Glycyl-glycine endopeptidase ALE-1 precursor - Staphylococcus capitis

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Reviewed, UniProtKB/Swiss-Prot O05156 (ALE1_STACP)

Last modified January 19, 2010. Version 62. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names	Recommended name: Glycyl-glycine endopeptidase ALE-1 EC=3.4.24.75 Alternative name(s): Staphylolytic enzyme ALE-1
Organism	Staphylococcus capitis
Taxonomic identifier	29388 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	362 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	Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan.
Catalytic activity	Hydrolysis of the -Gly-\|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans.
Cofactor	Binds 1 zinc ion per subunit.
Subcellular location	Secreted.
Sequence similarities	Belongs to the peptidase M23B family.
Biophysicochemical properties	pH dependence: Optimum pH is 7-9.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro 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

35

Chain

327

Glycyl-glycine endopeptidase ALE-1

PRO_0000026814

Sites

Active site

1

By similarity

Metal binding

1

Zinc Probable

Metal binding

1

Zinc Probable

Metal binding

1

Zinc Probable

Secondary structure

1

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362

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

O05156-1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: C50DCDFDF9F6400E
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362

39,350

        10         20         30         40         50         60 
MDTNRKFTLV KSLSIGLGTF LVGSVFLTVN DEASASTKVD APKVEQEAPA KADAPKVEQE 

        70         80         90        100        110        120 
APAKADAPKV EQEAPAKVDA PKVEQEAPAK VDAPKVEQEA PAKADAPKVE QKRTFVREAA 

       130        140        150        160        170        180 
QSNHSASWLN NYKKGYGYGP YPLGINGGNH YGVDFFMNVG TPVRAISDGK IVEAGWTNYG 

       190        200        210        220        230        240 
GGNEIGLVEN DGVHRQWYMH LSKFNVKVGD RVKAGQIIGW SGSTGYSTAP HLHFQRMTNS 

       250        260        270        280        290        300 
FSNNTAQDPM PFLKSAGYGS NSTSSSNNNG YKTNKYGTLY KSESASFTAN TDIITRLTGP 

       310        320        330        340        350        360 
FRSMPQSGVL RKGLTIKYDE VMKQDGHVWV GYNTNSGKRV YLPVRTWNES TGELGPLWGT 


IK

References

[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: 9023202] [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: 15629919] [Abstract] Cited for: MUTAGENESIS OF HIS-150; ASP-154; HIS-200; HIS-231 AND HIS-233.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D86328 Genomic DNA. Translation: BAA13069.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R77	X-ray	1.75	A/B	271-362	[»]

SMR

O05156. Positions 125-254.

ModBase

Protein family/group databases

MEROPS

Enzyme and pathway databases

BRENDA

3.4.24.75. 19152.

Family and domain databases

InterPro

IPR011055. Dup_hybrid_motif.
IPR016047. Peptidase_M23.
IPR002886. Peptidase_M23B.
IPR003646. SH3-like_bac.
IPR013667. SH3_5_bac.
[Graphical view]

PANTHER

PTHR21666:SF7. Peptidase_M23B. 1 hit.

Pfam

PF01551. Peptidase_M23. 1 hit.
PF08460. SH3_5. 1 hit.
[Graphical view]

SMART

SM00287. SH3b. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

ALE1_STACP

Accession

Primary (citable) accession number: O05156

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	January 19, 2010
This is version 62 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)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents