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Conserved domains on  [gi|2670045098|ref|WP_330956053|]
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MULTISPECIES: Ig-like domain-containing protein [unclassified Mycolicibacterium]

Protein Classification

L,D-transpeptidase( domain architecture ID 16057555)

L,D-transpeptidase catalyzes the formation of 3->3 peptidoglycan cross-links

CATH:  2.40.440.10|2.60.40.3780|2.60.40.3710
EC:  2.3.2.-
Gene Ontology:  GO:0018104|GO:0071972
PubMed:  18266857
SCOP:  4000465|4002015

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Big_10 pfam17964
Bacterial Ig domain; This entry represents a bacterial Ig-like domain found associated with ...
 65-251 1.77e-71

Bacterial Ig domain; This entry represents a bacterial Ig-like domain found associated with transpeptidase domains.


:

Pssm-ID: 465591 [Multi-domain]  Cd Length: 182  Bit Score: 222.50  E-value: 1.77e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098  65 AEVDPLARILVTAETGTIDSVTLVNDGGKQIPGVLTPDAKTWKPTTSLGFGRTYTMTVSAKGPGGMPTRQVTTFSTLTPS 144
Cdd:pfam17964   2 TGVNPGTPVTVTVAGGTLTDVTVTDSDGKEVPGKLSADGTSWTSTEPLGYGTTYTVTATAKGAGGKATTQTSSFTTVSPA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098 145 NQAQVYLdgtsggMLQDGAKYGVGMVIVARFDEPITDKASAERRLKVTTNPPVFGAWNWIDDQTAHWRPEKYYAPGTQVT 224
Cdd:pfam17964  82 NTTSGTL------TPLDGSTVGVGMPISINFDKPVTDKAAVEKAITVTTSPAVEGAWHWFGDQRVDWRPKEYWPPGTKVT 155

                         170       180
                  ....*....|....*....|....*..
gi 2670045098 225 VNADIYGARLGDGLYGAEDEKVSFTIG 251
Cdd:pfam17964 156 VDARLYGVDLGDGVYGQQDRTVTFTIG 182
ErfK COG1376
Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];
257-388 4.30e-27

Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440986 [Multi-domain]  Cd Length: 121  Bit Score: 104.56  E-value: 4.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098 257 IADDNTKQVSVFENGKLVRTMPTSMGMGGTETigdttlsfwtPRGIYTVMDKANPVIMDSSTFGlPVNSRLGYKE-TIPY 335
Cdd:COG1376     2 VVDLSEQRLYVYEDGGLVRTYPVSVGRPGFPT----------PTGTFRVLRKAENPTWTPPAEM-PAGMPGGPDNpLGPY 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2670045098 336 ATRISTDGIYLHQLNAtVWAQGnTNTSHGCLNLNSENAKWFFDFAVPGDIVEV 388
Cdd:COG1376    71 ALYLSDGGYGIHGTPW-PSSIG-RNVSHGCIRLSNEDAKWLYDRVPVGTPVVV 121
 
Name Accession Description Interval E-value
Big_10 pfam17964
Bacterial Ig domain; This entry represents a bacterial Ig-like domain found associated with ...
 65-251 1.77e-71

Bacterial Ig domain; This entry represents a bacterial Ig-like domain found associated with transpeptidase domains.


Pssm-ID: 465591 [Multi-domain]  Cd Length: 182  Bit Score: 222.50  E-value: 1.77e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098  65 AEVDPLARILVTAETGTIDSVTLVNDGGKQIPGVLTPDAKTWKPTTSLGFGRTYTMTVSAKGPGGMPTRQVTTFSTLTPS 144
Cdd:pfam17964   2 TGVNPGTPVTVTVAGGTLTDVTVTDSDGKEVPGKLSADGTSWTSTEPLGYGTTYTVTATAKGAGGKATTQTSSFTTVSPA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098 145 NQAQVYLdgtsggMLQDGAKYGVGMVIVARFDEPITDKASAERRLKVTTNPPVFGAWNWIDDQTAHWRPEKYYAPGTQVT 224
Cdd:pfam17964  82 NTTSGTL------TPLDGSTVGVGMPISINFDKPVTDKAAVEKAITVTTSPAVEGAWHWFGDQRVDWRPKEYWPPGTKVT 155

                         170       180
                  ....*....|....*....|....*..
gi 2670045098 225 VNADIYGARLGDGLYGAEDEKVSFTIG 251
Cdd:pfam17964 156 VDARLYGVDLGDGVYGQQDRTVTFTIG 182
LDT_IgD_like_2 cd13432
IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found ...
 154-251 5.12e-51

IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3->3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain; this model represents the repeat adjacent to the catalytic domain.


