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Conserved domains on  [gi|446657277|ref|WP_000734623|]
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MULTISPECIES: cell wall-binding protein EntD [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_EntD super family cl48941
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.


The actual alignment was detected with superfamily member NF040675:

Pssm-ID: 468641 [Multi-domain]  Cd Length: 310  Bit Score: 570.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKVNGKEAFVSAEF 80
Cdd:NF040675   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKLDGKEAFVSAEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  81 TKSTYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKVGYVHVPFLTGTAPVVEKKEVVTQEEAP 160
Cdd:NF040675  81 TKSTYYVTANVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKAAYVHVPFLTGTAPVIEKKEVVTQEEAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 161 VRVNAPVKNNKVVKNKESVKNVESSKPVAKAKPAVQQVAKSKGTSAPAGGREITVEATAYTAHPSENGTYGGRVLTAMGH 240
Cdd:NF040675 161 ARVNTSVKNNTAVKSKESVKNVESSKPVAKEKPAAKPVAKSTETSAPAGGREITVEATAYTANPSENGTYGGRVLTAMGH 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 241 DLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSANSWGRKSVKVKVIE 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: 570.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKVNGKEAFVSAEF 80
Cdd:NF040675   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKLDGKEAFVSAEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  81 TKSTYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKVGYVHVPFLTGTAPVVEKKEVVTQEEAP 160
Cdd:NF040675  81 TKSTYYVTANVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKAAYVHVPFLTGTAPVIEKKEVVTQEEAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 161 VRVNAPVKNNKVVKNKESVKNVESSKPVAKAKPAVQQVAKSKGTSAPAGGREITVEATAYTAHPSENGTYGGRVLTAMGH 240
Cdd:NF040675 161 ARVNTSVKNNTAVKSKESVKNVESSKPVAKEKPAAKPVAKSTETSAPAGGREITVEATAYTANPSENGTYGGRVLTAMGH 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 241 DLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSANSWGRKSVKVKVIE 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 5.76e-161

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: 450.34  E-value: 5.76e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKVNGKEAFVSAEF 80
Cdd:NF040670   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGHKLDVLNTENGWSQIKLDGKDAFVSAEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  81 TKSTYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKVGYVHVPFLTGTAPVVEKKEvvtqEEAP 160
Cdd:NF040670  81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPVIEKQE----TPAP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 161 VRVNAPVknnkvvknkesvknveSSKPVAKAKPAVQQVAKSKGTSAPAGGREITVEATAYTAHPSEN-GTYGGRVLTAMG 239
Cdd:NF040670 157 AKAEAPA----------------KAQAPAQAKPAAKPAVKAAETSEPSGGRELTVVATAYTAHPSENgGTYGGRVLTAMG 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446657277 240 HDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSANSWGRKSVKVKVIE 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 5.90e-130

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: 376.46  E-value: 5.90e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKVN-GKEAFVSAE 79
Cdd:NF040677   1 MKKFMGIATAAVFGLGIFTTSAKAETIVTTDVLNVRENPTTESKVVGKLLDGYKVNVLHTENGWSKVKLNsGKEAFISAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  80 FTKSTYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKVGYVHVPFLTGTAPV-------VEK-- 150
Cdd:NF040677  81 YTKDTYYVTANVLNVRAGANTDSEILGKLKKDDVIETTHQVQNDWIQFEYNGKTAYVHVPYLTGKAPVkvqpvvkVEKtt 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 151 ---------------------------------------KEVVTQEEAPVR----------VNAPVKNNKVVKNKESVKN 181
Cdd:NF040677 161 kvqdtakvreavkagevaetqakakaqeatkareaaeaqAEAKAQEAAKAReaakaqeeakAQAAAEAQAEAKAQEAAKA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 182 VESSKPVAKA---------------------------------------------------KPAVQQ-VAKSKGTSAPAG 209
Cdd:NF040677 241 REAAKAQAAAeaqaaakaqeaakareaakaqaaaeareaakaqeaaeareaakaqeaakaqKPATQQpVAKETETSAPSS 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 210 GREITVEATAYTAHPSENGTYGG-RVLTAMGHDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDV 288
Cdd:NF040677 321 SRELRVVATAYTADPLENGYKAGdQVKSALGHNLTANPNMKLIAVDPSVIPLGSKVWVEGYGVAIAGDTGGAIKGNKIDV 400

