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Conserved domains on  [gi|822525635|ref|WP_046955549|]
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MULTISPECIES: cell wall-binding protein EntA [Bacillus]

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_EntA NF040670
cell wall-binding protein EntA; This HMM describes the cell wall-binding protein EntA, as ...
 1-292 0e+00

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: 515.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTENGWSKITLDGKDAFVSTEF 80
Cdd:NF040670   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGHKLDVLNTENGWSQIKLDGKDAFVSAEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPVIEKQEQPAPAKTV 160
Cdd:NF040670  81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPVIEKQETPAPAKAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 161 aPAKAQAPAAQAKPAAKPAVKAAETSTPSGGRELTVVATAYTAHPSENGGTYGGRVLTAMGHDLTANPNMKMIAVDPKVI 240
Cdd:NF040670 161 -APAKAQAPAQAKPAAKPAVKAAETSEPSGGRELTVVATAYTAHPSENGGTYGGRVLTAMGHDLTANPNMKMIAVDPKVI 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 822525635 241 PLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSDSAAQKWGRKTVKVKILK 292
Cdd:NF040670 240 PLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSDSAAQKWGRKTVKVKILK 291
 
Name Accession Description Interval E-value
wall_bind_EntA NF040670
cell wall-binding protein EntA; This HMM describes the cell wall-binding protein EntA, as ...
 1-292 0e+00

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: 515.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTENGWSKITLDGKDAFVSTEF 80
Cdd:NF040670   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGHKLDVLNTENGWSQIKLDGKDAFVSAEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPVIEKQEQPAPAKTV 160
Cdd:NF040670  81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPVIEKQETPAPAKAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 161 aPAKAQAPAAQAKPAAKPAVKAAETSTPSGGRELTVVATAYTAHPSENGGTYGGRVLTAMGHDLTANPNMKMIAVDPKVI 240
Cdd:NF040670 161 -APAKAQAPAQAKPAAKPAVKAAETSEPSGGRELTVVATAYTAHPSENGGTYGGRVLTAMGHDLTANPNMKMIAVDPKVI 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 822525635 241 PLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSDSAAQKWGRKTVKVKILK 292
Cdd:NF040670 240 PLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSDSAAQKWGRKTVKVKILK 291
wall_bind_EntD NF040675
cell wall-binding protein EntD; This HMM describes the cell wall-binding protein EntD, as ...
 1-292 1.30e-164

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: 459.17  E-value: 1.30e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTENGWSKITLDGKDAFVSTEF 80
Cdd:NF040675   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKLDGKEAFVSAEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPVIEKQEQP----AP 156
Cdd:NF040675  81 TKSTYYVTANVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKAAYVHVPFLTGTAPVIEKKEVVtqeeAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 157 AKT---------------VAPAKAQAPAAQAKPAAKPAVKAAETSTPSGGRELTVVATAYTAHPSENGgTYGGRVLTAMG 221
Cdd:NF040675 161 ARVntsvknntavkskesVKNVESSKPVAKEKPAAKPVAKSTETSAPAGGREITVEATAYTANPSENG-TYGGRVLTAMG 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822525635 222 HDLTANPNMKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSDSAAQKWGRKTVKVKILK 292
Cdd:NF040675 240 HDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSANSWGRKSVKVKVIK 310
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1-291 6.54e-129

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: 374.89  E-value: 6.54e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTENGWSKITLDGKDAFVSTEF 80
Cdd:NF040676   1 MKKVIGAATATVFGLGAFTTTATAETIVTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIELNGKEVFVSSEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAP-------------- 146
Cdd:NF040676  81 TKDVYHVTANLLNVRTEANTESEILGRLKKDDVIESTHQVKDGWLQFEYKGKTAYANVSFLSSTAPtekkadektkqvak 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 147 ----VIEKQE---------------------------------------------------------------------- 152
Cdd:NF040676 161 vqksVKAKEEaktqkvakakettkaqeivkpkeevkvqevvkpkeepkvqeivkpkeevkvqeevkpkeeekvqeivkpk 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 153 ------------------QPAPAKTVAPAKAQAPAAQAKPAAKPAVKAAE------------------------------ 184
Cdd:NF040676 241 eeakvqeevkvkeeakvqEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEakaqeiakakeeekaqeiakakeeakarei 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 185 --------------------------------------------------TSTPSGGRELTVVATAYTAHPSENGgTYGG 214
Cdd:NF040676 321 akakeeekareiakakeeakareiakakeeakareiakakeeerakeaskNNIQSAKRELTVVATAYTADPSENG-TYGG 399