Pssm-ID: 240447  Cd Length: 99  Bit Score: 166.92  E-value: 5.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098 154 TSGGMLQDGAKYGVGMVIVARFDEPITDKASAERRLKVTTNPPVFGAWNWIDDQTAHWRPEKYYAPGTQVTVNADIYGAR 233
Cdd:cd13432     2 TASVNPLDGETVGVGMPVIVTFDEPVTDRAAVEKALKVTTSPPVEGAWYWLSDREVHWRPKEYWPPGTKVTVDANLYGVD 81

                          90
                  ....*....|....*...
gi 2670045098 234 LGDGLYGAEDEKVSFTIG 251
Cdd:cd13432    82 LGDGVYGQEDRSTTFTIG 99
ErfK COG1376
Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];
257-388 4.30e-27

Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440986 [Multi-domain]  Cd Length: 121  Bit Score: 104.56  E-value: 4.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098 257 IADDNTKQVSVFENGKLVRTMPTSMGMGGTETigdttlsfwtPRGIYTVMDKANPVIMDSSTFGlPVNSRLGYKE-TIPY 335
Cdd:COG1376     2 VVDLSEQRLYVYEDGGLVRTYPVSVGRPGFPT----------PTGTFRVLRKAENPTWTPPAEM-PAGMPGGPDNpLGPY 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2670045098 336 ATRISTDGIYLHQLNAtVWAQGnTNTSHGCLNLNSENAKWFFDFAVPGDIVEV 388
Cdd:COG1376    71 ALYLSDGGYGIHGTPW-PSSIG-RNVSHGCIRLSNEDAKWLYDRVPVGTPVVV 121
YkuD_like cd16913
L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like ...
 257-389 8.33e-20

L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.


Pssm-ID: 341130 [Multi-domain]  Cd Length: 121  Bit Score: 84.67  E-value: 8.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098 257 IADDNTKQVSVFENGKLVRTMPTSMGMGGTETigdttlsfwtPRGIYTVMDKANPVIMDSSTFGLPvnsrLGYKETIPYA 336
Cdd:cd16913     3 VVDLSEQRLYLYENGKLVKTYPVSTGKPGTPT----------PTGTFRITRKVKNPTWTGPPSIPP----GPYNPLGPYA 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2670045098 337 TRIST--DGIYLHQLNATVWaqGNTNTSHGCLNLNSENAKWFFDFAVPGDIVEVR 389
Cdd:cd16913    69 LRLSGpgSGIGIHGTPWPSS--IGRPASHGCIRLSNEDAKELYDWVPVGTPVVIY 121
YkuD pfam03734
L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. ...
 267-388 1.34e-13

L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. It has been shown that this domain can act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. This gives bacteria resistance to beta-lactam antibiotics that inhibit PBPs which usually carry out the cross-linking reaction. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue. Several members of this family contain peptidoglycan binding domains. The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. The two beta-sheets form a cradle capped by an alpha-helix. This family was formerly called the ErfK/YbiS/YcfS/YnhG family, but is now named after the first protein of known structure.


Pssm-ID: 461031 [Multi-domain]  Cd Length: 89  Bit Score: 65.83  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098 267 VFENGKLVRTMPTSMGMGGTETigdttlsfwtPRGIYTVmdkanpvimdsstfglpvnsrlgyketipyatristdgIYL 346
Cdd:pfam03734  16 LYENGGLVLRYPVSVGRGDGPT----------PTGTFRI--------------------------------------IYI 47

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2670045098 347 HQLNATVWAQGNTNTSHGCLNLNSENAKWFFDFAVPGDIVEV 388
Cdd:pfam03734  48 HDTGTPDLFGLGRRRSHGCIRLSNEDAKELYDRVLVGTPVVI 89
 
Name Accession Description Interval E-value
Big_10 pfam17964
Bacterial Ig domain; This entry represents a bacterial Ig-like domain found associated with ...
 65-251 1.77e-71

Bacterial Ig domain; This entry represents a bacterial Ig-like domain found associated with transpeptidase domains.