                        410       420
                 ....*....|....*....|.
gi 446657277 289 LVGSDGSANSWGRKSVKVKVI 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 7.69e-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: 362.95  E-value: 7.69e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKVNGKEAFVSAEF 80
Cdd:NF040676   1 MKKVIGAATATVFGLGAFTTTATAETIVTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIELNGKEVFVSSEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  81 TKSTYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKVGYVHVPFLTGTAP-------------- 146
Cdd:NF040676  81 TKDVYHVTANLLNVRTEANTESEILGRLKKDDVIESTHQVKDGWLQFEYKGKTAYANVSFLSSTAPtekkadektkqvak 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 147 ----VVEKKEVVTQ------------------------------------------------------------------ 156
Cdd:NF040676 161 vqksVKAKEEAKTQkvakakettkaqeivkpkeevkvqevvkpkeepkvqeivkpkeevkvqeevkpkeeekvqeivkpk 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 157 ------------EEAPVRVNAPVKNNKVVKNKESVKNVESSKPVAKAK--PAVQQVAKSK-------------------- 202
Cdd:NF040676 241 eeakvqeevkvkEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKeeAKAQEIAKAKeeekaqeiakakeeakarei 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 203 -------------------------------------------------GTSAPAGGREITVEATAYTAHPSENGTYGGR 233
Cdd:NF040676 321 akakeeekareiakakeeakareiakakeeakareiakakeeerakeasKNNIQSAKRELTVVATAYTADPSENGTYGGR 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446657277 234 VLTAMGHDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSANSWGRKSVKVKVI 309
Cdd:NF040676 401 VLTAMGHDLTANPNMRIIAVDPKVIPLGSKVWVEGYGEAIAGDTGSAIKGNRIDVLMGSKSKAMNWGRQTVKVKIL 476
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
 214-310 9.13e-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: 142.17  E-value: 9.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 214 TVEATAYTAHPSENGTYGGRvlTAMGHDLTANpnmKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSD 293
Cdd:COG3584    1 TVTATAYTAGPECTGKGGGI--TASGTRLRPG---GVIAVDPDVIPLGTKVYIEGYGYAVAEDTGGAIKGNRIDIYMPSV 75

                         90
                 ....*....|....*..
gi 446657277 294 GSANSWGRKSVKVKVIE 310
Cdd:COG3584   76 SEALNWGRRTVTVYILE 92
DPBB_YuiC-like cd22786
double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of ...
 210-310 8.92e-35

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: 121.56  E-value: 8.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 210 GREITVEATAYTAHPSENGTYGGRvlTAMGHDLTanpNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVL 289
Cdd:cd22786    1 SKKITVEATAYSPCSSSGGGCYGI--TASGTPLK---RKGTIAVDPSVIPLGTKVYIPGYGYAVVADTGGAIKGNRIDLY 75

                         90       100
                 ....*....|....*....|.
gi 446657277 290 VGSDGSANSWGRKSVKVKVIE 310
Cdd:cd22786   76 FPTHEEAINWGRKTVEVYVLK 96
3D pfam06725
3D domain; This short presumed domain contains three conserved aspartate residues, hence the ...
 249-310 2.16e-18

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: 77.63  E-value: 2.16e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446657277  249 KVIAVDPKVIPLGSKVWVEG-------YGEAIAGDTGGAIKGNRIDVLVGSDGSA-NSWG--RKSVKVKVIE 310
Cdd:pfam06725   1 RSIAVDPSVIPLGTPVYVEGplggkpvYRLAIAQDTGGAIKGNRIDLYFGTGDEAgNLAGlyRKTGRVYILL 72
SH3b smart00287
Bacterial SH3 domain homologues;
84-141 5.57e-08

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 48.87  E-value: 5.57e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 446657277    84 TYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDY-NGKVGYVHVPFL 141
Cdd:smart00287   3 TAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGQDWAKITYgSGQRGYVPGYVV 61
PRK13914 PRK13914
invasion associated endopeptidase;
1-197 2.95e-07