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822525635 215 RVLTAMGHDLTANPNMKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSDSAAQKWGRKTVKVKIL 291
Cdd:NF040676 400 RVLTAMGHDLTANPNMRIIAVDPKVIPLGSKVWVEGYGEAIAGDTGSAIKGNRIDVLMGSKSKAMNWGRQTVKVKIL 476
wall_bind_EntC NF040677
cell wall-binding protein EntC; This HMM describes the cell wall-binding protein EntC, as ...
 1-291 2.11e-127

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: 369.14  E-value: 2.11e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTENGWSKITLD-GKDAFVSTE 79
Cdd:NF040677   1 MKKFMGIATAAVFGLGIFTTSAKAETIVTTDVLNVRENPTTESKVVGKLLDGYKVNVLHTENGWSKVKLNsGKEAFISAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  80 FTKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPV-------IEK-- 150
Cdd:NF040677  81 YTKDTYYVTANVLNVRAGANTDSEILGKLKKDDVIETTHQVQNDWIQFEYNGKTAYVHVPYLTGKAPVkvqpvvkVEKtt 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 151 -------------------------------------------QEQPAPAKTVAPAKAQAPAAQAKPAAKPAVKA----- 182
Cdd:NF040677 161 kvqdtakvreavkagevaetqakakaqeatkareaaeaqaeakAQEAAKAREAAKAQEEAKAQAAAEAQAEAKAQeaaka 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 183 ------------------------------------------------------------------------AETSTPSG 190
Cdd:NF040677 241 reaakaqaaaeaqaaakaqeaakareaakaqaaaeareaakaqeaaeareaakaqeaakaqkpatqqpvakeTETSAPSS 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 191 GRELTVVATAYTAHPSENGGTYGGRVLTAMGHDLTANPNMKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDI 270
Cdd:NF040677 321 SRELRVVATAYTADPLENGYKAGDQVKSALGHNLTANPNMKLIAVDPSVIPLGSKVWVEGYGVAIAGDTGGAIKGNKIDV 400

                        410       420
                 ....*....|....*....|.
gi 822525635 271 LLGSDSAAQKWGRKTVKVKIL 291
Cdd:NF040677 401 LMPDKGTSSNWGRKTVTVKVL 421
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
 195-292 5.04e-44

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: 144.87  E-value: 5.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 195 TVVATAYTAHPSENGGTYGgrvLTAMGHDLTANpnmKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGS 274
Cdd:COG3584    1 TVTATAYTAGPECTGKGGG---ITASGTRLRPG---GVIAVDPDVIPLGTKVYIEGYGYAVAEDTGGAIKGNRIDIYMPS 74

                         90
                 ....*....|....*...
gi 822525635 275 DSAAQKWGRKTVKVKILK 292
Cdd:COG3584   75 VSEALNWGRRTVTVYILE 92
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
 196-291 2.03e-35

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: 122.63  E-value: 2.03e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 196 VVATAYTAHPSENGGTYGGrvlTAMGhdlTANPNMKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSD 275
Cdd:cd14667    1 FTATAYTSCEGCCGGGPGG---TASG---GLPVGGGTIAVDPSVIPLGTKVYIEGYGVYVVEDTGGAIKGNRIDIYMDSH 74

                         90
                 ....*....|....*.
gi 822525635 276 SAAQKWGRKTVKVKIL 291
Cdd:cd14667   75 AEALAFGRRYVEVYIL 90
3D pfam06725
3D domain; This short presumed domain contains three conserved aspartate residues, hence the ...
 233-292 2.33e-20

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: 82.64  E-value: 2.33e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  233 IAVDPKVIPLGSKVWVEG-------YGEAIAGDTGGAIKGNRIDILLGS-DSAAQKWG--RKTVKVKILK 292
Cdd:pfam06725   3 IAVDPSVIPLGTPVYVEGplggkpvYRLAIAQDTGGAIKGNRIDLYFGTgDEAGNLAGlyRKTGRVYILL 72
SH3b smart00287
Bacterial SH3 domain homologues;
85-141 7.77e-07

