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        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741210158  34 QVGKASFYADKYHGRTTANGERFSQQAATAAHLEFDFGTKVVVTNLANNKSVTVRINDRGPYVRGRIIDLSKSMFKKIAD 113
Cdd:cd22268     1 ETGKASWYGPGFHGRRTASGERYDPNALTAAHKTLPFGTKVRVTNLENGKSVVVRVNDRGPFVKGRIIDLSYAAAKKLGM 80

                          90
                  ....*....|..
gi 1741210158 114 PKVGVIDVSVTV 125
Cdd:cd22268    81 LGAGVAPVRIEV 92

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741210158  34 QVGKASFYADKyhgrtTANGERFSQQAATAAHLEFDFGTKVVVtnlANNKSVTVRINDRGPYVRGRIIDLSKSMFKKIAD 113
Cdd:pfam03330   1 AAGSASLYNNG-----TACGECYDVRCLTAAHPTLPFGTYCRV---LSGRSVIVRITDRGPFPPGRHFDLSGAAFEKLAM 72

                          90
                  ....*....|
gi 1741210158 114 PKVGVIDVSV 123
Cdd:pfam03330  73 PRAGIVPVQY 82

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        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741210158  34 QVGKASFYADKYHGRTTANGERFSQQAATAAHLEFDFGTKVVVTNLANNKSVTVRINDRGPYVRGRIIDLSKSMFKKIAD 113
Cdd:cd22268     1 ETGKASWYGPGFHGRRTASGERYDPNALTAAHKTLPFGTKVRVTNLENGKSVVVRVNDRGPFVKGRIIDLSYAAAKKLGM 80

                          90
                  ....*....|..
gi 1741210158 114 PKVGVIDVSVTV 125
Cdd:cd22268    81 LGAGVAPVRIEV 92

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1741210158  34 QVGKASFYADKyhgrtTANGERFSQQAATAAHLEFDFGTKVVVtnlANNKSVTVRINDRGPYVRGRIIDLSKSMFKKIAD 113
Cdd:pfam03330   1 AAGSASLYNNG-----TACGECYDVRCLTAAHPTLPFGTYCRV---LSGRSVIVRITDRGPFPPGRHFDLSGAAFEKLAM 72

                          90
                  ....*....|
gi 1741210158 114 PKVGVIDVSV 123
Cdd:pfam03330  73 PRAGIVPVQY 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 1741210158  36 GKASFYAdkYHGRTTANGERFSQQAATAA--HLEFD----FGTKVVVTNlANNKSVTVRINDRGPYVRGRIIDLSKSMFK 109
Cdd:cd22191     1 GRATYYD--PSGGLGACGTTNSDSDLVVAlsAALFDsgplCGKCIRITY-NDGKTVTATVVDECPGCGPGDLDLSPAAFQ 77

                          90
                  ....*....|....
gi 1741210158 110 KIADPK-VGVIDVS 122
Cdd:cd22191    78 ALAGDLdGGVIPVT 91

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
                  ....*....|....*....|....*....|....*....|.
gi 1741210158  81 NNKSVTVRINDRGPYVRGRIIDLSKSMFKKIADPKVGVIDV 121
Cdd:cd22269    63 TGGSVVVKIVDYCPGCCGATFDLSQEAFAKIADPDAGRINI 103

Putative EG45-like domain containing protein 1; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1741210158  71 GTKVVVTNLANNKSVTVRINDRGPYVRGRIIDLSKSMFKKIADPKVGVIDV 121
Cdd:PLN03024   71 GPRNAVPHPCTGKSVTVKIVDHCPSGCASTLDLSREAFAQIANPVAGIINI 121