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Conserved domains on  [gi|488404528|ref|WP_002473913|]
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MULTISPECIES: Mur ligase family protein [Staphylococcus]

Protein Classification

Mur ligase family protein( domain architecture ID 11433679)

Mur ligase family protein such as MurC, MurD, and MurE, which catalyze consecutive steps in the synthesis of peptidoglycan

CATH:  3.90.190.20|3.40.1190.10|3.40.1390.10
EC:  6.3.2.13
Gene Ontology:  GO:0005524|GO:0000287|GO:0009252|GO:0008765
PubMed:  11124264|28201974
SCOP:  4000234

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MurT_C pfam08353
MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from ...
 313-421 2.43e-36

MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189, MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain of MurT.


:

Pssm-ID: 462442  Cd Length: 110  Bit Score: 129.15  E-value: 2.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  313 LAKNPAGMNASLSVGEQIDDKKVYVISLNDNAADGRDISWIYDADFEKLATQDIEAIIVSGTRAEELQLRLKLAEVEV-P 391
Cdd:pfam08353   1 LVKNPVGFNQVLNYIASDPGPKSLLLLLNDNYADGRDVSWIWDVDFEKLNDSNIKKIIVSGDRAYDMALRLKYAGVPEeK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 488404528  392 VKVEKDIYKATAlTMKYSSFTVAI-PNYTSL 421
Cdd:pfam08353  81 IEIEEDLEEALD-AIKAPTENVYIlPTYTAM 110
murD super family cl36818
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
 36-390 9.24e-15

UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


The actual alignment was detected with superfamily member TIGR01087:

Pssm-ID: 273436 [Multi-domain]  Cd Length: 433  Bit Score: 75.84  E-value: 9.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528   36 DHNILRKLAKQ----VDDI-----------VFISGTNGKTTTSNLIGHTLKKNQINIIhnnEGANMAagiTSAFIMQSSK 100
Cdd:TIGR01087  75 DHPLVQAAAKRgipvVGDIelflrlvplpvVAITGTNGKTTTTSLLYHLLKAAGLKAF---LGGNIG---TPALEVLDQE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  101 NTNIAIIEIDEGSIPRvLNEVTPSMMVFTNFFRDQMDRFGEIDIMVDNIAK--SINNKGIKLLLNADDPFVSRLKIASHS 178
Cdd:TIGR01087 149 GAELYVLELSSFQLET-TESLRPEIALILNISEDHLDWHGSFEDYVAAKLKifARQTEGDVAVLNADDPRFARLAQKSKA 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  179 IVYYGmkkfahdFEQSTMNESKYCPNCGRLLQydyihynqighyhcecgfkreeptyevsSFDASPFLKmiinqsefnmk 258
Cdd:TIGR01087 228 QVIWF-------SVEKDAERGLCIRDGGLYLK----------------------------PNDLEGSLL----------- 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  259 iaGDFNSYNAIAAYTVLRELGLNDDAIRKGFETYTSDNGRMQYFsKNKKEAM-INLAK--NPAGMNASLSVGeqidDKKV 335
Cdd:TIGR01087 262 --GLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYV-GQKNGVHfYNDSKatNVHATLAALSAF----DNPV 334

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488404528  336 YVIslndnaADGRDISWIYDADFEKLATQDIEAIIVsGTRAEELQLRLKLAEVEV 390
Cdd:TIGR01087 335 ILI------VGGDDKGADFSPLAPAAAGKVKAVLAI-GEDAAKIAPLLKEAGLSV 382
 
Name Accession Description Interval E-value
MurT_C pfam08353
MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from ...
 313-421 2.43e-36

MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189, MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain of MurT.