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 45.40  E-value: 7.77e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 822525635    85 YYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEY-NGKTAYVHVPFL 141
Cdd:smart00287   4 AVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGQDWAKITYgSGQRGYVPGYVV 61
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 33-123 7.43e-06

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 46.66  E-value: 7.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  33 LNVRENPTTESKVVGKLLNGNKIDV------------QNTENGWSKITLDG--KDAFVS-------------TEFTKSIY 85
Cdd:NF038016   1 LNVRSGPATDSAVVGTLANGAKVTVvckvrgeqirgtVRTTSQWDRLGSGRyvSHAYVRwspslptcpwcapKAATVATV 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 822525635  86 YVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNE 123
Cdd:NF038016  81 TTGGGALNVRAAAGTGAARVGTVANGATVTVECQVWGQ 118
PRK13914 PRK13914
invasion associated endopeptidase;
20-119 2.79e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 42.10  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  20 SSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTE-NGWSKITL-DGKDAFVSTEF--TKSIYYVTANVLNVR 95
Cdd:PRK13914  76 AAEKTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTEsNGWHKITYnDGKTGFVNGKYltDKVTSTPVAPTQEVK 155

                         90       100
                 ....*....|....*....|....
gi 822525635  96 AEANTNSEILGTLKKDDMIETTNQ 119
Cdd:PRK13914 156 KETTTQQAAPAAETKTEVKQTTQA 179
 
Name Accession Description Interval E-value
wall_bind_EntA NF040670
cell wall-binding protein EntA; This HMM describes the cell wall-binding protein EntA, as ...
 1-292 0e+00

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: 515.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTENGWSKITLDGKDAFVSTEF 80
Cdd:NF040670   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGHKLDVLNTENGWSQIKLDGKDAFVSAEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPVIEKQEQPAPAKTV 160
Cdd:NF040670  81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPVIEKQETPAPAKAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 161 aPAKAQAPAAQAKPAAKPAVKAAETSTPSGGRELTVVATAYTAHPSENGGTYGGRVLTAMGHDLTANPNMKMIAVDPKVI 240
Cdd:NF040670 161 -APAKAQAPAQAKPAAKPAVKAAETSEPSGGRELTVVATAYTAHPSENGGTYGGRVLTAMGHDLTANPNMKMIAVDPKVI 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 822525635 241 PLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSDSAAQKWGRKTVKVKILK 292
Cdd:NF040670 240 PLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSDSAAQKWGRKTVKVKILK 291
wall_bind_EntD NF040675
cell wall-binding protein EntD; This HMM describes the cell wall-binding protein EntD, as ...
 1-292 1.30e-164

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: 459.17  E-value: 1.30e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTENGWSKITLDGKDAFVSTEF 80
Cdd:NF040675   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKLDGKEAFVSAEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPVIEKQEQP----AP 156
Cdd:NF040675  81 TKSTYYVTANVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKAAYVHVPFLTGTAPVIEKKEVVtqeeAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 157 AKT---------------VAPAKAQAPAAQAKPAAKPAVKAAETSTPSGGRELTVVATAYTAHPSENGgTYGGRVLTAMG 221
Cdd:NF040675 161 ARVntsvknntavkskesVKNVESSKPVAKEKPAAKPVAKSTETSAPAGGREITVEATAYTANPSENG-TYGGRVLTAMG 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822525635 222 HDLTANPNMKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSDSAAQKWGRKTVKVKILK 292
Cdd:NF040675 240 HDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSANSWGRKSVKVKVIK 310
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1-291 6.54e-129

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: 374.89  E-value: 6.54e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTENGWSKITLDGKDAFVSTEF 80
Cdd:NF040676   1 MKKVIGAATATVFGLGAFTTTATAETIVTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIELNGKEVFVSSEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAP-------------- 146
Cdd:NF040676  81 TKDVYHVTANLLNVRTEANTESEILGRLKKDDVIESTHQVKDGWLQFEYKGKTAYANVSFLSSTAPtekkadektkqvak 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 147 ----VIEKQE---------------------------------------------------------------------- 152
Cdd:NF040676 161 vqksVKAKEEaktqkvakakettkaqeivkpkeevkvqevvkpkeepkvqeivkpkeevkvqeevkpkeeekvqeivkpk 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 153 ------------------QPAPAKTVAPAKAQAPAAQAKPAAKPAVKAAE------------------------------ 184
Cdd:NF040676 241 eeakvqeevkvkeeakvqEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEakaqeiakakeeekaqeiakakeeakarei 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 185 --------------------------------------------------TSTPSGGRELTVVATAYTAHPSENGgTYGG 214
Cdd:NF040676 321 akakeeekareiakakeeakareiakakeeakareiakakeeerakeaskNNIQSAKRELTVVATAYTADPSENG-TYGG 399

