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Conserved domains on  [gi|1684957995|gb|TNP10131|]
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enterotoxin [Bacillus cereus]

Protein Classification

3D domain-containing protein( domain architecture ID 13395976)

3D (Asp-Asp-Asp) domain-containing protein contains the critical active site aspartate of MltA-like lytic transglycosylases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
wall_bind_EntD NF040675
cell wall-binding protein EntD; This HMM describes the cell wall-binding protein EntD, as ...
 1-310 0e+00

cell wall-binding protein EntD; This HMM describes the cell wall-binding protein EntD, as found in Bacillus cereus. EntD, like its close homolog EntA, is related to EntB and EntC, but lacks the central region of KAXEXX repeats that EntB and EndC share. Ent proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. They may play a role in maintenance of cell wall structure and stress responses that support virulence, and probably lack any direct role as enterotoxins.


:

Pssm-ID: 468641 [Multi-domain]  Cd Length: 310  Bit Score: 590.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWAKIKLNGKEAFVSAEF 80
Cdd:NF040675    1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKLDGKEAFVSAEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  81 TKSTYYVTPGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKTGYVHMPFLTGTAPVIEKKEVVTQEEAP 160
Cdd:NF040675   81 TKSTYYVTANVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKAAYVHVPFLTGTAPVIEKKEVVTQEEAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 161 VRVNTPVKNNKVVKSKESVKNVESSKPVAKQQSTTKQVTKSTETSAPAGGREITVEATAYTAHPSENGTYGGRVLTAMGH 240
Cdd:NF040675  161 ARVNTSVKNNTAVKSKESVKNVESSKPVAKEKPAAKPVAKSTETSAPAGGREITVEATAYTANPSENGTYGGRVLTAMGH 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 241 DLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSADSWGRKSVKVKVIK 310
Cdd:NF040675  241 DLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSANSWGRKSVKVKVIK 310
 
Name Accession Description Interval E-value
wall_bind_EntD NF040675
cell wall-binding protein EntD; This HMM describes the cell wall-binding protein EntD, as ...
 1-310 0e+00

cell wall-binding protein EntD; This HMM describes the cell wall-binding protein EntD, as found in Bacillus cereus. EntD, like its close homolog EntA, is related to EntB and EntC, but lacks the central region of KAXEXX repeats that EntB and EndC share. Ent proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. They may play a role in maintenance of cell wall structure and stress responses that support virulence, and probably lack any direct role as enterotoxins.


Pssm-ID: 468641 [Multi-domain]  Cd Length: 310  Bit Score: 590.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWAKIKLNGKEAFVSAEF 80
Cdd:NF040675    1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKLDGKEAFVSAEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  81 TKSTYYVTPGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKTGYVHMPFLTGTAPVIEKKEVVTQEEAP 160
Cdd:NF040675   81 TKSTYYVTANVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKAAYVHVPFLTGTAPVIEKKEVVTQEEAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 161 VRVNTPVKNNKVVKSKESVKNVESSKPVAKQQSTTKQVTKSTETSAPAGGREITVEATAYTAHPSENGTYGGRVLTAMGH 240
Cdd:NF040675  161 ARVNTSVKNNTAVKSKESVKNVESSKPVAKEKPAAKPVAKSTETSAPAGGREITVEATAYTANPSENGTYGGRVLTAMGH 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 241 DLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSADSWGRKSVKVKVIK 310
Cdd:NF040675  241 DLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSANSWGRKSVKVKVIK 310
wall_bind_EntA NF040670
cell wall-binding protein EntA; This HMM describes the cell wall-binding protein EntA, as ...
 1-310 2.28e-159

cell wall-binding protein EntA; This HMM describes the cell wall-binding protein EntA, as found in Bacillus cereus. EntA is related to EntB, EntC, and EndD, but it lacks the central region of KAXEXX repeats that EntB and EndC have. EntD also lacks those repeats. Ent proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain.