Pssm-ID: 462442  Cd Length: 110  Bit Score: 129.15  E-value: 2.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  313 LAKNPAGMNASLSVGEQIDDKKVYVISLNDNAADGRDISWIYDADFEKLATQDIEAIIVSGTRAEELQLRLKLAEVEV-P 391
Cdd:pfam08353   1 LVKNPVGFNQVLNYIASDPGPKSLLLLLNDNYADGRDVSWIWDVDFEKLNDSNIKKIIVSGDRAYDMALRLKYAGVPEeK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 488404528  392 VKVEKDIYKATAlTMKYSSFTVAI-PNYTSL 421
Cdd:pfam08353  81 IEIEEDLEEALD-AIKAPTENVYIlPTYTAM 110
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
 36-390 9.24e-15

UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273436 [Multi-domain]  Cd Length: 433  Bit Score: 75.84  E-value: 9.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528   36 DHNILRKLAKQ----VDDI-----------VFISGTNGKTTTSNLIGHTLKKNQINIIhnnEGANMAagiTSAFIMQSSK 100
Cdd:TIGR01087  75 DHPLVQAAAKRgipvVGDIelflrlvplpvVAITGTNGKTTTTSLLYHLLKAAGLKAF---LGGNIG---TPALEVLDQE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  101 NTNIAIIEIDEGSIPRvLNEVTPSMMVFTNFFRDQMDRFGEIDIMVDNIAK--SINNKGIKLLLNADDPFVSRLKIASHS 178
Cdd:TIGR01087 149 GAELYVLELSSFQLET-TESLRPEIALILNISEDHLDWHGSFEDYVAAKLKifARQTEGDVAVLNADDPRFARLAQKSKA 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  179 IVYYGmkkfahdFEQSTMNESKYCPNCGRLLQydyihynqighyhcecgfkreeptyevsSFDASPFLKmiinqsefnmk 258
Cdd:TIGR01087 228 QVIWF-------SVEKDAERGLCIRDGGLYLK----------------------------PNDLEGSLL----------- 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  259 iaGDFNSYNAIAAYTVLRELGLNDDAIRKGFETYTSDNGRMQYFsKNKKEAM-INLAK--NPAGMNASLSVGeqidDKKV 335
Cdd:TIGR01087 262 --GLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYV-GQKNGVHfYNDSKatNVHATLAALSAF----DNPV 334

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488404528  336 YVIslndnaADGRDISWIYDADFEKLATQDIEAIIVsGTRAEELQLRLKLAEVEV 390
Cdd:TIGR01087 335 ILI------VGGDDKGADFSPLAPAAAGKVKAVLAI-GEDAAKIAPLLKEAGLSV 382
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 40-380 3.22e-14

UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440533 [Multi-domain]  Cd Length: 451  Bit Score: 73.98  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  40 LRKLAK----QVDDIVF-ISGTNGKTTTSNLIGHTLK------KNQINiiHNNE-G-----ANMaagitsafimqsSKNT 102
Cdd:COG0770   87 LQQLAAahraRFNIPVIaITGSNGKTTTKEMLAAVLStkgkvlATPGN--FNNEiGvpltlLRL------------PEDH 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 103 NIAIIE--------IDE-GSIprvlneVTPSMMVFTNFFRDQMDRFGEIDimvdNIAK-------SINNKGIkLLLNADD 166
Cdd:COG0770  153 EFAVLEmgmnhpgeIAYlARI------ARPDIAVITNIGPAHLEGFGSLE----GIARakgeifeGLPPGGV-AVLNADD 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 167 PFVSRL-KIASHSIVYYGMKKFAHdfeqstmneskycpncgrlLQYDYIHYNQIGhyhcecgfkreeptyevSSFDASPF 245
Cdd:COG0770  222 PLLAALaERAKARVLTFGLSEDAD-------------------VRAEDIELDEDG-----------------TRFTLHTP 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 246 LKMIinqsEFNMKIAGDFNSYNAIAAYTVLRELGLNDDAIRKGFETYTSDNGRMQyfsknkkeaMINLAK---------- 315
Cdd:COG0770  266 GGEL----EVTLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQPVKGRLE---------VIEGAGgvtliddsyn 332

