double-psi beta-barrel fold of EG45-like domain-containing proteins; This family contains plant EG45-like domain-containing proteins which show sequence similarity to expansins, and similar proteins. Citrus jambhiri EG45-like domain-containing protein was identified as a protein associated with citrus blight (CB), and is also called blight-associated protein p12 (CjBAp12) or plant natriuretic peptide (PNP). CjBAp12 does not display cell wall loosening activity of expansins. Arabidopsis thaliana EG45-like domain-containing protein 2, also called plant natriuretic peptide A (AtPNP-A), is a systemically mobile natriuretic peptide immunoanalog, recognized by antibodies against vertebrate atrial natriuretic peptides (ANPs), that functions in cell volume regulation. Thus, it has an important and systemic role in plant growth and homeostasis. Due to their similarity to the N-terminal domain of expansin and to endolytic peptidoglycan transglycosylase RlpA, EG45-like domain-containing proteins may adopt a double-psi beta-barrel fold.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680435  26 AQGKAVYYDPPYTRSACYGTQRE---TLVVGVKNNLWQNGRACGRRYRVRCIGATYNFDRACTGRTVDVKVVDFCREPCN 102
Cdd:cd22269   1 DVGTATFYTPPYTPSACYGNDPSpsgNLFAAAGDALWDNGAACGRRYRVRCIGGTNPGPRPCTGGSVVVKIVDYCPGCCG 80

                        90       100
                ....*....|....*....|....*.
gi 30680435 103 GDLNLSRDAFRVIANTDAGNIRVVYT 128
Cdd:cd22269  81 ATFDLSQEAFAKIADPDAGRINIEYV 106

double-psi beta-barrel fold of EG45-like domain-containing proteins; This family contains plant EG45-like domain-containing proteins which show sequence similarity to expansins, and similar proteins. Citrus jambhiri EG45-like domain-containing protein was identified as a protein associated with citrus blight (CB), and is also called blight-associated protein p12 (CjBAp12) or plant natriuretic peptide (PNP). CjBAp12 does not display cell wall loosening activity of expansins. Arabidopsis thaliana EG45-like domain-containing protein 2, also called plant natriuretic peptide A (AtPNP-A), is a systemically mobile natriuretic peptide immunoanalog, recognized by antibodies against vertebrate atrial natriuretic peptides (ANPs), that functions in cell volume regulation. Thus, it has an important and systemic role in plant growth and homeostasis. Due to their similarity to the N-terminal domain of expansin and to endolytic peptidoglycan transglycosylase RlpA, EG45-like domain-containing proteins may adopt a double-psi beta-barrel fold.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680435  26 AQGKAVYYDPPYTRSACYGTQRE---TLVVGVKNNLWQNGRACGRRYRVRCIGATYNFDRACTGRTVDVKVVDFCREPCN 102
Cdd:cd22269   1 DVGTATFYTPPYTPSACYGNDPSpsgNLFAAAGDALWDNGAACGRRYRVRCIGGTNPGPRPCTGGSVVVKIVDYCPGCCG 80

                        90       100
                ....*....|....*....|....*.
gi 30680435 103 GDLNLSRDAFRVIANTDAGNIRVVYT 128
Cdd:cd22269  81 ATFDLSQEAFAKIADPDAGRINIEYV 106

Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Recent studies show that the full-length RlpA protein from Pseudomonas Aeruginosa is an outer membrane protein that is a lytic transglycolase with specificity for peptidoglycan lacking stem peptides. Residue D157 in UniProtKB:Q9X6V6 is critical for lytic activity.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30680435    58 LWQNGRACGRRYRVRCIGA---TYNFDRACT---GRTVDVKVVDFCREPCNGDLNLSRDAFRVIANTDAGNIRVVY 127
Cdd:pfam03330   7 LYNNGTACGECYDVRCLTAahpTLPFGTYCRvlsGRSVIVRITDRGPFPPGRHFDLSGAAFEKLAMPRAGIVPVQY 82