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822525635 215 RVLTAMGHDLTANPNMKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSDSAAQKWGRKTVKVKIL 291
Cdd:NF040676 400 RVLTAMGHDLTANPNMRIIAVDPKVIPLGSKVWVEGYGEAIAGDTGSAIKGNRIDVLMGSKSKAMNWGRQTVKVKIL 476
wall_bind_EntC NF040677
cell wall-binding protein EntC; This HMM describes the cell wall-binding protein EntC, as ...
 1-291 2.11e-127

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: 369.14  E-value: 2.11e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTENGWSKITLD-GKDAFVSTE 79
Cdd:NF040677   1 MKKFMGIATAAVFGLGIFTTSAKAETIVTTDVLNVRENPTTESKVVGKLLDGYKVNVLHTENGWSKVKLNsGKEAFISAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  80 FTKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPV-------IEK-- 150
Cdd:NF040677  81 YTKDTYYVTANVLNVRAGANTDSEILGKLKKDDVIETTHQVQNDWIQFEYNGKTAYVHVPYLTGKAPVkvqpvvkVEKtt 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 151 -------------------------------------------QEQPAPAKTVAPAKAQAPAAQAKPAAKPAVKA----- 182
Cdd:NF040677 161 kvqdtakvreavkagevaetqakakaqeatkareaaeaqaeakAQEAAKAREAAKAQEEAKAQAAAEAQAEAKAQeaaka 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 183 ------------------------------------------------------------------------AETSTPSG 190
Cdd:NF040677 241 reaakaqaaaeaqaaakaqeaakareaakaqaaaeareaakaqeaaeareaakaqeaakaqkpatqqpvakeTETSAPSS 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 191 GRELTVVATAYTAHPSENGGTYGGRVLTAMGHDLTANPNMKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDI 270
Cdd:NF040677 321 SRELRVVATAYTADPLENGYKAGDQVKSALGHNLTANPNMKLIAVDPSVIPLGSKVWVEGYGVAIAGDTGGAIKGNKIDV 400

                        410       420
                 ....*....|....*....|.
gi 822525635 271 LLGSDSAAQKWGRKTVKVKIL 291
Cdd:NF040677 401 LMPDKGTSSNWGRKTVTVKVL 421
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
 195-292 5.04e-44

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: 144.87  E-value: 5.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 195 TVVATAYTAHPSENGGTYGgrvLTAMGHDLTANpnmKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGS 274
Cdd:COG3584    1 TVTATAYTAGPECTGKGGG---ITASGTRLRPG---GVIAVDPDVIPLGTKVYIEGYGYAVAEDTGGAIKGNRIDIYMPS 74

                         90
                 ....*....|....*...
gi 822525635 275 DSAAQKWGRKTVKVKILK 292
Cdd:COG3584   75 VSEALNWGRRTVTVYILE 92
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
 196-291 2.03e-35

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: 122.63  E-value: 2.03e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 196 VVATAYTAHPSENGGTYGGrvlTAMGhdlTANPNMKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDILLGSD 275
Cdd:cd14667    1 FTATAYTSCEGCCGGGPGG---TASG---GLPVGGGTIAVDPSVIPLGTKVYIEGYGVYVVEDTGGAIKGNRIDIYMDSH 74

                         90
                 ....*....|....*.
gi 822525635 276 SAAQKWGRKTVKVKIL 291
Cdd:cd14667   75 AEALAFGRRYVEVYIL 90
DPBB_YuiC-like cd22786
double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of ...
 191-292 1.87e-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: 120.40  E-value: 1.87e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 191 GRELTVVATAYTAHPSENGGTYGgrvLTAMGHDLTanpNMKMIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDI 270
Cdd:cd22786    1 SKKITVEATAYSPCSSSGGGCYG---ITASGTPLK---RKGTIAVDPSVIPLGTKVYIPGYGYAVVADTGGAIKGNRIDL 74