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488404528 316 -NPAGMNASLSVGEQI--DDKKVYVIS----LNDNAADG-RDISwiydadfEKLATQDIEAIIVSGTRAEELQ 380
Cdd:COG0770  333 aNPDSMKAALDVLAQLpgGGRRIAVLGdmleLGEESEELhREVG-------ELAAELGIDRLFTVGELARAIA 398
Mur_ligase_M pfam08245
Mur ligase middle domain;
53-271 8.62e-14

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 69.64  E-value: 8.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528   53 ISGTNGKTTTSNLIGHTLKK---------NQINIIHNNEgaNMAAGITSAFIMQSSKNTNIAIIEIDEGSIP--RVLNEV 121
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLaggvigtigTYIGKSGNTT--NNAIGLPLTLAEMVEAGAEYAVLEVSSHGLGegRLSGLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  122 TPSMMVFTNFFRDQMDRFGEIdimvDNIAKS-------INNKGIkLLLNADDP----FVSRLKIASHSIVYYGMKKFAhd 190
Cdd:pfam08245  79 KPDIAVFTNISPDHLDFHGTM----ENYAKAkaelfegLPEDGI-AVINADDPygafLIAKLKKAGVRVITYGIEGEA-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  191 feqstmneskycpncgrllqydYIHYNQIghyhcecgfkreeptYEVSSFDASPFLKMIINQSEFNMKIAGDFNSYNAIA 270
Cdd:pfam08245 152 ----------------------DLRAANI---------------ELSSDGTSFDLFTVPGGELEIEIPLLGRHNVYNALA 194


                  .
gi 488404528  271 A 271
Cdd:pfam08245 195 A 195
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 50-345 1.07e-07

bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;


Pssm-ID: 237025 [Multi-domain]  Cd Length: 958  Bit Score: 54.32  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  50 IVFISGTNGKTTTSNLIGHTLKKNQ-INIIHNNEGA-NMAAGITSAfIMQSSKNTNIAIIEI---DEGSIPRVLNEVTPS 124
Cdd:PRK11929 605 VVAITGSNGKTTTKEMIAAILAAWQgEDRVLATEGNfNNEIGVPLT-LLRLRAQHRAAVFELgmnHPGEIAYLAAIAAPT 683

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 125 MMVFTNFFRDQMDRFGEIDIMVDNIAKSINN---KGIkLLLNADDPFVSrlkiashsivyygmkkfahdfEQSTMNESKy 201
Cdd:PRK11929 684 VALVTNAQREHQEFMHSVEAVARAKGEIIAAlpeDGV-AVVNGDDPYTA---------------------IWAKLAGAR- 740

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 202 cpncgRLLQYDyihYNQIGHYHCECgFKREEPTYEVSSFDAspFLKMIINQSEFNMKIAGDFNSYNAIAAYTVLRELGLN 281
Cdd:PRK11929 741 -----RVLRFG---LQPGADVYAEK-IAKDISVGEAGGTRC--QVVTPAGSAEVYLPLIGEHNLRNALAAIACALAAGAS 809

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488404528 282 DDAIRKGFETYTSDNGRMQYFSKNKKEAMIN--LAKNPAGMNASLSVGEQIDD-KKVYVIS----LNDNAA 345
Cdd:PRK11929 810 LKQIRAGLERFQPVAGRMQRRRLSCGTRIIDdtYNANPDSMRAAIDVLAELPNgPRALVLGdmleLGDNGP 880
 
Name Accession Description Interval E-value
MurT_C pfam08353
MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from ...
 313-421 2.43e-36

MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189, MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain of MurT.


