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Conserved domains on  [gi|446587358|ref|WP_000664704|]
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MULTISPECIES: transglycosylase domain-containing protein [Bacillus]

Protein Classification

transglycosylase domain-containing protein( domain architecture ID 11432910)

transglycosylase domain-containing protein catalyzes the polymerization of murein glycan chains; such as biosynthetic peptidoglycan transglycosylase and bifunctional penicillin-binding proteins

CATH:  3.40.710.10|1.10.3810.10
CAZY:  GT51
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0071555|GO:0008955|GO:0009252|GO:0008360
PubMed:  8830253
SCOP:  4002510

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 61-239 1.89e-97

Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 297.60  E-value: 1.89e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  61 EVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIER 140
Cdd:COG0744   81 QIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEALLALKLER 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:COG0744  161 KYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPEAAKERRNLVLDRMVEQ 240

                        170
                 ....*....|....*....
gi 446587358 221 GYINHDEYVQAVSEKLVIR 239
Cdd:COG0744  241 GYITQAEADAAKAEPLTLV 259
 
Name Accession Description Interval E-value
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 61-239 1.89e-97

Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 297.60  E-value: 1.89e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  61 EVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIER 140
Cdd:COG0744   81 QIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEALLALKLER 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:COG0744  161 KYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPEAAKERRNLVLDRMVEQ 240

                        170
                 ....*....|....*....
gi 446587358 221 GYINHDEYVQAVSEKLVIR 239
Cdd:COG0744  241 GYITQAEADAAKAEPLTLV 259
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 42-218 1.06e-84

Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.


Pssm-ID: 459993 [Multi-domain]  Cd Length: 177  Bit Score: 250.13  E-value: 1.06e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358   42 GNVMIEKSDISKLHVPAKlEVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTN 121
Cdd:pfam00912   2 GTLLAELGEENREYVPLD-DIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIVQGGSTITQQLAKNLFLTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  122 ERTFSRKWKEIFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQ 201
Cdd:pfam00912  81 ERTLTRKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLR 160

                         170
                  ....*....|....*..
gi 446587358  202 NYDKAVERRNVVLRLME 218
Cdd:pfam00912 161 NPERAKRRRNLVLDRMV 177
PBP_1a_fam TIGR02074
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ...
 61-237 1.87e-83

penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273955 [Multi-domain]  Cd Length: 531  Bit Score: 258.73  E-value: 1.87e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358   61 EVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIER 140
Cdd:TIGR02074   9 DIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLEGGSTITQQLAKNLYLTNERTITRKIQEALLALKLEQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:TIGR02074  89 KLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAPSAYNPFKNPERAKDRRNLVLSNMVEN 168

                         170
                  ....*....|....*..
gi 446587358  221 GYINHDEYVQAVSEKLV 237
Cdd:TIGR02074 169 GYITAEEAEEAINEPIQ 185
mrcA PRK11636
penicillin-binding protein 1a; Provisional
 53-240 1.68e-66

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 220.77  E-value: 1.68e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  53 KLHVPAKL-EVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKE 131
Cdd:PRK11636  64 KRRIPLTLdQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358 132 IFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRN 211
Cdd:PRK11636 144 AFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAGLPKAPSTFNPLYSMDRAVARRN 223

                        170       180
                 ....*....|....*....|....*....
gi 446587358 212 VVLRLMEKEGYINHDEYVQAVSEKLVIRH 240
Cdd:PRK11636 224 VVLSRMLDEGYITQAQYDQARSEPIVANY 252
 
Name Accession Description Interval E-value
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 61-239 1.89e-97

Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 297.60  E-value: 1.89e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  61 EVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIER 140
Cdd:COG0744   81 QIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEALLALKLER 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:COG0744  161 KYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPEAAKERRNLVLDRMVEQ 240

                        170
                 ....*....|....*....
gi 446587358 221 GYINHDEYVQAVSEKLVIR 239
Cdd:COG0744  241 GYITQAEADAAKAEPLTLV 259
MrcA COG5009
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
61-239 1.76e-92

Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444033 [Multi-domain]  Cd Length: 785  Bit Score: 288.60  E-value: 1.76e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  61 EVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIER 140
Cdd:COG5009   73 EIPPLLINAFLAAEDKRFYEHPGVDPIGIARAAVVNLRTGRRVQGGSTITQQVAKNFLLSPERTLTRKIKEAILALRIEQ 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:COG5009  153 ELSKDEILELYLNKIYLGHRAYGVAAAAQTYFGKSLDELTLAEAAMLAGLPKAPSRYNPIRNPERALERRNYVLGRMLEL 232

                        170
                 ....*....|....*....
gi 446587358 221 GYINHDEYVQAVSEKLVIR 239
Cdd:COG5009  233 GYITQAEYEAAKAEPLTAR 251
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 42-218 1.06e-84

Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.


Pssm-ID: 459993 [Multi-domain]  Cd Length: 177  Bit Score: 250.13  E-value: 1.06e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358   42 GNVMIEKSDISKLHVPAKlEVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTN 121
Cdd:pfam00912   2 GTLLAELGEENREYVPLD-DIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIVQGGSTITQQLAKNLFLTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  122 ERTFSRKWKEIFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQ 201
Cdd:pfam00912  81 ERTLTRKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLR 160

                         170
                  ....*....|....*..
gi 446587358  202 NYDKAVERRNVVLRLME 218
Cdd:pfam00912 161 NPERAKRRRNLVLDRMV 177
PBP_1a_fam TIGR02074
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ...
 61-237 1.87e-83

penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273955 [Multi-domain]  Cd Length: 531  Bit Score: 258.73  E-value: 1.87e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358   61 EVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIER 140
Cdd:TIGR02074   9 DIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLEGGSTITQQLAKNLYLTNERTITRKIQEALLALKLEQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:TIGR02074  89 KLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAPSAYNPFKNPERAKDRRNLVLSNMVEN 168

                         170
                  ....*....|....*..
gi 446587358  221 GYINHDEYVQAVSEKLV 237
Cdd:TIGR02074 169 GYITAEEAEEAINEPIQ 185
mrcA PRK11636
penicillin-binding protein 1a; Provisional
 53-240 1.68e-66

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 220.77  E-value: 1.68e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  53 KLHVPAKL-EVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKE 131
Cdd:PRK11636  64 KRRIPLTLdQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358 132 IFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRN 211
Cdd:PRK11636 144 AFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAGLPKAPSTFNPLYSMDRAVARRN 223

                        170       180
                 ....*....|....*....|....*....
gi 446587358 212 VVLRLMEKEGYINHDEYVQAVSEKLVIRH 240
Cdd:PRK11636 224 VVLSRMLDEGYITQAQYDQARSEPIVANY 252
PBP_1b TIGR02071
penicillin-binding protein 1B; Bacterial that synthesize a cell wall of peptidoglycan (murein) ...
 61-236 4.00e-57

penicillin-binding protein 1B; Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273952 [Multi-domain]  Cd Length: 730  Bit Score: 193.78  E-value: 4.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358   61 EVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIER 140
Cdd:TIGR02071 154 QFPELLVDTLLATEDRDFYEHDGISLYSIGRAVWVNLTAGRTVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMALILDA 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  141 TFTKDEILKLYVSNIYYG----EGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRL 216
Cdd:TIGR02071 234 RYSKDRILELYLNEVYLGqsgdDAIHGFPLASQYYFGRPLGELSLDQVALLVGMVKGPSYYNPWRNPDRALERRNLVLRL 313

                         170       180
                  ....*....|....*....|
gi 446587358  217 MEKEGYINHDEYVQAVSEKL 236
Cdd:TIGR02071 314 LQEQKIIDDEEYDMLSARPL 333
PbpC COG4953
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ...
 61-239 1.88e-53

Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443980 [Multi-domain]  Cd Length: 773  Bit Score: 184.27  E-value: 1.88e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  61 EVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLsknAFLT--NERTFSRKWKEIFYTKKI 138
Cdd:COG4953   72 EVSPRYLQALLAYEDRRFYYHPGVNPLALLRAAWQNLRSGRIVSGGSTLTMQV---ARLLepRPRTLSGKLRQILRALQL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358 139 ERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLME 218
Cdd:COG4953  149 ERRYSKDEILELYLNLAPYGGNIEGVEAASLAYFGKPPSRLSLAEAALLAVLPQAPSRRRPDRNPERARAARDRVLARLA 228