Pssm-ID: 468636 [Multi-domain]  Cd Length: 291  Bit Score: 446.10  E-value: 2.28e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWAKIKLNGKEAFVSAEF 80
Cdd:NF040670    1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGHKLDVLNTENGWSQIKLDGKDAFVSAEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  81 TKSTYYVTPGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKTGYVHMPFLTGTAPVIEKKEvvtqEEAP 160
Cdd:NF040670   81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPVIEKQE----TPAP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 161 VRVNTPVKNNKVVKSKesvknvesskPVAKQqsttkqVTKSTETSAPAGGREITVEATAYTAHPSENG-TYGGRVLTAMG 239
Cdd:NF040670  157 AKAEAPAKAQAPAQAK----------PAAKP------AVKAAETSEPSGGRELTVVATAYTAHPSENGgTYGGRVLTAMG 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1684957995 240 HDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSADSWGRKSVKVKVIK 310
Cdd:NF040670  221 HDLTANPNMKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSDSAAQKWGRKTVKVKILK 291
wall_bind_EntC NF040677
cell wall-binding protein EntC; This HMM describes the cell wall-binding protein EntC, as ...
 1-309 8.48e-132

cell wall-binding protein EntC; This HMM describes the cell wall-binding protein EntC, as found in Bacillus cereus. EntC is related to EntA, EntB, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468643 [Multi-domain]  Cd Length: 422  Bit Score: 381.08  E-value: 8.48e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWAKIKLN-GKEAFVSAE 79
Cdd:NF040677    1 MKKFMGIATAAVFGLGIFTTSAKAETIVTTDVLNVRENPTTESKVVGKLLDGYKVNVLHTENGWSKVKLNsGKEAFISAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  80 FTKSTYYVTPGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKTGYVHMPFLTGTAPV----IEKKEVVT 155
Cdd:NF040677   81 YTKDTYYVTANVLNVRAGANTDSEILGKLKKDDVIETTHQVQNDWIQFEYNGKTAYVHVPYLTGKAPVkvqpVVKVEKTT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 156 QEEAPVRVNTPVKNNKV------------------------VKSKESVKNVESSKPVAK--------------------- 190
Cdd:NF040677  161 KVQDTAKVREAVKAGEVaetqakakaqeatkareaaeaqaeAKAQEAAKAREAAKAQEEakaqaaaeaqaeakaqeaaka 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 191 ------------------------------------------------------------QQSTTKQ-VTKSTETSAPAG 209
Cdd:NF040677  241 reaakaqaaaeaqaaakaqeaakareaakaqaaaeareaakaqeaaeareaakaqeaakaQKPATQQpVAKETETSAPSS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 210 GREITVEATAYTAHPSENGTYGG-RVLTAMGHDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDV 288
Cdd:NF040677  321 SRELRVVATAYTADPLENGYKAGdQVKSALGHNLTANPNMKLIAVDPSVIPLGSKVWVEGYGVAIAGDTGGAIKGNKIDV 400

                         410       420
                  ....*....|....*....|.
gi 1684957995 289 LVGSDGSADSWGRKSVKVKVI 309
Cdd:NF040677  401 LMPDKGTSSNWGRKTVTVKVL 421
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1-309 3.96e-124

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 363.72  E-value: 3.96e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWAKIKLNGKEAFVSAEF 80
Cdd:NF040676    1 MKKVIGAATATVFGLGAFTTTATAETIVTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIELNGKEVFVSSEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  81 TKSTYYVTPGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKTGYVHMPFLTGTAP-------------- 146
Cdd:NF040676   81 TKDVYHVTANLLNVRTEANTESEILGRLKKDDVIESTHQVKDGWLQFEYKGKTAYANVSFLSSTAPtekkadektkqvak 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 147 ----VIEKKEVVTQ------------------EEAPV----RVNTPVKNNKVVKSKESVKNVESSKPV------------ 188
Cdd:NF040676  161 vqksVKAKEEAKTQkvakakettkaqeivkpkEEVKVqevvKPKEEPKVQEIVKPKEEVKVQEEVKPKeeekvqeivkpk 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 189 ----------------------------------------------------------------------AKQQSTTKQV 198
Cdd:NF040676  241 eeakvqeevkvkeeakvqeiakakeeakaqeiakakeeakaqeiakakeeakaqeiakakeeekaqeiakAKEEAKAREI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 199 TKSTE---------------------------------------------TSAPAGGREITVEATAYTAHPSENGTYGGR 233
Cdd:NF040676  321 AKAKEeekareiakakeeakareiakakeeakareiakakeeerakeaskNNIQSAKRELTVVATAYTADPSENGTYGGR 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1684957995 234 VLTAMGHDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSADSWGRKSVKVKVI 309
Cdd:NF040676  401 VLTAMGHDLTANPNMRIIAVDPKVIPLGSKVWVEGYGEAIAGDTGSAIKGNRIDVLMGSKSKAMNWGRQTVKVKIL 476
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
 214-310 4.49e-43