Pssm-ID: 462442  Cd Length: 110  Bit Score: 129.15  E-value: 2.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  313 LAKNPAGMNASLSVGEQIDDKKVYVISLNDNAADGRDISWIYDADFEKLATQDIEAIIVSGTRAEELQLRLKLAEVEV-P 391
Cdd:pfam08353   1 LVKNPVGFNQVLNYIASDPGPKSLLLLLNDNYADGRDVSWIWDVDFEKLNDSNIKKIIVSGDRAYDMALRLKYAGVPEeK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 488404528  392 VKVEKDIYKATAlTMKYSSFTVAI-PNYTSL 421
Cdd:pfam08353  81 IEIEEDLEEALD-AIKAPTENVYIlPTYTAM 110
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
 36-390 9.24e-15

UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273436 [Multi-domain]  Cd Length: 433  Bit Score: 75.84  E-value: 9.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528   36 DHNILRKLAKQ----VDDI-----------VFISGTNGKTTTSNLIGHTLKKNQINIIhnnEGANMAagiTSAFIMQSSK 100
Cdd:TIGR01087  75 DHPLVQAAAKRgipvVGDIelflrlvplpvVAITGTNGKTTTTSLLYHLLKAAGLKAF---LGGNIG---TPALEVLDQE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  101 NTNIAIIEIDEGSIPRvLNEVTPSMMVFTNFFRDQMDRFGEIDIMVDNIAK--SINNKGIKLLLNADDPFVSRLKIASHS 178
Cdd:TIGR01087 149 GAELYVLELSSFQLET-TESLRPEIALILNISEDHLDWHGSFEDYVAAKLKifARQTEGDVAVLNADDPRFARLAQKSKA 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  179 IVYYGmkkfahdFEQSTMNESKYCPNCGRLLQydyihynqighyhcecgfkreeptyevsSFDASPFLKmiinqsefnmk 258
Cdd:TIGR01087 228 QVIWF-------SVEKDAERGLCIRDGGLYLK----------------------------PNDLEGSLL----------- 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  259 iaGDFNSYNAIAAYTVLRELGLNDDAIRKGFETYTSDNGRMQYFsKNKKEAM-INLAK--NPAGMNASLSVGeqidDKKV 335
Cdd:TIGR01087 262 --GLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYV-GQKNGVHfYNDSKatNVHATLAALSAF----DNPV 334

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488404528  336 YVIslndnaADGRDISWIYDADFEKLATQDIEAIIVsGTRAEELQLRLKLAEVEV 390
Cdd:TIGR01087 335 ILI------VGGDDKGADFSPLAPAAAGKVKAVLAI-GEDAAKIAPLLKEAGLSV 382
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 40-380 3.22e-14

UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440533 [Multi-domain]  Cd Length: 451  Bit Score: 73.98  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  40 LRKLAK----QVDDIVF-ISGTNGKTTTSNLIGHTLK------KNQINiiHNNE-G-----ANMaagitsafimqsSKNT 102
Cdd:COG0770   87 LQQLAAahraRFNIPVIaITGSNGKTTTKEMLAAVLStkgkvlATPGN--FNNEiGvpltlLRL------------PEDH 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 103 NIAIIE--------IDE-GSIprvlneVTPSMMVFTNFFRDQMDRFGEIDimvdNIAK-------SINNKGIkLLLNADD 166
Cdd:COG0770  153 EFAVLEmgmnhpgeIAYlARI------ARPDIAVITNIGPAHLEGFGSLE----GIARakgeifeGLPPGGV-AVLNADD 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 167 PFVSRL-KIASHSIVYYGMKKFAHdfeqstmneskycpncgrlLQYDYIHYNQIGhyhcecgfkreeptyevSSFDASPF 245
Cdd:COG0770  222 PLLAALaERAKARVLTFGLSEDAD-------------------VRAEDIELDEDG-----------------TRFTLHTP 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 246 LKMIinqsEFNMKIAGDFNSYNAIAAYTVLRELGLNDDAIRKGFETYTSDNGRMQyfsknkkeaMINLAK---------- 315
Cdd:COG0770  266 GGEL----EVTLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQPVKGRLE---------VIEGAGgvtliddsyn 332