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 51.73  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277   1 MKKLLGIATAavfglGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKmlsGNKLDVINTENGWTKIK-VNGKEAFVS-- 77
Cdd:PRK13914   3 MKKATIAATA-----GIAVTAFAAPTIASASTVVVEAGDTLWGIAQSK---GTTVDAIKKANNLTTDKiVPGQKLQVNev 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  78 AEFTKSTYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYN-GKVGYVHVPFLTG---TAPVVEKKEV 153
Cdd:PRK13914  75 AAAEKTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNdGKTGFVNGKYLTDkvtSTPVAPTQEV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446657277 154 vtQEEAPVRVNAPvknnkvvkNKESVKNVESSKPVAKAKPAVQQ 197
Cdd:PRK13914 155 --KKETTTQQAAP--------AAETKTEVKQTTQATTPAPKVAE 188
 
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: 570.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKVNGKEAFVSAEF 80
Cdd:NF040675   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKLDGKEAFVSAEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  81 TKSTYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKVGYVHVPFLTGTAPVVEKKEVVTQEEAP 160
Cdd:NF040675  81 TKSTYYVTANVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKAAYVHVPFLTGTAPVIEKKEVVTQEEAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 161 VRVNAPVKNNKVVKNKESVKNVESSKPVAKAKPAVQQVAKSKGTSAPAGGREITVEATAYTAHPSENGTYGGRVLTAMGH 240
Cdd:NF040675 161 ARVNTSVKNNTAVKSKESVKNVESSKPVAKEKPAAKPVAKSTETSAPAGGREITVEATAYTANPSENGTYGGRVLTAMGH 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 241 DLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSANSWGRKSVKVKVIE 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 5.76e-161

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: 450.34  E-value: 5.76e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKVNGKEAFVSAEF 80
Cdd:NF040670   1 MKKLIGIATAAVFGLGIFTSSANAETVVTTDVLNVRENPTTESKVVGKLLNGHKLDVLNTENGWSQIKLDGKDAFVSAEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  81 TKSTYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKVGYVHVPFLTGTAPVVEKKEvvtqEEAP 160
Cdd:NF040670  81 TKSIYYVTANVLNVRAEANTNSEILGTLKKDDMIETTNQVQNEWLQFEYNGKTAYVHVPFLTGTAPVIEKQE----TPAP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 161 VRVNAPVknnkvvknkesvknveSSKPVAKAKPAVQQVAKSKGTSAPAGGREITVEATAYTAHPSEN-GTYGGRVLTAMG 239
Cdd:NF040670 157 AKAEAPA----------------KAQAPAQAKPAAKPAVKAAETSEPSGGRELTVVATAYTAHPSENgGTYGGRVLTAMG 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446657277 240 HDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSANSWGRKSVKVKVIE 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 5.90e-130

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: 376.46  E-value: 5.90e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKVN-GKEAFVSAE 79
Cdd:NF040677   1 MKKFMGIATAAVFGLGIFTTSAKAETIVTTDVLNVRENPTTESKVVGKLLDGYKVNVLHTENGWSKVKLNsGKEAFISAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  80 FTKSTYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKVGYVHVPFLTGTAPV-------VEK-- 150
Cdd:NF040677  81 YTKDTYYVTANVLNVRAGANTDSEILGKLKKDDVIETTHQVQNDWIQFEYNGKTAYVHVPYLTGKAPVkvqpvvkVEKtt 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 151 ---------------------------------------KEVVTQEEAPVR----------VNAPVKNNKVVKNKESVKN 181
Cdd:NF040677 161 kvqdtakvreavkagevaetqakakaqeatkareaaeaqAEAKAQEAAKAReaakaqeeakAQAAAEAQAEAKAQEAAKA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 182 VESSKPVAKA---------------------------------------------------KPAVQQ-VAKSKGTSAPAG 209
Cdd:NF040677 241 REAAKAQAAAeaqaaakaqeaakareaakaqaaaeareaakaqeaaeareaakaqeaakaqKPATQQpVAKETETSAPSS 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 210 GREITVEATAYTAHPSENGTYGG-RVLTAMGHDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDV 288
Cdd:NF040677 321 SRELRVVATAYTADPLENGYKAGdQVKSALGHNLTANPNMKLIAVDPSVIPLGSKVWVEGYGVAIAGDTGGAIKGNKIDV 400