3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases is part of the Pathway/BioSystem: 3D


Pssm-ID: 442803 [Multi-domain]  Cd Length: 92  Bit Score: 142.94  E-value: 4.49e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 214 TVEATAYTAHPSENGTYGGRvlTAMGHDLTANpnmKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSD 293
Cdd:COG3584     1 TVTATAYTAGPECTGKGGGI--TASGTRLRPG---GVIAVDPDVIPLGTKVYIEGYGYAVAEDTGGAIKGNRIDIYMPSV 75

                          90
                  ....*....|....*..
gi 1684957995 294 GSADSWGRKSVKVKVIK 310
Cdd:COG3584    76 SEALNWGRRTVTVYILE 92
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
 215-309 2.09e-34

Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; This family contains the 3D domain, named for its 3 conserved aspartates, including similar uncharacterized proteins. These proteins contain the critical active site aspartate of mltA-like lytic transglycosylases where the 3D domain forms a larger domain with the N-terminal region. This domain is also found in conjunction with numerous other domains such as the Escherichia coli MltA, a membrane-bound lytic transglycosylase comprised of 2 domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, corresponding to the 3D domain and Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial LTs, which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond.


Pssm-ID: 270620 [Multi-domain]  Cd Length: 90  Bit Score: 120.71  E-value: 2.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 215 VEATAYTAHPSENGTYGGRvlTAMGhdlTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDG 294
Cdd:cd14667     1 FTATAYTSCEGCCGGGPGG--TASG---GLPVGGGTIAVDPSVIPLGTKVYIEGYGVYVVEDTGGAIKGNRIDIYMDSHA 75

                          90
                  ....*....|....*
gi 1684957995 295 SADSWGRKSVKVKVI 309
Cdd:cd14667    76 EALAFGRRYVEVYIL 90
3D pfam06725
3D domain; This short presumed domain contains three conserved aspartate residues, hence the ...
 249-310 6.02e-19

3D domain; This short presumed domain contains three conserved aspartate residues, hence the name 3D. It has been shown to be part of the catalytic double psi beta barrel domain of MltA.


Pssm-ID: 399598 [Multi-domain]  Cd Length: 72  Bit Score: 79.17  E-value: 6.02e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1684957995 249 KVIAVDPKVIPLGSKVWVEG-------YGEAIAGDTGGAIKGNRIDVLVGSDGSA-DSWG--RKSVKVKVIK 310
Cdd:pfam06725   1 RSIAVDPSVIPLGTPVYVEGplggkpvYRLAIAQDTGGAIKGNRIDLYFGTGDEAgNLAGlyRKTGRVYILL 72
SH3b smart00287
Bacterial SH3 domain homologues;
84-137 8.51e-08

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 48.48  E-value: 8.51e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1684957995   84 TYYVTPGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDY-NGKTGYVH 137
Cdd:smart00287   3 TAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGQDWAKITYgSGQRGYVP 57
PRK13914 PRK13914
invasion associated endopeptidase;
19-214 1.43e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 43.25  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  19 AGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTE-NGWAKIKLN-GKEAFVSAEFTKSTYYVTPGVLN--V 94
Cdd:PRK13914   75 AAAEKTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTEsNGWHKITYNdGKTGFVNGKYLTDKVTSTPVAPTqeV 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  95 RAGANTDSEILGKLNKDDVIETTNQvqnewlqfdyngkTGYVHMPFLTGTAPVIEKKEVV-TQEEAPVRVNTPVKNNKVV 173
Cdd:PRK13914  155 KKETTTQQAAPAAETKTEVKQTTQA-------------TTPAPKVAETKETPVVDQNATThAVKSGDTIWALSVKYGVSV 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1684957995 174 KSKESVKNVESSKPVAKQQSTTKQVTKST------ETSAPAGGREIT 214
Cdd:PRK13914  222 QDIMSWNNLSSSSIYVGQKLAIKQTANTAtpkaevKTEAPAAEKQAA 268
 
Name Accession Description Interval E-value
wall_bind_EntD NF040675
cell wall-binding protein EntD; This HMM describes the cell wall-binding protein EntD, as ...
 1-310 0e+00

cell wall-binding protein EntD; This HMM describes the cell wall-binding protein EntD, as found in Bacillus cereus. EntD, like its close homolog EntA, is related to EntB and EntC, but lacks the central region of KAXEXX repeats that EntB and EndC share. Ent proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. They may play a role in maintenance of cell wall structure and stress responses that support virulence, and probably lack any direct role as enterotoxins.