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488404528 316 -NPAGMNASLSVGEQI--DDKKVYVIS----LNDNAADG-RDISwiydadfEKLATQDIEAIIVSGTRAEELQ 380
Cdd:COG0770  333 aNPDSMKAALDVLAQLpgGGRRIAVLGdmleLGEESEELhREVG-------ELAAELGIDRLFTVGELARAIA 398
Mur_ligase_M pfam08245
Mur ligase middle domain;
53-271 8.62e-14

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 69.64  E-value: 8.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528   53 ISGTNGKTTTSNLIGHTLKK---------NQINIIHNNEgaNMAAGITSAFIMQSSKNTNIAIIEIDEGSIP--RVLNEV 121
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLaggvigtigTYIGKSGNTT--NNAIGLPLTLAEMVEAGAEYAVLEVSSHGLGegRLSGLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  122 TPSMMVFTNFFRDQMDRFGEIdimvDNIAKS-------INNKGIkLLLNADDP----FVSRLKIASHSIVYYGMKKFAhd 190
Cdd:pfam08245  79 KPDIAVFTNISPDHLDFHGTM----ENYAKAkaelfegLPEDGI-AVINADDPygafLIAKLKKAGVRVITYGIEGEA-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  191 feqstmneskycpncgrllqydYIHYNQIghyhcecgfkreeptYEVSSFDASPFLKMIINQSEFNMKIAGDFNSYNAIA 270
Cdd:pfam08245 152 ----------------------DLRAANI---------------ELSSDGTSFDLFTVPGGELEIEIPLLGRHNVYNALA 194


                  .
gi 488404528  271 A 271
Cdd:pfam08245 195 A 195
MurC COG0773
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ...
 53-301 1.41e-13

UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440536 [Multi-domain]  Cd Length: 451  Bit Score: 72.02  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  53 ISGTNGKTTTSNLIGHTLKKNQINI------IHNNEGANMAAGitsafimqsskNTNIAIIEIDE--GSIprvLNeVTPS 124
Cdd:COG0773  109 VAGTHGKTTTTSMLAHILEEAGLDPtfliggILNNFGTNARLG-----------DGDYFVAEADEsdGSF---LH-YSPD 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 125 MMVFTNFFRDQMDRFGEIDIMVDNIAKSINN--KGIKLLLNADDPFVSRL-KIASHSIVYYGMKKFAhdfeqstmnesky 201
Cdd:COG0773  174 IAVVTNIEADHLDIYGDLEAIKEAFHEFARNvpFYGLLVLCADDPGLRELlPRCGRPVITYGFSEDA------------- 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 202 cpncgrllqyDYihynQIGHYHCECGFkreeptyevSSFDaspFLKMIINQSEFNMKIAGDFNSYNAIAAYTVLRELGLN 281
Cdd:COG0773  241 ----------DY----RAENIRIDGGG---------STFD---VLRRGEELGEVELNLPGRHNVLNALAAIAVALELGVD 294

                        250       260
                 ....*....|....*....|
gi 488404528 282 DDAIRKGFETYTSDNGRMQY 301
Cdd:COG0773  295 PEAIAEALASFKGVKRRFEL 314
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 50-301 3.13e-10