                        170       180
                 ....*....|....*....|.
gi 446587358 219 KEGYINHDEYVQAVSEKLVIR 239
Cdd:COG4953  229 EAGVIDAEEAALALLEPVPAR 249
PRK13481 PRK13481
glycosyltransferase; Provisional
 62-234 1.14e-46

glycosyltransferase; Provisional


Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 155.35  E-value: 1.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  62 VPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVvQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIERT 141
Cdd:PRK13481  53 MPEYVKGAFISMEDERFYKHHGFDLKGTTRALFSTISDRDV-QGGSTITQQVVKNYFYDNERSFTRKVKELFVAHRVEKQ 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358 142 FTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKV-------SQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVL 214
Cdd:PRK13481 132 YSKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVnknsttmSHITVLQSAILASKVNAPSVYNINDMSENFTQRVSTNL 211

                        170       180
                 ....*....|....*....|
gi 446587358 215 RLMEKEGYINHDEYVQAVSE 234
Cdd:PRK13481 212 EKMKQQNYINETQYQQAMSQ 231
mrcB PRK09506
bifunctional glycosyl transferase/transpeptidase; Reviewed
 63-228 2.29e-46

bifunctional glycosyl transferase/transpeptidase; Reviewed


Pssm-ID: 236544 [Multi-domain]  Cd Length: 830  Bit Score: 164.94  E-value: 2.29e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  63 PESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIERTF 142
Cdd:PRK09506 220 PDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMALIMDARY 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358 143 TKDEILKLYVSNIYYGEGA----WGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLME 218
Cdd:PRK09506 300 SKDRILELYLNEVYLGQSGddqiRGFPLASLYYFGRPVEELSLDQQALLVGMVKGASLYNPWRNPKLALERRNLVLRLLQ 379

                        170
                 ....*....|
gi 446587358 219 KEGYINHDEY 228
Cdd:PRK09506 380 QQQIIDQELY 389
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
 61-217 9.83e-42

monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the transglycosylases involved in the late stages of peptidoglycan biosynthesis. Members tend to be small, about 240 amino acids in length, and consist almost entirely of a domain described by pfam00912 for transglycosylases. Species with this protein will have several other transglycosylases as well. All species with this protein are Proteobacteria that produce murein (peptidoglycan). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273951 [Multi-domain]  Cd Length: 224  Bit Score: 142.22  E-value: 9.83e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358   61 EVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIER 140
Cdd:TIGR02070  62 QISPNLKRAVIASEDAKFVEHHGFDWEAIQDALEKNEKSGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLET 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446587358  141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLM 217
Cdd:TIGR02070 142 WWSKQRILEVYLNSVEWGNGVFGAEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQM 218
PRK14850 PRK14850
penicillin-binding protein 1b; Provisional
 53-239 1.26e-40

penicillin-binding protein 1b; Provisional


Pssm-ID: 237835 [Multi-domain]  Cd Length: 764  Bit Score: 148.45  E-value: 1.26e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  53 KLHVPAKlEVPESLTHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEI 132
Cdd:PRK14850 157 RLFIPRN-QYPEMLIKTLLAIEDKYFYEHDGIHLSSIGRAFLVNLMSGHTIQGGSTLTQQLVKNLFLTNTRSLWRKINEI 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358 133 FYTKKIERTFTKDEILKLYVSNIYYG----EGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVE 208
Cdd:PRK14850 236 YMALILDRFYSKDRILELYLNEVYLGqdgnEQIRGFPLASIYYFGRPINELNLDQYALLVGMVKGASLYNPWTNPNLTLK 315

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446587358 209 RRNVVLRLMEKEGYINHDEYVQAVSEKLVIR 239
Cdd:PRK14850 316 RRNLVLFLLYKQKVITRKLYKDLCSRPLNVQ 346
PRK11240 PRK11240
penicillin-binding protein 1C; Provisional
 63-221 1.42e-26

penicillin-binding protein 1C; Provisional


Pssm-ID: 183049 [Multi-domain]  Cd Length: 772  Bit Score: 108.25  E-value: 1.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358  63 PESLtHAFIATEDKRFYHHNGLDYIAIVRASVENIKAGGVVQGGSTITQQLsknAFLTN--ERTFSRKWKEIFYTKKIER 140
Cdd:PRK11240  72 PRYL-EALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQV---ARLLDphPRTFGGKIRQLWRALQLEW 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587358 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVSQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:PRK11240 148 HLSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYAEAALLAVLPQAPSRLRPDRWPERAEAARNKVLERMAEQ 227


                 .
gi 446587358 221 G 221
Cdd:PRK11240 228 G 228
 
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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