                        410       420
                 ....*....|....*....|.
gi 446657277 289 LVGSDGSANSWGRKSVKVKVI 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 7.69e-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: 362.95  E-value: 7.69e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277   1 MKKLLGIATAAVFGLGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIKVNGKEAFVSAEF 80
Cdd:NF040676   1 MKKVIGAATATVFGLGAFTTTATAETIVTADVLNVREKPTTESKVVEKVKNGQELKVINTEDGWSKIELNGKEVFVSSEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  81 TKSTYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYNGKVGYVHVPFLTGTAP-------------- 146
Cdd:NF040676  81 TKDVYHVTANLLNVRTEANTESEILGRLKKDDVIESTHQVKDGWLQFEYKGKTAYANVSFLSSTAPtekkadektkqvak 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 147 ----VVEKKEVVTQ------------------------------------------------------------------ 156
Cdd:NF040676 161 vqksVKAKEEAKTQkvakakettkaqeivkpkeevkvqevvkpkeepkvqeivkpkeevkvqeevkpkeeekvqeivkpk 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 157 ------------EEAPVRVNAPVKNNKVVKNKESVKNVESSKPVAKAK--PAVQQVAKSK-------------------- 202
Cdd:NF040676 241 eeakvqeevkvkEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKeeAKAQEIAKAKeeekaqeiakakeeakarei 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 203 -------------------------------------------------GTSAPAGGREITVEATAYTAHPSENGTYGGR 233
Cdd:NF040676 321 akakeeekareiakakeeakareiakakeeakareiakakeeerakeasKNNIQSAKRELTVVATAYTADPSENGTYGGR 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446657277 234 VLTAMGHDLTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDGSANSWGRKSVKVKVI 309
Cdd:NF040676 401 VLTAMGHDLTANPNMRIIAVDPKVIPLGSKVWVEGYGEAIAGDTGSAIKGNRIDVLMGSKSKAMNWGRQTVKVKIL 476
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
 214-310 9.13e-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: 142.17  E-value: 9.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 214 TVEATAYTAHPSENGTYGGRvlTAMGHDLTANpnmKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSD 293
Cdd:COG3584    1 TVTATAYTAGPECTGKGGGI--TASGTRLRPG---GVIAVDPDVIPLGTKVYIEGYGYAVAEDTGGAIKGNRIDIYMPSV 75

                         90
                 ....*....|....*..
gi 446657277 294 GSANSWGRKSVKVKVIE 310
Cdd:COG3584   76 SEALNWGRRTVTVYILE 92
DPBB_YuiC-like cd22786
double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of ...
 210-310 8.92e-35

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: 121.56  E-value: 8.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 210 GREITVEATAYTAHPSENGTYGGRvlTAMGHDLTanpNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVL 289
Cdd:cd22786    1 SKKITVEATAYSPCSSSGGGCYGI--TASGTPLK---RKGTIAVDPSVIPLGTKVYIPGYGYAVVADTGGAIKGNRIDLY 75

                         90       100
                 ....*....|....*....|.
gi 446657277 290 VGSDGSANSWGRKSVKVKVIE 310
Cdd:cd22786   76 FPTHEEAINWGRKTVEVYVLK 96
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
 215-309 2.16e-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: 120.32  E-value: 2.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 215 VEATAYTAHPSENGTYGGRvlTAMGhdlTANPNMKVIAVDPKVIPLGSKVWVEGYGEAIAGDTGGAIKGNRIDVLVGSDG 294
Cdd:cd14667    1 FTATAYTSCEGCCGGGPGG--TASG---GLPVGGGTIAVDPSVIPLGTKVYIEGYGVYVVEDTGGAIKGNRIDIYMDSHA 75

