NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(02)08713-5; PubMed=12044378 [NCBI, ExPASy, EBI, Israel, Japan]
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
"Genome and virulence determinants of high virulence community-acquired MRSA.";
Lancet 359:1819-1827(2002).

Comments

FUNCTION: Peptidoglycan hydrolase (autolysin) specifically acting on polyglycine interpeptide bridges of the cell wall peptidoglycan (By similarity).
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 (By similarity).
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Secreted (By similarity).
SIMILARITY: Belongs to the peptidase M23B family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000033; BAB94117.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_645067.1; -.

3D structure databases

SMR

Q8NYG1; 45-314.

ModBase

Q8NYG1.

Protein family/group databases

MEROPS

M23.004; -.

Enzyme and pathway databases

BioCyc

SAUR196620:MW0252-MON; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0004222;	Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007047;	Biological process: cell wall organization (inferred from electronic annotation from UniProtKB-KW).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR016047; Peptidase_M23.
IPR002886; Peptidase_M23B.
Graphical view of domain structure.

PANTHER

PTHR21666:SF7; Peptidase_M23B; 1.

Pfam

PF01551; Peptidase_M23; 1.
Pfam graphical view of domain structure.

Genome annotation databases

GeneID

1002352; -.

GenomeReviews

BA000033_GR; MW0252.

KEGG

sam:MW0252; -.

Phylogenomic databases

HOGENOM

Q8NYG1; -.

Genome annotation databases

CMR

Q8NYG1; MW0252.

Other

ProtoNet

Q8NYG1.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell wall biogenesis/degradation; Complete proteome; Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal; Virulence; Zinc; Zymogen.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 25`	`25`	`By similarity.`
`CHAIN`	`26 316`	`291`	`Glycyl-glycine endopeptidase lytM.`	`PRO_0000026825`
`METAL`	`117 117`		`Zinc (By similarity).`
`METAL`	`210 210`		`Zinc (By similarity).`
`METAL`	`214 214`		`Zinc (By similarity).`
`METAL`	`293 293`		`Zinc (By similarity).`

Sequence information

Length: 316 AA [This is the length of the unprocessed precursor]

Molecular weight: 34355 Da [This is the MW of the unprocessed precursor]

CRC64: 3A53C4331E8B024F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKLTAAAIA TMGFATFTMA HQADAAETTN TQQAHTQMST QSQDVSYGTY YTIDSNGDYH 

        70         80         90        100        110        120 
HTPDGNWNQA MFDNKEYSYT FVDAQGHTHY FYNCYPKNAN ANGSGQTYVN PAIAGDNNDY 

       130        140        150        160        170        180 
TASQSQQHIN QYGYQSNVGP DASYYSHSNN NQAYNSHDGN GKVNYPNGTS NQNGGLASKA 

       190        200        210        220        230        240 
TASGHAKDAS WLTSRKQLQP YGQYHGGGAH YGVDYAMPEN SPVYSLTDGT VVQAGWSNYG 

       250        260        270        280        290        300 
GGNQVTIKEA NSNNYQWYMH NNRLTVSAGD KVKAGDQIAY SGSTGNSTAP HVHFQRMSGG 

       310 
IGNQYAVDPT SYLQSR

Q8NYG1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools