Reviewed, UniProtKB/Swiss-Prot A9IZF6 (GCP_BART1)

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:	BT_2585

Organism

Bartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]

Taxonomic identifier

382640 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

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 By similarity.
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 – 364	364	Probable O-sialoglycoprotein endopeptidase HAMAP MF_01445		PRO_1000087467
Sites
	Metal binding	115	1	Zinc Potential
	Metal binding	119	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	A9IZF6-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 787686B32D27BD4C	FASTA	364	38,600
	10 20 30 40 50 60 MRLLGIETSC DETAAAVIEY NNESSSRILS NIVWSQIDHH APYGGVVPEI AARAHVEILD 70 80 90 100 110 120 HLILQALTEA NTKLKDIDGI AATSGPGLIG GLLVGVMSAK ALSLATGKPF IAVNHLEGHA 130 140 150 160 170 180 LTAVLTHNVK FPYLLLLVSG GHTQTILVHG VGNYQRLGTT IDDALGEAFD KTAKLLGLPY 190 200 210 220 230 240 PGGPALEKAA LLGDKNRIPL PRPLKGEKRL DFSFSGLKTA VRQAATAIAP LTENDVADIA 250 260 270 280 290 300 ASFQAAVTDT VRDRVHLALQ HFTHQYPLSH DQEKHSPALV VAGGVAANQA LRSTLQELAH 310 320 330 340 350 360 QHGFEFIAPP LSLCTDNAAM IAFAGAQKLA QGETSSLDIA PRSRWPLDEK AIPLIGMGRR GTKA

References

[1]

"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors." Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C. Nat. Genet. 39:1469-1476(2007) [PubMed: 18037886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM260525 Genomic DNA. Translation: CAK02538.1.
RefSeq	YP_001610533.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M22.001.
Genome annotation databases
GeneID	5830391.
GenomeReviews	Gene locus BT_2585 in contig AM260525_GR.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	EHSAYGG.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GCP_BART1

Accession

Primary (citable) accession number: A9IZF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	November 3, 2009
This is version 14 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)