double-psi beta-barrel fold of EG45-like domain-containing proteins; This family contains plant EG45-like domain-containing proteins which show sequence similarity to expansins, and similar proteins. Citrus jambhiri EG45-like domain-containing protein was identified as a protein associated with citrus blight (CB), and is also called blight-associated protein p12 (CjBAp12) or plant natriuretic peptide (PNP). CjBAp12 does not display cell wall loosening activity of expansins. Arabidopsis thaliana EG45-like domain-containing protein 2, also called plant natriuretic peptide A (AtPNP-A), is a systemically mobile natriuretic peptide immunoanalog, recognized by antibodies against vertebrate atrial natriuretic peptides (ANPs), that functions in cell volume regulation. Thus, it has an important and systemic role in plant growth and homeostasis. Due to their similarity to the N-terminal domain of expansin and to endolytic peptidoglycan transglycosylase RlpA, EG45-like domain-containing proteins may adopt a double-psi beta-barrel fold.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680435  26 AQGKAVYYDPPYTRSACYGTQRE---TLVVGVKNNLWQNGRACGRRYRVRCIGATYNFDRACTGRTVDVKVVDFCREPCN 102
Cdd:cd22269   1 DVGTATFYTPPYTPSACYGNDPSpsgNLFAAAGDALWDNGAACGRRYRVRCIGGTNPGPRPCTGGSVVVKIVDYCPGCCG 80

                        90       100
                ....*....|....*....|....*.
gi 30680435 103 GDLNLSRDAFRVIANTDAGNIRVVYT 128
Cdd:cd22269  81 ATFDLSQEAFAKIADPDAGRINIEYV 106

Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Recent studies show that the full-length RlpA protein from Pseudomonas Aeruginosa is an outer membrane protein that is a lytic transglycolase with specificity for peptidoglycan lacking stem peptides. Residue D157 in UniProtKB:Q9X6V6 is critical for lytic activity.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30680435    58 LWQNGRACGRRYRVRCIGA---TYNFDRACT---GRTVDVKVVDFCREPCNGDLNLSRDAFRVIANTDAGNIRVVY 127
Cdd:pfam03330   7 LYNNGTACGECYDVRCLTAahpTLPFGTYCRvlsGRSVIVRITDRGPFPPGRHFDLSGAAFEKLAMPRAGIVPVQY 82

double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains; The double-psi beta-barrel (DPBB) fold is found in a divergent group of proteins, including endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A), EG45-like domain containing proteins, kiwellins, Streptomyces papain inhibitor (SPI), the N-terminal domain of plant and bacterial expansins, GH45 family of endoglucanases, barwins, cerato-platanins, membrane-bound lytic murein transglycosylase A (MltA) and YuiC-like proteins. RlpA may work in tandem with amidases to degrade peptidoglycan (PG) in the division septum and lateral wall to facilitate daughter cell separation. An EG45-like domain containing protein from Arabidopsis thaliana, called plant natriuretic peptide A (AtPNP-A), functions in cell volume regulation. Kiwellin proteins comprise a widespread family of plant-defense proteins that target pathogenic bacterial/fungal effectors that down-regulate plant defense responses. SPI is a stress protein produced under hyperthermal stress conditions that serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes. Some expansin family proteins display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. Endoglucanases (EC 3.2.1.4) catalyze the endohydrolysis of (1-4)-beta-D-glucosidic linkages in cellulose, lichenin, and cereal beta-D-glucans. Animal cellulases, such as endoglucanase EG27II, have great potential for industrial applications such as bioethanol production. Barwin is a basic protein from barley seed. It is a probable plant lectin that may be involved in a defense mechanism. Cerato-platanin is a phytotoxin which causes production of phytoalexin in platanus acerifolia, platanus occidentalis, and platanus orientalis. It also induces cell necrosis. MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. YuiC is a Firmicute stationary phase survival (Sps) protein.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680435  28 GKAVYYDPPYTRSACYGTQRET-LVVGVKNNLWQNGRACGRryrvrCIGATYNfdracTGRTVDVKVVDFCREPCNGDLN 106
Cdd:cd22191   1 GRATYYDPSGGLGACGTTNSDSdLVVALSAALFDSGPLCGK-----CIRITYN-----DGKTVTATVVDECPGCGPGDLD 70

                        90       100
                ....*....|....*....|..
gi 30680435 107 LSRDAFRVIA-NTDAGNIRVVY 127
Cdd:cd22191  71 LSPAAFQALAgDLDGGVIPVTW 92