Pssm-ID: 465591 [Multi-domain]  Cd Length: 182  Bit Score: 222.50  E-value: 1.77e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098  65 AEVDPLARILVTAETGTIDSVTLVNDGGKQIPGVLTPDAKTWKPTTSLGFGRTYTMTVSAKGPGGMPTRQVTTFSTLTPS 144
Cdd:pfam17964   2 TGVNPGTPVTVTVAGGTLTDVTVTDSDGKEVPGKLSADGTSWTSTEPLGYGTTYTVTATAKGAGGKATTQTSSFTTVSPA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098 145 NQAQVYLdgtsggMLQDGAKYGVGMVIVARFDEPITDKASAERRLKVTTNPPVFGAWNWIDDQTAHWRPEKYYAPGTQVT 224
Cdd:pfam17964  82 NTTSGTL------TPLDGSTVGVGMPISINFDKPVTDKAAVEKAITVTTSPAVEGAWHWFGDQRVDWRPKEYWPPGTKVT 155

                         170       180
                  ....*....|....*....|....*..
gi 2670045098 225 VNADIYGARLGDGLYGAEDEKVSFTIG 251
Cdd:pfam17964 156 VDARLYGVDLGDGVYGQQDRTVTFTIG 182
LDT_IgD_like_2 cd13432
IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found ...
 154-251 5.12e-51

IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3->3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain; this model represents the repeat adjacent to the catalytic domain.


Pssm-ID: 240447  Cd Length: 99  Bit Score: 166.92  E-value: 5.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098 154 TSGGMLQDGAKYGVGMVIVARFDEPITDKASAERRLKVTTNPPVFGAWNWIDDQTAHWRPEKYYAPGTQVTVNADIYGAR 233
Cdd:cd13432     2 TASVNPLDGETVGVGMPVIVTFDEPVTDRAAVEKALKVTTSPPVEGAWYWLSDREVHWRPKEYWPPGTKVTVDANLYGVD 81

                          90
                  ....*....|....*...
gi 2670045098 234 LGDGLYGAEDEKVSFTIG 251
Cdd:cd13432    82 LGDGVYGQEDRSTTFTIG 99
ErfK COG1376
Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];
257-388 4.30e-27

Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440986 [Multi-domain]  Cd Length: 121  Bit Score: 104.56  E-value: 4.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098 257 IADDNTKQVSVFENGKLVRTMPTSMGMGGTETigdttlsfwtPRGIYTVMDKANPVIMDSSTFGlPVNSRLGYKE-TIPY 335
Cdd:COG1376     2 VVDLSEQRLYVYEDGGLVRTYPVSVGRPGFPT----------PTGTFRVLRKAENPTWTPPAEM-PAGMPGGPDNpLGPY 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2670045098 336 ATRISTDGIYLHQLNAtVWAQGnTNTSHGCLNLNSENAKWFFDFAVPGDIVEV 388
Cdd:COG1376    71 ALYLSDGGYGIHGTPW-PSSIG-RNVSHGCIRLSNEDAKWLYDRVPVGTPVVV 121
LDT_IgD_like cd13430
IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found ...
 156-250 3.47e-26

IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3->3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain.


Pssm-ID: 240445  Cd Length: 98  Bit Score: 101.25  E-value: 3.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098 156 GGMLQDGAKYGVGMVIVARFDEPITDKASAERRLKVTTNPPVFGAWNWIDD-QTAHWRPEKYYAPGTQVTVNADIYGARL 234
Cdd:cd13430     3 YVMPGDGEVVGVGAPVAIRFDENIADRGAAEKAITITTDPPVEGAFYWLPDgRRVRWRPEHFWKPGTAVDVAANTYGLDL 82

                          90
                  ....*....|....*.
gi 2670045098 235 GDGLYGAEDEKVSFTI 250
Cdd:cd13430    83 GEGMFGADNVQLHFQI 98
YkuD_like cd16913
L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like ...
 257-389 8.33e-20

L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.