                         90       100
                 ....*....|....*....|..
gi 822525635 271 LLGSDSAAQKWGRKTVKVKILK 292
Cdd:cd22786   75 YFPTHEEAINWGRKTVEVYVLK 96
DPBB_MltA_YuiC-like cd22784
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 196-290 2.61e-25

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: 96.56  E-value: 2.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 196 VVATAYTAHPSENGGTYGgrvLTAMGHDLTanpNMKMIAVDPKVIPLGSKVWVEG---YGEAIAGDTGGAIKGNRIDILL 272
Cdd:cd22784    1 VTVTAYTPDEEQTDGGPG---ITASGVTLR---GYGTVAVDRDLIPLGTKVKIEGpgsGGEYVVLDRGGAIKGNRIDIYF 74

                         90
                 ....*....|....*...
gi 822525635 273 GSDSAAQKWGRKTVKVKI 290
Cdd:cd22784   75 PSEKEAKKFGRQKVTVTV 92
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 20-136 4.20e-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: 91.72  E-value: 4.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  20 SSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTENGWSKITL-DGKDAFVSTEF---TKSIYYVTANVLNVR 95
Cdd:COG3103    1 AAAETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRYsNGKTGWVSSRYltvTPSARERLPDELNLR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 822525635  96 AEANTNSEILGTLKKDDMIETTNQvQNEWLQFEYNGkTAYV 136
Cdd:COG3103   81 AGPSTSSEVLGLLPKGETVTVLKK-SGGWFKVGYRG-TGWV 119
3D_domain cd14486
3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic ...
 198-291 1.20e-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: 84.73  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635 198 ATAYTA-----HPSENGGTYGGRVLTAMGhdlTANPNMKMIAVDPKVIPLGSKVWVEGY------GEAIAGDTGGAIKGN 266
Cdd:cd14486    3 ATGYTEwddgkRPSPPDEFSFSFRLTASG---RPPVPYRTIAVDPSVIPLGSVVYIPELrglpndGVFVAEDTGGAIKGN 79

                         90       100
                 ....*....|....*....|....*
gi 822525635 267 RIDILLGSDSAAQKWGRKTVKVKIL 291
Cdd:cd14486   80 HIDVYTGDGPDARSNALKTVTVYVV 104
3D pfam06725
3D domain; This short presumed domain contains three conserved aspartate residues, hence the ...
 233-292 2.33e-20

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: 82.64  E-value: 2.33e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  233 IAVDPKVIPLGSKVWVEG-------YGEAIAGDTGGAIKGNRIDILLGS-DSAAQKWG--RKTVKVKILK 292
Cdd:pfam06725   3 IAVDPSVIPLGTPVYVEGplggkpvYRLAIAQDTGGAIKGNRIDLYFGTgDEAGNLAGlyRKTGRVYILL 72
DPBB_MltA-like cd22785
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 233-291 5.36e-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: 66.51  E-value: 5.36e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822525635 233 IAVDPKVIPLGSKVWVEGY------------GEAIAGDTGGAIKGNRIDILLGSDSAAQK---WGRKTVKVKIL 291
Cdd:cd22785   24 VAVDPSVIPLGSVVYIPALdgvklpdgephdGLFIAQDTGGAIKGKHIDVFTGSGDEAGElagKLNHTGRVYVL 97
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
1-86 4.70e-12

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 60.85  E-value: 4.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635   1 MKKLIGIATAAVFGLGifTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQN--TENGWSKITLDGKDAFVST 78
Cdd:COG4991    1 MRRALLAAALALLLLA--PAAAAAATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCKVSYGGQRGWVSA 78


                 ....*...
gi 822525635  79 EFTKSIYY 86
Cdd:COG4991   79 RYLQVSYD 86
mltA_like_LT_A cd14485
Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B; ...
 233-278 2.28e-10

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: 58.03  E-value: 2.28e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 822525635 233 IAVDPKVIPLGSKVWVE-------GYGEA-----IAGDTGGAIKG-NRIDILLGSDSAA 278
Cdd:cd14485   85 LAVDRSLIPLGAPVWLEtplpdanGGGKPlrrlvIAQDTGGAIKGpVRADLFWGSGDEA 143
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 85-153 2.55e-09