                         90
                 ....*....|....*
gi 446657277 295 SANSWGRKSVKVKVI 309
Cdd:cd14667   76 EALAFGRRYVEVYIL 90
DPBB_MltA_YuiC-like cd22784
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
 215-308 3.76e-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: 3.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 215 VEATAYTAHPSEngTYGGRVLTAMGHDLTanpNMKVIAVDPKVIPLGSKVWVEG---YGEAIAGDTGGAIKGNRIDVLVG 291
Cdd:cd22784    1 VTVTAYTPDEEQ--TDGGPGITASGVTLR---GYGTVAVDRDLIPLGTKVKIEGpgsGGEYVVLDRGGAIKGNRIDIYFP 75

                         90
                 ....*....|....*..
gi 446657277 292 SDGSANSWGRKSVKVKV 308
Cdd:cd22784   76 SEKEAKKFGRQKVTVTV 92
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 21-136 1.24e-22

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: 90.57  E-value: 1.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  21 SAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTENGWTKIK-VNGKEAFVSAEF---TKSTYYVTAGVLNVRA 96
Cdd:COG3103    2 AAETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVLGRSGGWYKVRySNGKTGWVSSRYltvTPSARERLPDELNLRA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446657277  97 GANTDSEILGKLNKDDVIETTNQvQNEWLQFDYNGkVGYV 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 7.90e-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: 82.81  E-value: 7.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277 215 VEATAYTahPSENGTYGGRVLT-----AMGHDLTANPNMKVIAVDPKVIPLGSKVWVEGY------GEAIAGDTGGAIKG 283
Cdd:cd14486    1 FQATGYT--EWDDGKRPSPPDEfsfsfRLTASGRPPVPYRTIAVDPSVIPLGSVVYIPELrglpndGVFVAEDTGGAIKG 78

                         90       100
                 ....*....|....*....|....*.
gi 446657277 284 NRIDVLVGSDGSANSWGRKSVKVKVI 309
Cdd:cd14486   79 NHIDVYTGDGPDARSNALKTVTVYVV 104
3D pfam06725
3D domain; This short presumed domain contains three conserved aspartate residues, hence the ...
 249-310 2.16e-18

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: 77.63  E-value: 2.16e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446657277  249 KVIAVDPKVIPLGSKVWVEG-------YGEAIAGDTGGAIKGNRIDVLVGSDGSA-NSWG--RKSVKVKVIE 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 1.12e-13

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: 65.74  E-value: 1.12e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446657277 251 IAVDPKVIPLGSKVWVEGY------------GEAIAGDTGGAIKGNRIDVLVGSDGSA 296
Cdd:cd22785   24 VAVDPSVIPLGSVVYIPALdgvklpdgephdGLFIAQDTGGAIKGKHIDVFTGSGDEA 81
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
1-86 3.19e-10

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 55.84  E-value: 3.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277   1 MKKLLGIATAAVFGLGifAGSAKAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVIN--TENGWTKIKVNGKEAFVSA 78
Cdd:COG4991    1 MRRALLAAALALLLLA--PAAAAAATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGctSGGGWCKVSYGGQRGWVSA 78


                 ....*...
gi 446657277  79 EFTKSTYY 86
Cdd:COG4991   79 RYLQVSYD 86
YgiM COG3103
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ...
 82-150 4.35e-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: 56.28  E-value: 4.35e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  82 KSTYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTnQVQNEWLQFDY-NGKVGYVHVPFLTGTAPVVEK 150
Cdd:COG3103    4 ETRYVVDADALNVRSGPGTSYRIVGTLPKGEKVTVL-GRSGGWYKVRYsNGKTGWVSSRYLTVTPSARER 72
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 446657277 251 IAVDPKVIPLGSKVWVE-------GYGEA-----IAGDTGGAIKG-NRIDVLVGS 292
Cdd:cd14485   85 LAVDRSLIPLGAPVWLEtplpdanGGGKPlrrlvIAQDTGGAIKGpVRADLFWGS 139
SH3_3 pfam08239
Bacterial SH3 domain;
90-142 3.15e-08

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 49.17  E-value: 3.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446657277   90 GVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQ-FDYNGKVGYVHVPFLT 142
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGGWYKvRTYDGYEGWVSSSYLS 54
SH3b smart00287
Bacterial SH3 domain homologues;
84-141 5.57e-08

