SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2693085432 184 YIQVAAGSTLANIEALASTLREQY--KLPTNIVQKDDIYRLHLGPIKDTPHANEVLKKLKQNQFQNAFLL 251
Cdd:pfam05036   6 YVQLGAFSNEANAEALAAKLRAKGfaAYVAVTSKGGGLYRVRVGPFASREEARAALKKLKALAGLSPFVV 75

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 2693085432  81 EEGIASWYGRKFHGYHTSNGETYDMFAMTAAHKTLPLPSFVKVTNTANGKSVIVRVNDRGPFHDDRIIDLSYAAAYKLGY 160
Cdd:cd22268     1 ETGKASWYGPGFHGRRTASGERYDPNALTAAHKTLPFGTKVRVTNLENGKSVVVRVNDRGPFVKGRIIDLSYAAAKKLGM 80

                          90
                  ....*....|.
gi 2693085432 161 YTHGTAKVKLE 171
Cdd:cd22268    81 LGAGVAPVRIE 91

endolytic peptidoglycan transglycosylase RlpA;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2693085432  57 ASASRPYTVLGKSYSPMLDETGFNEEGIASWYGRKFHGYHTSNGETYDMFAMTAAHKTLPLPSFVKVTNTANGKSVIVRV 136
Cdd:PRK10672   55 PTANQDYQRNGKSYKIVQDPSNFSQAGLAAIYDAEAGSNLTASGERFDPNALTAAHPTLPIPSYVRVTNLANGRMIVVRI 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2693085432 137 NDRGPFHDDRIIDLSYAAAYKLGyyTHGTAKVKLEavtlagatarqtYIQVAAGSTLANIEALASTLREQ-YKLP 210
Cdd:PRK10672  135 NDRGPYGPGRVIDLSRAAADRLN--TSNNTKVRID------------PIIVAPDGSLSGPGTAGTTVAKQsYALP 195

SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2693085432 184 YIQVAAGSTLANIEALASTLREQY--KLPTNIVQKDDIYRLHLGPIKDTPHANEVLKKLKQNQFQNAFLL 251
Cdd:pfam05036   6 YVQLGAFSNEANAEALAAKLRAKGfaAYVAVTSKGGGLYRVRVGPFASREEARAALKKLKALAGLSPFVV 75

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 2693085432  81 EEGIASWYGRKFHGYHTSNGETYDMFAMTAAHKTLPLPSFVKVTNTANGKSVIVRVNDRGPFHDDRIIDLSYAAAYKLGY 160
Cdd:cd22268     1 ETGKASWYGPGFHGRRTASGERYDPNALTAAHKTLPFGTKVRVTNLENGKSVVVRVNDRGPFVKGRIIDLSYAAAKKLGM 80

                          90
                  ....*....|.
gi 2693085432 161 YTHGTAKVKLE 171
Cdd:cd22268    81 LGAGVAPVRIE 91

endolytic peptidoglycan transglycosylase RlpA;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2693085432  57 ASASRPYTVLGKSYSPMLDETGFNEEGIASWYGRKFHGYHTSNGETYDMFAMTAAHKTLPLPSFVKVTNTANGKSVIVRV 136
Cdd:PRK10672   55 PTANQDYQRNGKSYKIVQDPSNFSQAGLAAIYDAEAGSNLTASGERFDPNALTAAHPTLPIPSYVRVTNLANGRMIVVRI 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2693085432 137 NDRGPFHDDRIIDLSYAAAYKLGyyTHGTAKVKLEavtlagatarqtYIQVAAGSTLANIEALASTLREQ-YKLP 210
Cdd:PRK10672  135 NDRGPYGPGRVIDLSRAAADRLN--TSNNTKVRID------------PIIVAPDGSLSGPGTAGTTVAKQsYALP 195

SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2693085432 184 YIQVAAGSTLANIEALASTLREQY--KLPTNIVQKDDIYRLHLGPIKDTPHANEVLKKLKQNQFQNAFLL 251
Cdd:pfam05036   6 YVQLGAFSNEANAEALAAKLRAKGfaAYVAVTSKGGGLYRVRVGPFASREEARAALKKLKALAGLSPFVV 75

Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2693085432  82 EGIASWYGRKFHGYHTSNGETYDMFAMTAAHKTLPLPSFVKVTNTANGKSVIVRVNDRGPFHDDRIIDLSYAAAYKLGY- 160
Cdd:COG3087    14 ALLLELSAEAAAAASDNLRLAAGSAAAPALAEDALVASAAKAGLAETGAKAGAILAAAALAALNAAAAALAAASAAAAAa 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2693085432 161 ---------YTHGTAKVKLEAVTLAGATARQTYIQVAAGSTLANIEALASTLREQYkLPTNIVQ----KDDIYRLHLGPI 227
Cdd:COG3087    94 aapaaaaaeAAAAPAGMAKKEAAAAPAAKKPYYVQVGAFRSRANAERLRARLALLG-LEARVVEvevgGGTWYRVRVGPF 172

                         170       180
                  ....*....|....*....|...
gi 2693085432 228 KDTPHANEVLKKLKQNQFQNAFL 250
Cdd:COG3087   173 SSRAEAEKAREKLKAAGIDALVV 195

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 2693085432  83 GIASWYGrkFHGYHTSNGETYDMFAMTAAhktLPLPSF---------VKVTNTaNGKSVIVRVNDRGPFHDDRIIDLSYA 153
Cdd:cd22191     1 GRATYYD--PSGGLGACGTTNSDSDLVVA---LSAALFdsgplcgkcIRITYN-DGKTVTATVVDECPGCGPGDLDLSPA 74

                  ....*.
gi 2693085432 154 AAYKLG 159
Cdd:cd22191    75 AFQALA 80