Pssm-ID: 468641 [Multi-domain]  Cd Length: 310  Bit Score: 590.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWAKIKLNGKEAFVSAEF 80
Cdd:NF040675    1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKLDGKEAFVSAEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  81 TKSTYYVTPGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKTGYVHMPFLTGTAPVIEKKEVVTQEEAP 160
Cdd:NF040675   81 TKSTYYVTANVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKAAYVHVPFLTGTAPVIEKKEVVTQEEAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 161 VRVNTPVKNNKVVKSKESVKNVESSKPVAKQQSTTKQVTKSTETSAPAGGREITVEATAYTAHPSENGTYGGRVLTAMGH 240
Cdd:NF040675  161 ARVNTSVKNNTAVKSKESVKNVESSKPVAKEKPAAKPVAKSTETSAPAGGREITVEATAYTANPSENGTYGGRVLTAMGH 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 241 DLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSADSWGRKSVKVKVIK 310
Cdd:NF040675  241 DLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSANSWGRKSVKVKVIK 310
wall_bind_EntA NF040670
cell wall-binding protein EntA; This HMM describes the cell wall-binding protein EntA, as ...
 1-310 2.28e-159

cell wall-binding protein EntA; This HMM describes the cell wall-binding protein EntA, as found in Bacillus cereus. EntA is related to EntB, EntC, and EndD, but it lacks the central region of KAXEXX repeats that EntB and EndC have. EntD also lacks those repeats. Ent proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain.


Pssm-ID: 468636 [Multi-domain]  Cd Length: 291  Bit Score: 446.10  E-value: 2.28e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWAKIKLNGKEAFVSAEF 80
Cdd:NF040670    1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGHKLDVLNTENGWSQIKLDGKDAFVSAEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  81 TKSTYYVTPGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKTGYVHMPFLTGTAPVIEKKEvvtqEEAP 160
Cdd:NF040670   81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPVIEKQE----TPAP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 161 VRVNTPVKNNKVVKSKesvknvesskPVAKQqsttkqVTKSTETSAPAGGREITVEATAYTAHPSENG-TYGGRVLTAMG 239
Cdd:NF040670  157 AKAEAPAKAQAPAQAK----------PAAKP------AVKAAETSEPSGGRELTVVATAYTAHPSENGgTYGGRVLTAMG 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1684957995 240 HDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSADSWGRKSVKVKVIK 310
Cdd:NF040670  221 HDLTANPNMKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSDSAAQKWGRKTVKVKILK 291
wall_bind_EntC NF040677
cell wall-binding protein EntC; This HMM describes the cell wall-binding protein EntC, as ...
 1-309 8.48e-132

cell wall-binding protein EntC; This HMM describes the cell wall-binding protein EntC, as found in Bacillus cereus. EntC is related to EntA, EntB, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468643 [Multi-domain]  Cd Length: 422  Bit Score: 381.08  E-value: 8.48e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWAKIKLN-GKEAFVSAE 79
Cdd:NF040677    1 MKKFMGIATAAVFGLGIFTTSAKAETIVTTDVLNVRENPTTESKVVGKLLDGYKVNVLHTENGWSKVKLNsGKEAFISAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  80 FTKSTYYVTPGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKTGYVHMPFLTGTAPV----IEKKEVVT 155
Cdd:NF040677   81 YTKDTYYVTANVLNVRAGANTDSEILGKLKKDDVIETTHQVQNDWIQFEYNGKTAYVHVPYLTGKAPVkvqpVVKVEKTT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 156 QEEAPVRVNTPVKNNKV------------------------VKSKESVKNVESSKPVAK--------------------- 190
Cdd:NF040677  161 KVQDTAKVREAVKAGEVaetqakakaqeatkareaaeaqaeAKAQEAAKAREAAKAQEEakaqaaaeaqaeakaqeaaka 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 191 ------------------------------------------------------------QQSTTKQ-VTKSTETSAPAG 209
Cdd:NF040677  241 reaakaqaaaeaqaaakaqeaakareaakaqaaaeareaakaqeaaeareaakaqeaakaQKPATQQpVAKETETSAPSS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 210 GREITVEATAYTAHPSENGTYGG-RVLTAMGHDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDV 288
Cdd:NF040677  321 SRELRVVATAYTADPLENGYKAGdQVKSALGHNLTANPNMKLIAVDPSVIPLGSKVWVEGYGVAIAGDTGGAIKGNKIDV 400