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 48.87  E-value: 5.57e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 446657277    84 TYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDY-NGKVGYVHVPFL 141
Cdd:smart00287   3 TAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGQDWAKITYgSGQRGYVPGYVV 61
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 446657277 237 AMGHDLTAnpnMKVIAVDPKVIPLGSKVWVE-------GYGEA-----IAGDTGGAIKG-NRIDVLVGS 292
Cdd:COG2821  294 ALGVPLTP---GRSIAVDPSLIPLGAPVWLEttlpdanFSGKPlrrlmIAQDTGGAIKGaVRADLFWGT 359
SH3_3 pfam08239
Bacterial SH3 domain;
31-82 2.54e-07

Bacterial SH3 domain;


Pssm-ID: 462405 [Multi-domain]  Cd Length: 54  Bit Score: 46.86  E-value: 2.54e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446657277   31 DVLNVRENPTVESKLVGKMLSGNKLDVINTENG-WTKIK-VNGKEAFVSAEFTK 82
Cdd:pfam08239   1 SGLNVRSGPSTSSEVVGTLPKGEKVEVLEEQGGgWYKVRtYDGYEGWVSSSYLS 54
PRK13914 PRK13914
invasion associated endopeptidase;
1-197 2.95e-07

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 51.73  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277   1 MKKLLGIATAavfglGIFAGSAKAETIVTTDVLNVRENPTVESKLVGKmlsGNKLDVINTENGWTKIK-VNGKEAFVS-- 77
Cdd:PRK13914   3 MKKATIAATA-----GIAVTAFAAPTIASASTVVVEAGDTLWGIAQSK---GTTVDAIKKANNLTTDKiVPGQKLQVNev 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  78 AEFTKSTYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNEWLQFDYN-GKVGYVHVPFLTG---TAPVVEKKEV 153
Cdd:PRK13914  75 AAAEKTEKSVSATWLNVRSGAGVDNSIITSIKGGTKVTVETTESNGWHKITYNdGKTGFVNGKYLTDkvtSTPVAPTQEV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446657277 154 vtQEEAPVRVNAPvknnkvvkNKESVKNVESSKPVAKAKPAVQQ 197
Cdd:PRK13914 155 --KKETTTQQAAP--------AAETKTEVKQTTQATTPAPKVAE 188
YraI COG4991
Uncharacterized conserved protein YraI [Function unknown];
83-137 5.34e-07

Uncharacterized conserved protein YraI [Function unknown];


Pssm-ID: 444015 [Multi-domain]  Cd Length: 92  Bit Score: 46.98  E-value: 5.34e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446657277  83 STYYVTAGVLNVRAGANTDSEILGKLNKDDVIETTNQVQNE-WLQFDYNGKVGYVH 137
Cdd:COG4991   22 AATAVATDDLNLRSGPGTGYPVVGTLPAGATVTVLGCTSGGgWCKVSYGGQRGWVS 77
SH3b smart00287
Bacterial SH3 domain homologues;
23-82 2.99e-03

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 35.39  E-value: 2.99e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446657277    23 KAETIVTTDVLNVRENPTVESKLVGKMLSGNKLDVINTEN-GWTKIKV-NGKEAFVSAEFTK 82
Cdd:smart00287   1 SETAVVTGDGLNVRTGPGTSSPIIGTLKKGDKVKVLGVDGqDWAKITYgSGQRGYVPGYVVN 62
SH3 COG3807
SH3-like domain [Function unknown];
55-137 3.03e-03

SH3-like domain [Function unknown];


Pssm-ID: 443020 [Multi-domain]  Cd Length: 150  Bit Score: 37.58  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446657277  55 LDVINTENGWTKIK-VNGKEAFVSAEFT--KSTYYVTAGVLNVRAGANTDSEILGKLNKDdVIETTNQVQNEWLQFDYNG 131
Cdd:COG3807   52 VEVIAEFGNWRRVRdPEGDEGWVHQSLLsgRRTVIVTGDLANLRASPDENAAVVARLEPG-VVLRLLECDGGWCKVRADG 130


                 ....*.
gi 446657277 132 KVGYVH 137
Cdd:COG3807  131 YKGWVR 136
 
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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