Reviewed, UniProtKB/Swiss-Prot Q2FWL2 (GCP_STAA8)

Names and origin

Protein names

Recommended name:
    Probable O-sialoglycoprotein endopeptidase
      Short name=Glycoprotease
    EC=3.4.24.57

Gene names

Name:	gcp
Ordered Locus Names:	SAOUHSC_02277

Organism

Staphylococcus aureus (strain NCTC 8325) [Complete proteome] [HAMAP]

Taxonomic identifier

93061 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Critical mediator involved in the modification of cell wall peptidoglycan synthesis and/or cell division as well as in the positive regulation of the activities of different murein hydrolases. Essential for cell viability. Negatively affects the expression of lrgA. Positively affects cidA expression, maybe indirectly. May be an important chelator of excess zinc. Down-regulation of gcp eliminates penicillin- and vancomycin-caused cell lysis, inhibits several extracellular hydrolase activities, dramatically increasing tolerance to hydrolases and leads to a bacteriostatic effect. Ref.2 Ref.3
Catalytic activity	Hydrolysis of O-sialoglycoproteins; cleaves 31-Arg-|-Asp-32 bond in glycophorin A. Does not cleave unglycosylated proteins, desialylated glycoproteins or glycoproteins that are only N-glycosylated. HAMAP MF_01445
Cofactor	Zinc Probable.
Sequence similarities	Belongs to the peptidase M22 family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: HAMAP 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
	Chain	1 – 341	341	Probable O-sialoglycoprotein endopeptidase HAMAP MF_01445		PRO_0000303551
Sites
	Metal binding	115	1	Zinc Potential
	Metal binding	119	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	Q2FWL2-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: AB4C57F8D21132C6	FASTA	341	36,819
	10 20 30 40 50 60 MTKDILILAV ETSCDETSVS VIKNGRDILS NTVLSQIESH KRFGGVVPEV ASRHHVEGIT 70 80 90 100 110 120 ATINEALGDA DVSIEDIDAI AVTEGPGLIG ALLIGVNAAK ALAFAYDKPL IPVHHIAGHI 130 140 150 160 170 180 YANHIEEPLT FPLIALIVSG GHTELVYMKD HLSFEVIGET RDDAVGEAYD KVARTIGLNY 190 200 210 220 230 240 PGGPQVDRLA AEGEDTYSFP RVWLDKDSYD FSFSGLKSAV INQLHNQRQK NIPIIEANVA 250 260 270 280 290 300 TSFQNSVVEV LTFKAIQACK EYGVQRLIVA GGVASNKGLR QSLADQCKVN DIQLTIPSPK 310 320 330 340 LCTDNAAMIG VAGHYLYQQG RFADLALNGH SNIDLEEYSA E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Staphylococcus aureus NCTC8325 genome." Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Identification of an essential glycoprotease in Staphylococcus aureus." Zheng L., Yang J., Landwehr C., Fan F., Ji Y. FEMS Microbiol. Lett. 245:279-285(2005) [PubMed: 15837383] [Abstract] Cited for: FUNCTION IN CELL VIABILITY.
[3]	"Conditional mutation of an essential putative glycoprotease eliminates autolysis in Staphylococcus aureus." Zheng L., Yu C., Bayles K., Lasa I., Ji Y. J. Bacteriol. 189:2734-2742(2007) [PubMed: 17237169] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000253 Genomic DNA. Translation: ABD31315.1.
RefSeq	YP_500758.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q2FWL2.
Protein family/group databases
MEROPS	M22.001.
Genome annotation databases
GeneID	3919152.
GenomeReviews	Gene locus SAOUHSC_02277 in contig CP000253_GR.
KEGG	sao:SAOUHSC_02277.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2FWL2.
OMA	CKRALKQ.
Enzyme and pathway databases
BioCyc	SAUR93061:SAOUHSC_02277-MON.
Family and domain databases
HAMAP	MF_01445. [Tree]
InterPro	IPR009180. Pept_M22_Osialgl. IPR000905. Peptidase_M22. IPR017860. Peptidase_M22_CS. IPR017861. Peptidase_M22_subgr. [Graphical view]
PANTHER	PTHR11735. Pept_M22_Osialgl. 1 hit.
Pfam	PF00814. Peptidase_M22. 1 hit. [Graphical view]
PRINTS	PR00789. OSIALOPTASE.
ProDom	PD002367. Peptidase_M22. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00329. gcp. 1 hit.
PROSITE	PS01016. GLYCOPROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GCP_STAA8

Accession

Primary (citable) accession number: Q2FWL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	March 21, 2006
Last modified:	November 3, 2009
This is version 25 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)