315 – 32410Combined sources
Beta strandi327 – 3337Combined sources
Beta strandi339 – 3479Combined sources
Turni349 – 3513Combined sources
Beta strandi358 – 3625Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R77X-ray1.75A/B271-362[»]
ProteinModelPortaliO05156.
SMRiO05156. Positions 271-362.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO05156.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini282 – 35069SH3bPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M23B family.Curated
Contains 1 SH3b domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

InterProiIPR011055. Dup_hybrid_motif.
IPR016047. Peptidase_M23.
IPR003646. SH3-like_bac-type.
[Graphical view]
PfamiPF01551. Peptidase_M23. 1 hit.
PF08460. SH3_5. 1 hit.
[Graphical view]
SMARTiSM00287. SH3b. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.
PROSITEiPS51781. SH3B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O05156-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTNRKFTLV KSLSIGLGTF LVGSVFLTVN DEASASTKVD APKVEQEAPA
60 70 80 90 100
KADAPKVEQE APAKADAPKV EQEAPAKVDA PKVEQEAPAK VDAPKVEQEA
110 120 130 140 150
PAKADAPKVE QKRTFVREAA QSNHSASWLN NYKKGYGYGP YPLGINGGNH
160 170 180 190 200
YGVDFFMNVG TPVRAISDGK IVEAGWTNYG GGNEIGLVEN DGVHRQWYMH
210 220 230 240 250
LSKFNVKVGD RVKAGQIIGW SGSTGYSTAP HLHFQRMTNS FSNNTAQDPM
260 270 280 290 300
PFLKSAGYGS NSTSSSNNNG YKTNKYGTLY KSESASFTAN TDIITRLTGP
310 320 330 340 350
FRSMPQSGVL RKGLTIKYDE VMKQDGHVWV GYNTNSGKRV YLPVRTWNES
360
TGELGPLWGT IK
Length:362
Mass (Da):39,350
Last modified:July 1, 1997 - v1
Checksum:iC50DCDFDF9F6400E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86328 Genomic DNA. Translation: BAA13069.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86328 Genomic DNA. Translation: BAA13069.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R77X-ray1.75A/B271-362[»]
ProteinModelPortaliO05156.
SMRiO05156. Positions 271-362.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM23.012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO05156.

Family and domain databases

InterProiIPR011055. Dup_hybrid_motif.
IPR016047. Peptidase_M23.
IPR003646. SH3-like_bac-type.
[Graphical view]
PfamiPF01551. Peptidase_M23. 1 hit.
PF08460. SH3_5. 1 hit.
[Graphical view]
SMARTiSM00287. SH3b. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.
PROSITEiPS51781. SH3B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Purification and molecular characterization of glycylglycine endopeptidase produced by Staphylococcus capitis EPK1."
    Sugai M., Fujiwara T., Akiyama T., Ohara M., Komatsuzawa H., Inoue S., Suginaka H.
    J. Bacteriol. 179:1193-1202(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: EPK1.
  2. "Mutation analysis of the histidine residues in the glycylglycine endopeptidase ALE-1."
    Fujiwara T., Aoki S., Komatsuzawa H., Nishida T., Ohara M., Suginaka H., Sugai M.
    J. Bacteriol. 187:480-487(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-150; ASP-154; HIS-200; HIS-231 AND HIS-233.

Entry informationi

Entry nameiALE1_STACP
AccessioniPrimary (citable) accession number: O05156
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: March 16, 2016
This is version 89 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

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.