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 61.64  E-value: 3.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  50 IVFISGTNGKTTTSNLIGHTLKKNQINIIhnneganmAAGitsafimqsskntNI--AIIE-IDEGSIPRVL-------- 118
Cdd:COG0771  107 IIAITGTNGKTTTTTLIGHILKAAGLRVA--------VGG-------------NIgtPLLDlLLEPEPPDVYvlelssfq 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 119 ----NEVTPSMMVFTNFFRDQMDRFGEIDIMVDniAKS--INN--KGIKLLLNADDPFVSRL-KIASHSIVYYGMKK--- 186
Cdd:COG0771  166 lettPSLRPDVAVILNITPDHLDRHGSMEAYAA--AKAriFANqtPDDYAVLNADDPLTRALaEEAKARVVPFSLKEple 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 187 ---FAHDfeqstmneskycpncgrllqyDYIHYNQIGHyhcecgfkreeptyevssfdaspflkMIINQSEfnMKIAGDF 263
Cdd:COG0771  244 ggaGLED---------------------GKLVDRASGE--------------------------ELLPVDD--LRLPGRH 274

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 488404528 264 NSYNAIAAYTVLRELGLNDDAIRKGFETYTSDNGRMQY 301
Cdd:COG0771  275 NLENALAALAAARALGVPPEAIREALRSFKGLPHRLEF 312
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 53-303 2.83e-09

UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440532 [Multi-domain]  Cd Length: 459  Bit Score: 58.94  E-value: 2.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  53 ISGTNGKTTTSNLIGHTLKKNQINI-----IHNNEG--------------------ANMA-AGITSAFIMQSSkntnIAI 106
Cdd:COG0769   85 VTGTNGKTTTTYLLAQILRALGKKTgligtVGNGIGgelipsslttpealdlqrllAEMVdAGVTHVVMEVSS----HAL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 107 ieiDEGsipRVlNEVTPSMMVFTNFFRD------QMDRFGEidimvdniAKSI----NNKGIKLLLNADDPFVSRL-KIA 175
Cdd:COG0769  161 ---DQG---RV-DGVRFDVAVFTNLTRDhldyhgTMEAYFA--------AKARlfdqLGPGGAAVINADDPYGRRLaAAA 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 176 SHSIVYYGMKKFAHdfeqstmneskycpncgrlLQYDYIHYNQIGHyhcecgfkreepTYEVSSFDaspflkmiiNQSEF 255
Cdd:COG0769  226 PARVITYGLKADAD-------------------LRATDIELSADGT------------RFTLVTPG---------GEVEV 265

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 488404528 256 NMKIAGDFNSYNAIAAYTVLRELGLNDDAIRKGFETYTSDNGRMQYFS 303
Cdd:COG0769  266 RLPLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRMERVD 313
murF TIGR01143
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ...
 34-380 4.91e-08

UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the strictly bacterial MurF gene of peptidoglycan biosynthesis. This enzyme is almost always UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanyl ligase, but in a few species, MurE adds lysine rather than diaminopimelate. This enzyme acts on the product from MurE activity, and so is also subfamily rather than equivalog. Staphylococcus aureus is an example of species in this MurF protein would differ. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273468 [Multi-domain]  Cd Length: 417  Bit Score: 54.96  E-value: 4.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528   34 RVDHNI--LRKLAKQVDD-----IVFISGTNGKTTTSNLIGHTLKKNQINIIHNnegANMAAGITSA-FIMQSSKNTNIA 105
Cdd:TIGR01143  53 LVDDTLeaLQALARAKRAkfsgkVIGITGSSGKTTTKEMLAAILSHKYKVFATP---GNFNNEIGLPlTLLRAPGDHDYA 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  106 IIE--IDE-GSIPRVLNEVTPSMMVFTNFFRDQMDRFGEIDIMVDniAKSINNKGIK----LLLNADDPFVSRLK--IAS 176
Cdd:TIGR01143 130 VLEmgASHpGEIAYLAEIAKPDIAVITNIGPAHLEGFGSLEGIAE--AKGEILQGLKengiAVINADDPAFADLAkrLPN 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  177 HSIVYYGMKKfaHDFEqstmneskycpncGRLLQYDYIHynqighyhcecgfkreeptyevssfdaSPFLKMIINQSEFN 256
Cdd:TIGR01143 208 RNILSFGFEG--GDFV-------------AKDISYSALG---------------------------STSFTLVAPGGEFE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  257 MK--IAGDFNSYNAIAAYTVLRELGLNDDAIRKGFETYTSDNGRMQYFSKNKKeAMINLAKN--PAGMNASLSVGEQIDD 332
Cdd:TIGR01143 246 VSlpLLGRHNVMNALAAAALALELGIPLEEIAEGLAELKLVKGRFEVQTKNGL-TLIDDTYNanPDSMRAALDALARFPG 324

