Reviewed, UniProtKB/Swiss-Prot P36175 (GCP_PASHA)

Names and origin

Protein names

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

Gene names

Name:

gcp

Organism

Pasteurella haemolytica (Mannheimia haemolytica)

Taxonomic identifier

75985 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Mannheimia

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Neutral metalloprotease that cleaves specifically O-sialoglycoproteins such as glycophorin A. HAMAP MF_01445
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. HAMAP MF_01445
Subcellular location	Secreted. Note: Not secreted through the conventional secretory pathway since it lacks a signal sequence. HAMAP MF_01445
Sequence similarities	Belongs to the peptidase M22 family.

Ontologies

Keywords
Cellular component	Secreted
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	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: 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 – 325	325	O-sialoglycoprotein endopeptidase HAMAP MF_01445		PRO_0000096976
Sites
	Metal binding	111	1	Zinc Potential
	Metal binding	115	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	P36175-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 161D58F60AD1D589	FASTA	325	35,190
	10 20 30 40 50 60 MRILGIETSC DETGVAIYDE DKGLVANQLY SQIDMHADYG GVVPELASRD HIRKTLPLIQ 70 80 90 100 110 120 EALKEANLQP SDIDGIAYTA GPGLVGALLV GSTIARSLAY AWNVPALGVH HMEGHLLAPM 130 140 150 160 170 180 LEENAPEFPF VALLISGGHT QLVKVDGVGQ YELLGESIDD AAGEAFDKTG KLLGLDYPAG 190 200 210 220 230 240 VAMSKLAESG TPNRFKFPRP MTDRPGLDFS FSGLKTFAAN TIKANLNENG ELDEQTKCDI 250 260 270 280 290 300 AHAFQQAVVD TILIKCKRAL EQTGYKRLVM AGGVSANKQL RADLAEMMKK LKGEVFYPRP 310 320 QFCTDNGAMI AYTGFLRLKT MNKPT

References

[1]	"Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene." Abdullah K.M., Lo R.Y.C., Mellors A. J. Bacteriol. 173:5597-5603(1991) [PubMed: 1885539] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: Serotype A1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U15958 Genomic DNA. Translation: AAA80282.1.
PIR	A38108.
3D structure databases
SMR	P36175. Positions 1-320.
ModBase	Search...
Protein family/group databases
MEROPS	M22.001.
Enzyme and pathway databases
BRENDA	3.4.24.57. 267636.
Family and domain databases
HAMAP	MF_01445. Glycoptase_bact. [Tree]
InterPro	IPR009180. Pept_M22_O-sialoglycoprot. 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.
TIGRFAMs	TIGR00329. gcp. 1 hit.
PROSITE	PS01016. GLYCOPROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GCP_PASHA

Accession

Primary (citable) accession number: P36175

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	February 9, 2010
This is version 60 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)