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: 53.97  E-value: 2.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  85 YYVTANVLNVRAEANTNSEILGTLKKDDMIETTnQVQNEWLQFEY-NGKTAYVHVPFLTGTAPVIEKQEQ 153
Cdd:COG3103    7 YVVDADALNVRSGPGTSYRIVGTLPKGEKVTVL-GRSGGWYKVRYsNGKTGWVSSRYLTVTPSARERLPD 75
SH3_3 pfam08239
Bacterial SH3 domain;
31-82 1.07e-08

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 50.32  E-value: 1.07e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 822525635   31 DVLNVRENPTTESKVVGKLLNGNKIDV-QNTENGWSKI-TLDGKDAFVSTEFTK 82
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVlEEQGGGWYKVrTYDGYEGWVSSSYLS 54
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
219-283 1.37e-08

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


Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 55.27  E-value: 1.37e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822525635 219 AMGHDLTAnpnMKMIAVDPKVIPLGSKVWVE-------GYGEA-----IAGDTGGAIKG-NRIDILLGS-DSAAQKWGR 283
Cdd:COG2821  294 ALGVPLTP---GRSIAVDPSLIPLGAPVWLEttlpdanFSGKPlrrlmIAQDTGGAIKGaVRADLFWGTgDEAGERAGR 369
SH3_3 pfam08239
Bacterial SH3 domain;
90-142 1.90e-07

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 46.86  E-value: 1.90e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 822525635   90 NVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQ-FEYNGKTAYVHVPFLT 142
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGGWYKvRTYDGYEGWVSSSYLS 54
SH3b smart00287
Bacterial SH3 domain homologues;
85-141 7.77e-07

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 45.40  E-value: 7.77e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 822525635    85 YYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEY-NGKTAYVHVPFL 141
Cdd:smart00287   4 AVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGQDWAKITYgSGQRGYVPGYVV 61
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 18-71 8.06e-07

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: 47.04  E-value: 8.06e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 822525635  18 FTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTENGWSKITLDG 71
Cdd:COG3103   62 YLTVTPSARERLPDELNLRAGPSTSSEVLGLLPKGETVTVLKKSGGWFKVGYRG 115
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 33-123 7.43e-06

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 46.66  E-value: 7.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  33 LNVRENPTTESKVVGKLLNGNKIDV------------QNTENGWSKITLDG--KDAFVS-------------TEFTKSIY 85
Cdd:NF038016   1 LNVRSGPATDSAVVGTLANGAKVTVvckvrgeqirgtVRTTSQWDRLGSGRyvSHAYVRwspslptcpwcapKAATVATV 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 822525635  86 YVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNE 123
Cdd:NF038016  81 TTGGGALNVRAAAGTGAARVGTVANGATVTVECQVWGQ 118
SH3b smart00287
Bacterial SH3 domain homologues;
24-82 9.11e-05

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 39.62  E-value: 9.11e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822525635    24 AETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTEN-GWSKITLD-GKDAFVSTEFTK 82
Cdd:smart00287   2 ETAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGqDWAKITYGsGQRGYVPGYVVN 62
PRK13914 PRK13914
invasion associated endopeptidase;
20-119 2.79e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 42.10  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  20 SSANAETVVTTDVLNVRENPTTESKVVGKLLNGNKIDVQNTE-NGWSKITL-DGKDAFVSTEF--TKSIYYVTANVLNVR 95
Cdd:PRK13914  76 AAEKTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTEsNGWHKITYnDGKTGFVNGKYltDKVTSTPVAPTQEVK 155

                         90       100
                 ....*....|....*....|....
gi 822525635  96 AEANTNSEILGTLKKDDMIETTNQ 119
Cdd:PRK13914 156 KETTTQQAAPAAETKTEVKQTTQA 179
PRK13914 PRK13914
invasion associated endopeptidase;
87-211 4.73e-03

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 38.24  E-value: 4.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525635  87 VTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYN-GKTAYVHVPFLTG---TAPVIEKQE--------QP 154
Cdd:PRK13914  84 VSATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNdGKTGFVNGKYLTDkvtSTPVAPTQEvkketttqQA 163

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 822525635 155 APAktvapAKAQAPAAQAKPAAKPAVKAAETstpsggRELTVVATAYTAHPSENGGT 211
Cdd:PRK13914 164 APA-----AETKTEVKQTTQATTPAPKVAET------KETPVVDQNATTHAVKSGDT 209
 
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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