                         410       420
                  ....*....|....*....|.
gi 1684957995 289 LVGSDGSADSWGRKSVKVKVI 309
Cdd:NF040677  401 LMPDKGTSSNWGRKTVTVKVL 421
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1-309 3.96e-124

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 363.72  E-value: 3.96e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWAKIKLNGKEAFVSAEF 80
Cdd:NF040676    1 MKKVIGAATATVFGLGAFTTTATAETIVTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIELNGKEVFVSSEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  81 TKSTYYVTPGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKTGYVHMPFLTGTAP-------------- 146
Cdd:NF040676   81 TKDVYHVTANLLNVRTEANTESEILGRLKKDDVIESTHQVKDGWLQFEYKGKTAYANVSFLSSTAPtekkadektkqvak 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 147 ----VIEKKEVVTQ------------------EEAPV----RVNTPVKNNKVVKSKESVKNVESSKPV------------ 188
Cdd:NF040676  161 vqksVKAKEEAKTQkvakakettkaqeivkpkEEVKVqevvKPKEEPKVQEIVKPKEEVKVQEEVKPKeeekvqeivkpk 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 189 ----------------------------------------------------------------------AKQQSTTKQV 198
Cdd:NF040676  241 eeakvqeevkvkeeakvqeiakakeeakaqeiakakeeakaqeiakakeeakaqeiakakeeekaqeiakAKEEAKAREI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 199 TKSTE---------------------------------------------TSAPAGGREITVEATAYTAHPSENGTYGGR 233
Cdd:NF040676  321 AKAKEeekareiakakeeakareiakakeeakareiakakeeerakeaskNNIQSAKRELTVVATAYTADPSENGTYGGR 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1684957995 234 VLTAMGHDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSADSWGRKSVKVKVI 309
Cdd:NF040676  401 VLTAMGHDLTANPNMRIIAVDPKVIPLGSKVWVEGYGEAIAGDTGSAIKGNRIDVLMGSKSKAMNWGRQTVKVKIL 476
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
 214-310 4.49e-43

3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases is part of the Pathway/BioSystem: 3D


Pssm-ID: 442803 [Multi-domain]  Cd Length: 92  Bit Score: 142.94  E-value: 4.49e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 214 TVEATAYTAHPSENGTYGGRvlTAMGHDLTANpnmKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSD 293
Cdd:COG3584     1 TVTATAYTAGPECTGKGGGI--TASGTRLRPG---GVIAVDPDVIPLGTKVYIEGYGYAVAEDTGGAIKGNRIDIYMPSV 75

                          90
                  ....*....|....*..
gi 1684957995 294 GSADSWGRKSVKVKVIK 310
Cdd:COG3584    76 SEALNWGRRTVTVYILE 92
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
 215-309 2.09e-34

Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; This family contains the 3D domain, named for its 3 conserved aspartates, including similar uncharacterized proteins. These proteins contain the critical active site aspartate of mltA-like lytic transglycosylases where the 3D domain forms a larger domain with the N-terminal region. This domain is also found in conjunction with numerous other domains such as the Escherichia coli MltA, a membrane-bound lytic transglycosylase comprised of 2 domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, corresponding to the 3D domain and Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial LTs, which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond.


Pssm-ID: 270620 [Multi-domain]  Cd Length: 90  Bit Score: 120.71  E-value: 2.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 215 VEATAYTAHPSENGTYGGRvlTAMGhdlTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDG 294
Cdd:cd14667     1 FTATAYTSCEGCCGGGPGG--TASG---GLPVGGGTIAVDPSVIPLGTKVYIEGYGVYVVEDTGGAIKGNRIDIYMDSHA 75

                          90
                  ....*....|....*
gi 1684957995 295 SADSWGRKSVKVKVI 309
Cdd:cd14667    76 EALAFGRRYVEVYIL 90
DPBB_YuiC-like cd22786
double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of ...
 210-310 2.36e-34

double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of conserved double-psi beta-barrel (DPBB) fold proteins, such as Bacillus subtilis protein YuiC, cell wall shaping protein YabE, cell wall-binding protein YocH, as well as Clostridium tetani phosphatase-associated protein PapQ. YuiC is a Firmicute stationary phase survival (Sps) protein that closely resembles the Barwin-like endoglucanase beta barrel of MltA. It is a double-psi beta-barrel (DPBB) fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis and may be involved in substrate binding and catalysis.