Pssm-ID: 341130 [Multi-domain]  Cd Length: 121  Bit Score: 84.67  E-value: 8.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098 257 IADDNTKQVSVFENGKLVRTMPTSMGMGGTETigdttlsfwtPRGIYTVMDKANPVIMDSSTFGLPvnsrLGYKETIPYA 336
Cdd:cd16913     3 VVDLSEQRLYLYENGKLVKTYPVSTGKPGTPT----------PTGTFRITRKVKNPTWTGPPSIPP----GPYNPLGPYA 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2670045098 337 TRIST--DGIYLHQLNATVWaqGNTNTSHGCLNLNSENAKWFFDFAVPGDIVEVR 389
Cdd:cd16913    69 LRLSGpgSGIGIHGTPWPSS--IGRPASHGCIRLSNEDAKELYDWVPVGTPVVIY 121
YkuD pfam03734
L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. ...
 267-388 1.34e-13

L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. It has been shown that this domain can act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. This gives bacteria resistance to beta-lactam antibiotics that inhibit PBPs which usually carry out the cross-linking reaction. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue. Several members of this family contain peptidoglycan binding domains. The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. The two beta-sheets form a cradle capped by an alpha-helix. This family was formerly called the ErfK/YbiS/YcfS/YnhG family, but is now named after the first protein of known structure.


Pssm-ID: 461031 [Multi-domain]  Cd Length: 89  Bit Score: 65.83  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098 267 VFENGKLVRTMPTSMGMGGTETigdttlsfwtPRGIYTVmdkanpvimdsstfglpvnsrlgyketipyatristdgIYL 346
Cdd:pfam03734  16 LYENGGLVLRYPVSVGRGDGPT----------PTGTFRI--------------------------------------IYI 47

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2670045098 347 HQLNATVWAQGNTNTSHGCLNLNSENAKWFFDFAVPGDIVEV 388
Cdd:pfam03734  48 HDTGTPDLFGLGRRRSHGCIRLSNEDAKELYDRVLVGTPVVI 89
LDT_IgD_like_1 cd13431
IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found ...
 161-227 9.73e-11

IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3->3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain; this model represents the first (N-terminal) repeat in LdtMt2 and related proteins.


Pssm-ID: 240446  Cd Length: 95  Bit Score: 58.09  E-value: 9.73e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2670045098 161 DGAKYGVGMVIVARFDEPITDKASAERRLKVTTNPPVFGAWNWIDDQTAHWRPEKYYAPGTQVTVNA 227
Cdd:cd13431    17 DGAVVGVAHPVVVTFADPVADRAAAENAIGITVAGPVAGGFSWTDDEPLGWTPTYFWPAHATVTVGA 83
LDT_IgD_like_1 cd13431
IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found ...
 48-143 5.00e-09

IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3->3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain; this model represents the first (N-terminal) repeat in LdtMt2 and related proteins.


Pssm-ID: 240446  Cd Length: 95  Bit Score: 53.09  E-value: 5.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098  48 QASPTEPAKLTITPKPNAEVDPLARILVTAETGTIDSVTLVNDGGKQIPGVLtPDAKTWKPTTSLGFGRTYTMTVSAKGP 127
Cdd:cd13431     2 PAPPLPVPVATVSPADGAVVGVAHPVVVTFADPVADRAAAENAIGITVAGPV-AGGFSWTDDEPLGWTPTYFWPAHATVT 80

                          90
                  ....*....|....*.
gi 2670045098 128 GGMPTRQvTTFSTLTP 143
Cdd:cd13431    81 VGAGGTR-TSFRTGDA 95
LDT_IgD_like cd13430
IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found ...
 56-140 2.15e-03

IgD-like repeat domain of mycobacterial L,D-transpeptidases; Immunoglobulin-like domain found in actinobacterial L,D-transpeptidases, including Mycobacterium tuberculosis LdtMt2, which is a non-classical transpeptidase that generates 3->3 transpeptide linkages. LdtMt2 is associated with virulence and resistance to amoxicillin. This domain may occur in a tandem-repeat arrangement and is found N-terminal to the catalytic L,D-transpeptidase domain.


Pssm-ID: 240445  Cd Length: 98  Bit Score: 37.31  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2670045098  56 KLTITPKPNAEVDPLARILVTAETGTID------SVTLVNDGGKQIPGVLTPDAK--TWKPTTSLGFGRTYTMTVSA--- 124
Cdd:cd13430     1 MPYVMPGDGEVVGVGAPVAIRFDENIADrgaaekAITITTDPPVEGAFYWLPDGRrvRWRPEHFWKPGTAVDVAANTygl 80

                          90
                  ....*....|....*....
gi 2670045098 125 ---KGPGGMPTRQvTTFST 140
Cdd:cd13430    81 dlgEGMFGADNVQ-LHFQI 98
 
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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