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InterPro: IPR001343 Haemolysin-type calcium-binding repeat

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UniProtKB

Matches:

2663 proteins

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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
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Accession

IPR001343 Hemolysn_Ca-bd

Type

Repeat

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00353	HemolysinCabind	2663
Signatures in BioMart

InterPro Relationships Help

Found in

IPR003995 RTX cytolytic toxin, protein A, core, bacterial
IPR011049 Serralysin-like metalloprotease, C-terminal
IPR013858 Peptidase M10, serralysin, C-terminal
IPR016294 Peptidase M10B
IPR018512 Haemolysin-type calcium-binding domain NodA

Contains

IPR018511 Hemolysin-type calcium-binding subgroup

GO Term annotation Help

Function

GO:0005509 calcium ion binding

InterPro annotation

Entry Details in BioMart

Abstract

Gram-negative bacteria produce a number of proteins that are secreted into the growth medium by a mechanism that does not require a cleaved N-terminal signal sequence. These proteins, while having different functions, seem to share two properties: they bind calcium and they contain a multiple tandem repeat of a nonapeptide [1]. The nonapeptide is found in a group of bacterial exported proteins that includes haemolysin, cyclolysin, leukotoxin and metallopeptidases belonging to MEROPS peptidase family M10 (clan MA(M)), subfamily 10B (serralysin).

It has been suggested that the internally repeated domain of haemolysin may be involved in Ca-mediated binding to erythrocytes. It has been shown that such a domain is involved in the binding of calcium ions in a parallel beta roll structure [2].

Structural links Help

PDB - click here

SCOP: b.80.7.1

CATH: 2.150.10.10

Database links Help

PDBe-motif: PS00330

PROSITE doc: PDOC00293

PANDIT: PF00353

Blocks: IPB001343

MEROPS: M10

COMe: PRX000484

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001343

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P07268 Serralysin

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001818	Peptidase M10A/M12B, matrixin/adamalysin
IPR006026	Peptidase, metallopeptidases
IPR001343	Haemolysin-type calcium-binding repeat
IPR016294	Peptidase M10B
IPR018511	Hemolysin-type calcium-binding subgroup
IPR011049	Serralysin-like metalloprotease, C-terminal
IPR018512	Haemolysin-type calcium-binding domain NodA
IPR013858	Peptidase M10, serralysin, C-terminal
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Economou A, Hamilton WD, Johnston AW, Downie JA. The Rhizobium nodulation gene nodO encodes a Ca2(+)-binding protein that is exported without N-terminal cleavage and is homologous to haemolysin and related proteins. EMBO J. 9 349-54 1990 [PubMed: 2303029] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=2303029&action=stream&blobtype=pdf
2.	Baumann U, Wu S, Flaherty KM, McKay DB. Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif. EMBO J. 12 3357-64 1993 [PubMed: 8253063] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=8253063&action=stream&blobtype=pdf

Additional Reading Open in usermanual
	Ravaud S, Gouet P, Haser R, Aghajari N. Probing the role of divalent metal ions in a bacterial psychrophilic metalloprotease: binding studies of an enzyme in the crystalline state by x-ray crystallography. J. Bacteriol. 185 2003 4195-203 [PubMed: 12837794] http://dx.doi.org/10.1128/JB.185.14.4195-4203.2003
	Chung YJ, Steen MT, Hansen JN. The subtilin gene of Bacillus subtilis ATCC 6633 is encoded in an operon that contains a homolog of the hemolysin B transport protein. J. Bacteriol. 174 1992 1417-22 [PubMed: 1735728] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1735728
	Hege T, Feltzer RE, Gray RD, Baumann U. Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond. J. Biol. Chem. 276 2001 35087-92 [PubMed: 11445573] http://dx.doi.org/10.1074/jbc.M104020200
	Hamada K, Hata Y, Katsuya Y, Hiramatsu H, Fujiwara T, Katsube Y. Crystal structure of Serratia protease, a zinc-dependent proteinase from Serratia sp. E-15, containing a beta-sheet coil motif at 2.0 A resolution. J. Biochem. 119 1996 844-51 [PubMed: 8797082] http://jb.oxfordjournals.org/cgi/content/abstract/119/5/844
	Hege T, Baumann U. Protease C of Erwinia chrysanthemi: the crystal structure and role of amino acids Y228 and E189. J. Mol. Biol. 314 2001 187-93 [PubMed: 11718553] http://dx.doi.org/10.1006/jmbi.2001.5124
	Aghajari N, Van Petegem F, Villeret V, Chessa JP, Gerday C, Haser R, Van Beeumen J. Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. Proteins 50 2003 636-47 [PubMed: 12577270] http://dx.doi.org/10.1002/prot.10264

InterPro 23.1