Pssm-ID: 439263 [Multi-domain]  Cd Length: 96  Bit Score: 120.79  E-value: 2.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 210 GREITVEATAYTAHPSENGTYGGRvlTAMGHDLTanpNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVL 289
Cdd:cd22786     1 SKKITVEATAYSPCSSSGGGCYGI--TASGTPLK---RKGTIAVDPSVIPLGTKVYIPGYGYAVVADTGGAIKGNRIDLY 75

                          90       100
                  ....*....|....*....|.
gi 1684957995 290 VGSDGSADSWGRKSVKVKVIK 310
Cdd:cd22786    76 FPTHEEAINWGRKTVEVYVLK 96
DPBB_MltA_YuiC-like cd22784
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 215-308 2.29e-24

double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and YuiC-like proteins; This family includes two subfamilies of conserved double-psi beta-barrel (DPBB) domain proteins, such as membrane-bound lytic murein transglycosylase A (MltA)-like proteins and YuiC-like proteins. MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in the recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. Bacterial lytic transglycosylases (LTs) are classified into 4 families: family 1 includes slt70 MltC-MltF, family 2 includes MltA, family 3 includes MltB, and family 4 includes proteins of bacteriophage origin. MltA is distinct from other bacterial LTs, which are similar in structure and sequence with a lysozyme-like fold. MltA is a kidney bean-shaped monomeric protein comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which corresponds to a double-psi beta-barrel (DPBB) fold. Domain B also has a beta-barrel fold topology, but it is inserted within the linear sequence of domain A. YuiC is a Firmicute stationary phase survival (Sps) protein that closely resembles the Barwin-like endoglucanase beta barrel of MltA. It is a DPBB fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis and may be involved in substrate binding and catalysis.


Pssm-ID: 439261 [Multi-domain]  Cd Length: 92  Bit Score: 94.25  E-value: 2.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 215 VEATAYTAHPSEngTYGGRVLTAMGHDLTanpNMKVIAVDPKVIPLGSKVWVEG---YGEAIAGDTGGAIKGNRIDVLVG 291
Cdd:cd22784     1 VTVTAYTPDEEQ--TDGGPGITASGVTLR---GYGTVAVDRDLIPLGTKVKIEGpgsGGEYVVLDRGGAIKGNRIDIYFP 75

                          90
                  ....*....|....*..
gi 1684957995 292 SDGSADSWGRKSVKVKV 308
Cdd:cd22784    76 SEKEAKKFGRQKVTVTV 92
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 21-136 1.01e-23

Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];


Pssm-ID: 442337 [Multi-domain]  Cd Length: 119  Bit Score: 93.65  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  21 SAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWAKIKL-NGKEAFVSAEF---TKSTYYVTPGVLNVRA 96
Cdd:COG3103     2 AAETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRYsNGKTGWVSSRYltvTPSARERLPDELNLRA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1684957995  97 GANTDSEILGKLNKDDVIETTNQvQNEWLQFDYNGkTGYV 136
Cdd:COG3103    82 GPSTSSEVLGLLPKGETVTVLKK-SGGWFKVGYRG-TGWV 119
3D_domain cd14486
3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic ...
 215-309 5.22e-20

3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic transglycosylases and numerous other contexts; This family contains the 3D domain, named for its 3 conserved aspartates. It is found in conjunction with numerous other domains such as MltA (membrane-bound lytic murein transglycosylase A). These aspartates are critical active site residues of mltA-like lytic transglycosylases. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. MltA has 2 domains, separated by a large groove, where the peptidoglycan strand binds. The C-terminus has a double-psi beta barrel fold within the 3D domain, which forms the larger A domain along with the N-terminal region of Mlts, but is also found in various other domain architectures. Peptigoglycan (also known as murein) chains, the primary structural component of bacterial cells walls, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc); lytic transglycosylases (LTs) cleave this beta-1-4 bond. Typically, LTs are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, membrane-bound lytic murein transglycosylase E (MltE) is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane- bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and family 4 of bacteriophage origin. While most LTs are related members of the lysozyme-like lytic transglycosylase family, MltA represents a distinct fold and sequence conservation.