N-terminal double-psi beta-barrel fold domain of the beta-expansin subfamily; Beta-expansins (EXPB, expansin-B) have cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. They also affect environmental stress responses. The EXPB subfamily is known in the allergen literature as group-1 grass pollen allergens. EXPB of Bermuda, Johnson, and Para grass pollens, is a major cross-reactive allergen for allergic rhinitis patients in subtropical climate. EXPB1 induces extension and stress relaxation of grass cell walls. Wheat TaEXPB7-B is a beta-expansin gene involved in low-temperature stress and abscisic acid responses. Beta-expansins belong to the expansin family of proteins that contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This model represents the N-terminal domain of beta-expansins, which adopts a double-psi beta-barrel (DPBB) fold.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30680435  58 LWQNGRACGRRYRVRCIGatynfDRACTGRTVDVKVVDFCREPCNGD--LNLSRDAFRVIANT-------DAGNIRVVY 127
Cdd:cd22275  43 IFKDGKGCGSCYEVKCTG-----PPACSGKPVTVVITDECPGGPIAPyhFDLSGTAFGAMAKPgqedqlrNAGILDVQY 116

double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar proteins; Endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A, RlpA) is a lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. It adopts a double-psi beta-barrel (DPBB) fold and is one of four SPOR-domain containing proteins in Escherichia coli (including FtsN, DedA and DamX) that bind peptidoglycan (PG) and are targeted to the septum during division. It directly interacts with the divisome protein FtsK in vitro, and deletion of the rlpA gene partially bypasses the requirement for functional FtsK, a large, multi-spanning membrane protein that facilitates double-stranded DNA translocation during division and sporulation in E. coli and Bacillus subtilis, respectively. In Pseudomonas aeruginosa, RlpA contributes to rod shape maintenance and daughter cell separation. The separation of daughter cells requires extensive PG remodeling. It has been suggested that amidases and RlpA work in tandem to degrade PG in the division septum and lateral wall to facilitate daughter cell separation.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 30680435  85 TGRTVDVKVVDfcREPCNGD--LNLSRDAFRVIANTDAGNIRVVYTP 129
Cdd:cd22268  48 NGKSVVVRVND--RGPFVKGriIDLSYAAAKKLGMLGAGVAPVRIEV 92

double-psi beta-barrel fold of the cerato-platanin family; This family represents a group of double-psi beta-barrel (DPBB) fold proteins similar to cerato-platanin, including protein SnodProt1, heat-stable 19 kDa antigen, allergen Asp f 15/Asp f 13, and Epl1 protein. They are involved in plant pathogenesis and elicitation of plant defense responses. Cerato-platanin is a phytotoxin which causes production of phytoalexin in Platanus acerifolia, P. occidentalis, and P. orientalis. It also induces cell necrosis. Cerato-platanin behaves as a fungal toxin. Protein SnodProt1 is also a phytotoxic protein. Heat-stable 19 kDa antigen is a Coccidioides-specific antigen (CS antigen) with serine proteinase activity. Epl1 protein is an elicitor of plant defence responses from Trichoderma virens.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680435  51 VVGVKNNLWQNGRACGRryrvrCIGATYNFdracTGRTVDVKVVDfcrePCNGDLNLSRDAFRVIAN---TDAGNIRVVY 127
Cdd:cd22778  43 IGGSPAITGWNSPSCGS-----CWKLTYAG----NGNTIYVTAVD----SAGEGFVLSTEAFDDLTGgqaVELGTVDVTA 109

                .
gi 30680435 128 T 128
Cdd:cd22778 110 T 110

double-psi beta-barrel fold of Streptomyces papain inhibitor and similar proteins; Streptomyces papain inhibitor (SPI) adopts a rigid, thermo-resistant double-psi-beta-barrel (DPBB) fold that is stabilized by two cysteine bridges. SPI serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes, that is used to covalently and specifically link functional amines to glutamine donor sites of therapeutic proteins. SPI is a stress protein produced under hyperthermal stress conditions, and is able to inhibit the cysteine proteases, papain and bromelain, as well as the bovine serine protease trypsin.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680435  27 QGKAVYYDPPyTRSACyGTQ---RETLVVGVKNNLWQNGRACGRRY-RVRCIGATYNfdractGRTVDVKVVDFCREPCN 102
Cdd:cd22273   2 NGDFTYYNDA-GYGAC-GTPinaATEMLVAVSPAYWTTPNPNNDPPcCNVCVKVTYN------GKTITVPVKDKCPSCGK 73

                        90       100
                ....*....|....*....|.
gi 30680435 103 GDLNLSRDAFRVIANTDAGNI 123
Cdd:cd22273  74 NHIDLSQPAFKQLAPLLVGGI 94