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 488404528  333 KKVYVisLNDNAADGRDISWIYDADFEKLATQDIEAIIVSGTRAEELQ 380
Cdd:TIGR01143 325 KKILV--LGDMAELGEYSEELHAEVGRYANSLGIDLVFLVGEEAAVIY 370
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 50-345 1.07e-07

bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;


Pssm-ID: 237025 [Multi-domain]  Cd Length: 958  Bit Score: 54.32  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  50 IVFISGTNGKTTTSNLIGHTLKKNQ-INIIHNNEGA-NMAAGITSAfIMQSSKNTNIAIIEI---DEGSIPRVLNEVTPS 124
Cdd:PRK11929 605 VVAITGSNGKTTTKEMIAAILAAWQgEDRVLATEGNfNNEIGVPLT-LLRLRAQHRAAVFELgmnHPGEIAYLAAIAAPT 683

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 125 MMVFTNFFRDQMDRFGEIDIMVDNIAKSINN---KGIkLLLNADDPFVSrlkiashsivyygmkkfahdfEQSTMNESKy 201
Cdd:PRK11929 684 VALVTNAQREHQEFMHSVEAVARAKGEIIAAlpeDGV-AVVNGDDPYTA---------------------IWAKLAGAR- 740

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 202 cpncgRLLQYDyihYNQIGHYHCECgFKREEPTYEVSSFDAspFLKMIINQSEFNMKIAGDFNSYNAIAAYTVLRELGLN 281
Cdd:PRK11929 741 -----RVLRFG---LQPGADVYAEK-IAKDISVGEAGGTRC--QVVTPAGSAEVYLPLIGEHNLRNALAAIACALAAGAS 809

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488404528 282 DDAIRKGFETYTSDNGRMQYFSKNKKEAMIN--LAKNPAGMNASLSVGEQIDD-KKVYVIS----LNDNAA 345
Cdd:PRK11929 810 LKQIRAGLERFQPVAGRMQRRRLSCGTRIIDdtYNANPDSMRAAIDVLAELPNgPRALVLGdmleLGDNGP 880
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 50-302 1.19e-07

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 54.01  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  50 IVFISGTNGKTTTSNLIGHTLKKNQINI---------IHNN---EGANmaAGITSAFIMQSSKNTNIAIIEIDEGSIprv 117
Cdd:PRK14016 482 IVAVTGTNGKTTTTRLIAHILKLSGKRVgmtttdgvyIDGRlidKGDC--TGPKSARRVLMNPDVEAAVLETARGGI--- 556

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 118 LNE--------VTpsmmVFTNFfrdQMDRFGEIDIM------------VDNIAKSinnkGIKlLLNADDPFVsrLKIASH 177
Cdd:PRK14016 557 LREglaydrcdVG----VVTNI---GEDHLGLGGINtledlakvkrvvVEAVKPD----GYA-VLNADDPMV--AAMAER 622

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 178 ---SIVYygmkkFAHDFEQSTMNEskYCPNCGRLLqydYIHYNQIghYHCECGFKreeptYEVSSFDASPFlkmiinqsE 254
Cdd:PRK14016 623 ckgKVIF-----FSMDPDNPVIAE--HRAQGGRAV---YVEGDYI--VLAEGGWE-----IRIISLADIPL--------T 677