Pssm-ID: 270619 [Multi-domain]  Cd Length: 104  Bit Score: 83.19  E-value: 5.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995 215 VEATAYTahPSENGTYGGRVLT-----AMGHDLTANPNMKVIAVDPKVIPLGSKVWVEGY------GEAIAGDTGGAIKG 283
Cdd:cd14486     1 FQATGYT--EWDDGKRPSPPDEfsfsfRLTASGRPPVPYRTIAVDPSVIPLGSVVYIPELrglpndGVFVAEDTGGAIKG 78

                          90       100
                  ....*....|....*....|....*.
gi 1684957995 284 NRIDVLVGSDGSADSWGRKSVKVKVI 309
Cdd:cd14486    79 NHIDVYTGDGPDARSNALKTVTVYVV 104
3D pfam06725
3D domain; This short presumed domain contains three conserved aspartate residues, hence the ...
 249-310 6.02e-19

3D domain; This short presumed domain contains three conserved aspartate residues, hence the name 3D. It has been shown to be part of the catalytic double psi beta barrel domain of MltA.


Pssm-ID: 399598 [Multi-domain]  Cd Length: 72  Bit Score: 79.17  E-value: 6.02e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1684957995 249 KVIAVDPKVIPLGSKVWVEG-------YGEAIAGDTGGAIKGNRIDVLVGSDGSA-DSWG--RKSVKVKVIK 310
Cdd:pfam06725   1 RSIAVDPSVIPLGTPVYVEGplggkpvYRLAIAQDTGGAIKGNRIDLYFGTGDEAgNLAGlyRKTGRVYILL 72
DPBB_MltA-like cd22785
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 251-296 5.02e-14

double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and similar proteins; MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in the recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. Bacterial lytic transglycosylases (LTs) are classified into 4 families: family 1 includes slt70 MltC-MltF, family 2 includes MltA, family 3 includes MltB, and family 4 includes proteins of bacteriophage origin. MltA is distinct from other bacterial LTs, which are similar in structure and sequence with a lysozyme-like fold. MltA is a kidney bean-shaped monomeric protein comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which corresponds to a double-psi beta-barrel (DPBB) fold. Domain B also has a beta-barrel fold topology, but it is inserted within the linear sequence of domain A. This model corresponds to the DPBB fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis. It is involved in substrate binding and catalysis.


Pssm-ID: 439262 [Multi-domain]  Cd Length: 97  Bit Score: 66.90  E-value: 5.02e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1684957995 251 IAVDPKVIPLGSKVWVEGY------------GEAIAGDTGGAIKGNRIDVLVGSDGSA 296
Cdd:cd22785    24 VAVDPSVIPLGSVVYIPALdgvklpdgephdGLFIAQDTGGAIKGKHIDVFTGSGDEA 81
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
1-92 1.94e-11

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 59.31  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995   1 MKKLLGIATAAVFGLGifAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVIN--TENGWAKIKLNGKEAFVSA 78
Cdd:COG4991     1 MRRALLAAALALLLLA--PAAAAAATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCKVSYGGQRGWVSA 78

                          90
                  ....*....|....
gi 1684957995  79 EFTKSTYYVTPGVL 92
Cdd:COG4991    79 RYLQVSYDGQPVPL 92
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 82-183 1.81e-10

Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only];


Pssm-ID: 442337 [Multi-domain]  Cd Length: 119  Bit Score: 57.44  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  82 KSTYYVTPGVLNVRAGANTDSEILGKLNKDDVIETTnQVQNEWLQFDY-NGKTGYVHMPFLTGTAPviekKEVVTQEEAP 160
Cdd:COG3103     4 ETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVL-GRSGGWYKVRYsNGKTGWVSSRYLTVTPS----ARERLPDELN 78

                          90       100
                  ....*....|....*....|...
gi 1684957995 161 VRvNTPVKNNKVVKSKESVKNVE 183
Cdd:COG3103    79 LR-AGPSTSSEVLGLLPKGETVT 100
mltA_like_LT_A cd14485
Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B; ...
 251-292 2.86e-09

Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B; Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.


