EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR009093 Phage P22 tailspike protein, head-binding

Protein matches Help

UniProtKB

Matches:

54 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR009093 Tailspk_head_bd

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:2.170.14.10	Tailspk_head_bd	51
Pfam	PF09008	Head_binding	51
SuperFamily	SSF51327	Tailspk_head_bd	54
Signatures in BioMart

GO Term annotation Help

Process

GO:0009405 pathogenesis

InterPro annotation

Entry Details in BioMart

Abstract

The tailspike protein of Salmonella bacteriophage P22 is a viral adhesion protein that mediates attachment of the viral protein to host cell-surface lipopolysaccharide. The tailspike protein displays both receptor binding and destroying properties, inactivating the receptor by endoglycosidase activity. The N-terminal, head-binding domain mediates the non-covalent attachment of the six homotrimeric tailspike molecules to the DNA injection apparatus [1]. The N-terminal domain of the P22 tailspike protein shows significant sequence similarity to the N-terminal domain of the Shigella phage Sf6 tailspike protein [2].

Structural links Help

PDB - click here

SCOP: b.80.1.6 , b.90.1.1

CATH: 2.170.14.10

Taxonomic coverage Help

Example proteins Help

P12528 Bifunctional tail protein

Q46636 Amylovoran biosynthesis protein amsF

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR012332	Phage P22 tailspike
IPR015331	Bacteriophage P22, tailspike
IPR006626	Parallel beta-helix repeat
IPR011050	Pectin lyase fold/virulence factor
IPR009093	Phage P22 tailspike protein, head-binding
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Steinbacher S, Miller S, Baxa U, Budisa N, Weintraub A, Seckler R, Huber R. Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56 A resolution, and the molecular basis of O-antigen recognition and cleavage. J. Mol. Biol. 267 865-80 1997 [PubMed: 9135118] http://dx.doi.org/10.1006/jmbi.1997.0922
2.	Freiberg A, Morona R, Van den Bosch L, Jung C, Behlke J, Carlin N, Seckler R, Baxa U. The tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain. J. Biol. Chem. 278 1542-8 2003 [PubMed: 12424253] http://dx.doi.org/10.1074/jbc.M205294200

Additional Reading Open in usermanual
	Baxa U, Steinbacher S, Weintraub A, Huber R, Seckler R. Mutations improving the folding of phage P22 tailspike protein affect its receptor binding activity. J. Mol. Biol. 293 1999 693-701 [PubMed: 10543960] http://dx.doi.org/10.1006/jmbi.1999.3165
	Steinbacher S, Seckler R, Miller S, Steipe B, Huber R, Reinemer P. Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer. Science 265 1994 383-6 [PubMed: 8023158] http://www.sciencemag.org/cgi/content/abstract/265/5170/383
	Schuler B, Furst F, Osterroth F, Steinbacher S, Huber R, Seckler R. Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein. Proteins 39 2000 89-101 [PubMed: 10737931] http://dx.doi.org/10.1002/(SICI)1097-0134(20000401)39:1<89::AID-PROT10>3.3.CO;2-H
	Steinbacher S, Baxa U, Miller S, Weintraub A, Seckler R, Huber R. Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors. Proc. Natl. Acad. Sci. U.S.A. 93 1996 10584-8 [PubMed: 8855221] http://dx.doi.org/10.1073/pnas.93.20.10584

InterPro 23.1