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488404528 255 FNMKIAgdFNSYNAIAAYTVLRELGLNDDAIRKGFETYTSD----NGRMQYF 302
Cdd:PRK14016 678 LGGKAG--FNIENALAAIAAAWALGIDIELIRAGLRTFVSDaaqaPGRFNLF 727
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 50-325 2.40e-06

UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 49.75  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  50 IVFISGTNGKTTTSNLIGHTLKKNQI---------NII--HNNEG--------------ANMA-AGITsAFIMQ-SSknt 102
Cdd:PRK00139  97 LIGVTGTNGKTTTAYLLAQILRLLGEktaligtlgNGIggELIPSglttpdaldlqrllAELVdAGVT-YAAMEvSS--- 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 103 nIAIieiDEGsipRVlNEVTPSMMVFTNFFRDQMDRFGEidiMVDNI-AKS--INNKGIKLLLNADDPFVSRLkiASHSI 179
Cdd:PRK00139 173 -HAL---DQG---RV-DGLKFDVAVFTNLSRDHLDYHGT---MEDYLaAKArlFSELGLAAVINADDEVGRRL--LALPD 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 180 VYygmkkfahdfeqstmneskycpncgrllqydyihynqighyhcecGFKREEPTYEVSSFDASPFLKMIINQSEFNMKI 259
Cdd:PRK00139 240 AY---------------------------------------------AVSMAGADLRATDVEYTDSGQTFTLVTEVESPL 274

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488404528 260 AGDFNSYNAIAAYTVLRELGLNDDAIRKGFETYTSDNGRMQYF-SKNKKEAMINLAKNPAGMNASLS 325
Cdd:PRK00139 275 IGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVPGRMERVdAGQGPLVIVDYAHTPDALEKVLE 341
murD PRK14106
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
 50-293 7.21e-06

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional


Pssm-ID: 184511 [Multi-domain]  Cd Length: 450  Bit Score: 48.04  E-value: 7.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528  50 IVFISGTNGKTTTSNLIGHTLKKNQINIIhnneganMAAGITSAFIMQSSKNTNIAIIEIDEGSIP-RVLNEVTPSMMVF 128
Cdd:PRK14106 110 IVAITGTNGKTTTTTLLGEIFKNAGRKTL-------VAGNIGYPLIDAVEEYGEDDIIVAEVSSFQlETIKEFKPKVGCI 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 129 TNFFRDQMDRFGEIDIMVD---NIAKSINNKGIKlLLNADDPFVSRLKIASHSIVYYGMKKfaHDFEQstmneskycpnc 205
Cdd:PRK14106 183 LNITPDHLDRHKTMENYIKakaRIFENQRPSDYT-VLNYDDPRTRSLAKKAKARVIFFSRK--SLLEE------------ 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 206 GRLLQYDYIHYNQIGHyhcecgfkreepTYEVSSFDaspflkmiinqsefNMKIAGDFNSYNAIAAYTVLRELGLNDDAI 285
Cdd:PRK14106 248 GVFVKNGKIVISLGGK------------EEEVIDID--------------EIFIPGEHNLENALAATAAAYLLGISPDVI 301


                 ....*...
gi 488404528 286 RKGFETYT 293
Cdd:PRK14106 302 ANTLKTFK 309
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
239-364 2.02e-04

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 43.49  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488404528 239 SFDASPFLkmiinQSEFNMKIAGDFNSYNAIAAYTVLRELGLNDDAIRKGFETyTSDNGRMQYFS-KNKKEAMINLAKNP 317
Cdd:PRK14022 277 SFEATGKL-----AGTYDIQLIGKFNQENAMAAGLACLRLGASLEDIQKGIAQ-TPVPGRMEVLTqSNGAKVFIDYAHNG 350

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488404528 318 AGMNASLSVGEQIDDKKVYVISlndNAADGRDISwiYDADFEKLATQ 364
Cdd:PRK14022 351 DSLNKLIDVVEEHQKGKLILLL---GAAGNKGES--RRPDFGRVANR 392
 
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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