Pssm-ID: 270618 [Multi-domain]  Cd Length: 159  Bit Score: 54.95  E-value: 2.86e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1684957995 251 IAVDPKVIPLGSKVWVE-------GYGEA-----IAGDTGGAIKG-NRIDVLVGS 292
Cdd:cd14485    85 LAVDRSLIPLGAPVWLEtplpdanGGGKPlrrlvIAQDTGGAIKGpVRADLFWGS 139
SH3_3 pfam08239
Bacterial SH3 domain;
90-142 9.27e-09

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 50.71  E-value: 9.27e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1684957995  90 GVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQ-FDYNGKTGYVHMPFLT 142
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGGWYKvRTYDGYEGWVSSSYLS 54
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
83-146 8.21e-08

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 49.29  E-value: 8.21e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1684957995  83 STYYVTPGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNE-WLQFDYNGKTGYVHMPFLTGTAP 146
Cdd:COG4991    22 AATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGCTSGGgWCKVSYGGQRGWVSARYLQVSYD 86
SH3b smart00287
Bacterial SH3 domain homologues;
84-137 8.51e-08

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 48.48  E-value: 8.51e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1684957995   84 TYYVTPGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDY-NGKTGYVH 137
Cdd:smart00287   3 TAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGQDWAKITYgSGQRGYVP 57
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
237-292 9.27e-08

Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 52.95  E-value: 9.27e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1684957995 237 AMGHDLTAnpnMKVIAVDPKVIPLGSKVWVE-------GYGEA-----IAGDTGGAIKG-NRIDVLVGS 292
Cdd:COG2821   294 ALGVPLTP---GRSIAVDPSLIPLGAPVWLEttlpdanFSGKPlrrlmIAQDTGGAIKGaVRADLFWGT 359
SH3_3 pfam08239
Bacterial SH3 domain;
31-82 9.79e-08

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 48.01  E-value: 9.79e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1684957995  31 DVLNVRENPTVESKLVGKMLSGNKLDVINTENG-WAKIKL-NGKEAFVSAEFTK 82
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGgWYKVRTyDGYEGWVSSSYLS 54
PRK13914 PRK13914
invasion associated endopeptidase;
19-214 1.43e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 43.25  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  19 AGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTE-NGWAKIKLN-GKEAFVSAEFTKSTYYVTPGVLN--V 94
Cdd:PRK13914   75 AAAEKTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTEsNGWHKITYNdGKTGFVNGKYLTDKVTSTPVAPTqeV 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  95 RAGANTDSEILGKLNKDDVIETTNQvqnewlqfdyngkTGYVHMPFLTGTAPVIEKKEVV-TQEEAPVRVNTPVKNNKVV 173
Cdd:PRK13914  155 KKETTTQQAAPAAETKTEVKQTTQA-------------TTPAPKVAETKETPVVDQNATThAVKSGDTIWALSVKYGVSV 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1684957995 174 KSKESVKNVESSKPVAKQQSTTKQVTKST------ETSAPAGGREIT 214
Cdd:PRK13914  222 QDIMSWNNLSSSSIYVGQKLAIKQTANTAtpkaevKTEAPAAEKQAA 268
SH3 COG3807
SH3-like domain [Function unknown];
28-146 4.19e-04

SH3-like domain [Function unknown];


Pssm-ID: 443020 [Multi-domain]  Cd Length: 150  Bit Score: 39.89  E-value: 4.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684957995  28 VTTDVLNVRENPTVESKLVGKML-SGNKLDVINTENGWAKIK-LNGKEAFVSAEFT--KSTYYVTPGVLNVRAGANTDSE 103
Cdd:COG3807    24 LKSDEVNLRDGPSTKYPILWVYKrRGLPVEVIAEFGNWRRVRdPEGDEGWVHQSLLsgRRTVIVTGDLANLRASPDENAA 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1684957995 104 ILGKLNKDdVIETTNQVQNEWLQFDYNGKTGYVHMPFLTGTAP 146
Cdd:COG3807   104 VVARLEPG-VVLRLLECDGGWCKVRADGYKGWVRQSLLWGVYP 145
SH3b smart00287
Bacterial SH3 domain homologues;
23-82 5.39e-04

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 37.70  E-value: 5.39e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1684957995   23 KAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTEN-GWAKIKL-NGKEAFVSAEFTK 82
Cdd:smart00287   1 SETAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGqDWAKITYgSGQRGYVPGYVVN 62
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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