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Conserved domains on  [gi|380763148|gb|AFE51667|]
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lipid-A-disaccharide synthase [Rickettsia prowazekii str. Dachau]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LpxB pfam02684
Lipid-A-disaccharide synthetase; This is a family of lipid-A-disaccharide synthetases, EC:2.4. ...
4-374 1.99e-172

Lipid-A-disaccharide synthetase; This is a family of lipid-A-disaccharide synthetases, EC:2.4.2.128. These enzymes catalyze the reaction: UDP-2,3-bis(3-hydroxytetradecanoyl) glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate <=> UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6 -beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. These enzymes catalyze the fist disaccharide step in the synthesis of lipid-A-disaccharide.


:

Pssm-ID: 397004  Cd Length: 374  Bit Score: 485.41  E-value: 1.99e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148    4 IYFIAGEMSGDFIGGHVIQNLKSN-EGLEFTGIGGKYMEeAGNFKSLFTITAINLIGFIEIIPHLLKIKKLIDKTVEHII 82
Cdd:pfam02684   1 IFLSAGEVSGDILGGELIKELKEHyPNLEFVGVGGPKME-AEGFESLAAMEEISVMGFIEVLPRLPKLLKIYQKLVRNIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148   83 NSKADLLITIDSPGFTYRVAKRVRKLLPNLKMIHIVAPSVWAYKADRAVNYAKIYDCLFALLPFEPPYFTKVGLDCRYIG 162
Cdd:pfam02684  80 KKKPDTLILIDAPDFNLRLAKKLRKLGPKLKIIHYVSPSVWAWKPKRATKIAKYTDLLLAILPFEKAFYQKFGLDCRYVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  163 HPIMEQEFYRDKIALRKELK-IDENERILCVTLGTRKGEILRHLPIFIDAIQEISKDYKNLTIIFPLAHPDHEA--IIKP 239
Cdd:pfam02684 160 HPLLDAIKLFKPRANAKELLgIDHNEPFLALLPGSRKSEIRRLLPPFLVAAQQLSSQFPNLKLLVPLVNKFYEHqiEEIK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  240 FLDNIQFNYLFLSNERLKAYAVSDLALAKSGTNTLEISASGTPMVVAYKVNIISFIIIMLLIKIKYVSLINIIAGSEIIP 319
Cdd:pfam02684 240 ALNNPDVQLLEISGERYKAMFAADAALIKSGTATLEAALSGTPMVVAYRVKPLTFFLAKRLVKIDYISLPNILLNREIVP 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 380763148  320 EFIQFNCKANLISNKLKELLSNSQKRYNQVVKSKKILQKLGFESNRSPSYIAAKI 374
Cdd:pfam02684 320 EFIQEECDAQLEAVALLLLLLNGSKAKKEKDSCRKFYQLLRFIACNADEQAALIV 374
 
Name Accession Description Interval E-value
LpxB pfam02684
Lipid-A-disaccharide synthetase; This is a family of lipid-A-disaccharide synthetases, EC:2.4. ...
4-374 1.99e-172

Lipid-A-disaccharide synthetase; This is a family of lipid-A-disaccharide synthetases, EC:2.4.2.128. These enzymes catalyze the reaction: UDP-2,3-bis(3-hydroxytetradecanoyl) glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate <=> UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6 -beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. These enzymes catalyze the fist disaccharide step in the synthesis of lipid-A-disaccharide.


Pssm-ID: 397004  Cd Length: 374  Bit Score: 485.41  E-value: 1.99e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148    4 IYFIAGEMSGDFIGGHVIQNLKSN-EGLEFTGIGGKYMEeAGNFKSLFTITAINLIGFIEIIPHLLKIKKLIDKTVEHII 82
Cdd:pfam02684   1 IFLSAGEVSGDILGGELIKELKEHyPNLEFVGVGGPKME-AEGFESLAAMEEISVMGFIEVLPRLPKLLKIYQKLVRNIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148   83 NSKADLLITIDSPGFTYRVAKRVRKLLPNLKMIHIVAPSVWAYKADRAVNYAKIYDCLFALLPFEPPYFTKVGLDCRYIG 162
Cdd:pfam02684  80 KKKPDTLILIDAPDFNLRLAKKLRKLGPKLKIIHYVSPSVWAWKPKRATKIAKYTDLLLAILPFEKAFYQKFGLDCRYVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  163 HPIMEQEFYRDKIALRKELK-IDENERILCVTLGTRKGEILRHLPIFIDAIQEISKDYKNLTIIFPLAHPDHEA--IIKP 239
Cdd:pfam02684 160 HPLLDAIKLFKPRANAKELLgIDHNEPFLALLPGSRKSEIRRLLPPFLVAAQQLSSQFPNLKLLVPLVNKFYEHqiEEIK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  240 FLDNIQFNYLFLSNERLKAYAVSDLALAKSGTNTLEISASGTPMVVAYKVNIISFIIIMLLIKIKYVSLINIIAGSEIIP 319
Cdd:pfam02684 240 ALNNPDVQLLEISGERYKAMFAADAALIKSGTATLEAALSGTPMVVAYRVKPLTFFLAKRLVKIDYISLPNILLNREIVP 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 380763148  320 EFIQFNCKANLISNKLKELLSNSQKRYNQVVKSKKILQKLGFESNRSPSYIAAKI 374
Cdd:pfam02684 320 EFIQEECDAQLEAVALLLLLLNGSKAKKEKDSCRKFYQLLRFIACNADEQAALIV 374
LpxB COG0763
Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide ...
3-375 3.35e-133

Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440526  Cd Length: 378  Bit Score: 385.96  E-value: 3.35e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148   3 KIYFIAGEMSGDFIGGHVIQNLKS-NEGLEFTGIGGKYMEEAGnFKSLFTITAINLIGFIEIIPHLLKIKKLIDKTVEHI 81
Cdd:COG0763    2 KIFIVAGEASGDLLGANLIRALKArDPDAEFVGIGGPRMQAAG-LESLFDMEELSVMGFVEVLKHLPRLLRLRRQLKRAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  82 INSKADLLITIDSPGFTYRVAKRVRKLlpNLKMIHIVAPSVWAYKADRAVNYAKIYDCLFALLPFEPPYFTKVGLDCRYI 161
Cdd:COG0763   81 LAEKPDVVILIDYPGFNLRLAKRLKKA--GIPVVYYVSPQVWAWRPGRVKKIARAVDHVLAIFPFEPEFYRKHGVPVTFV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 162 GHPIMEQ-EFYRDKIALRKELKIDENERILCVTLGTRKGEILRHLPIFIDAIQEISKDYKNLTIIFPLAHPDHEAIIKPF 240
Cdd:COG0763  159 GHPLADEiPLEPDRAAARARLGLDPDKPVIALLPGSRRSEIKRLLPVFLEAAKLLAARRPDLQFVVPLAPSLRRELIEAA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 241 LDNIQFNYLFLSNERLKAYAVSDLALAKSGTNTLEISASGTPMVVAYKVNIISFIIIMLLIKIKYVSLINIIAGSEIIPE 320
Cdd:COG0763  239 LADWPLPVTLVDGQTYDAMAAADAALVASGTATLEAALLGVPMVVAYKVSPLTYWIAKRLVKVPYISLPNLLAGREVVPE 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 380763148 321 FIQFNCKANLISNKLKELLSNSQKRYNQVVKSKKILQKLGfesNRSPSYIAAKII 375
Cdd:COG0763  319 LLQDDATPENLAAALLRLLDDPAARAAQLAAFAELRQLLG---EGGASERAAEAI 370
lpxB TIGR00215
lipid-A-disaccharide synthase; Lipid-A precursor biosynthesis producing lipid A disaccharide ...
4-359 1.43e-70

lipid-A-disaccharide synthase; Lipid-A precursor biosynthesis producing lipid A disaccharide in a condensation reaction. transcribed as part of an operon including lpxA [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 129319 [Multi-domain]  Cd Length: 385  Bit Score: 225.93  E-value: 1.43e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148    4 IYFIAGEMSGDFIGGHVIQNLKS-NEGLEFTGIGGKYMEEAGnFKSLFTITAINLIGFIEIIPHLLKIKKLIDKTVEHII 82
Cdd:TIGR00215   8 IALVAGEASGDILGAGLRQQLKEhYPNARFIGVAGPRMAAEG-CEVLYSMEELSVMGLREVLGRLGRLLKIRKEVVQLAK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148   83 NSKADLLITIDSPGFTyrVAKRVRKLLPNLKMIHIVAPSVWAYKADRAVNYAKIYDCLFALLPFEPPYFTKVGLDCRYIG 162
Cdd:TIGR00215  87 QAKPDLLVGIDAPDFN--LTKELKKKDPGIKIIYYISPQVWAWRKWRAKKIEKATDFLLAILPFEKAFYQKKNVPCRFVG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  163 HPIMEQ--EFYRDKIALRKELKIDENERILCVTLGTRKGEILRHLPIFIDAIQEISKDYKNLTIIFPLA----HPDHEAI 236
Cdd:TIGR00215 165 HPLLDAipLYKPDRKSAREKLGIDHNGETLALLPGSRGSEVEKLFPLFLKAAQLLEQQEPDLRRVLPVVnfkrRLQFEQI 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  237 IKPFLDNIQFnYLFLSNERlKAYAVSDLALAKSGTNTLEISASGTPMVVAYKVNIISFIIIMLLIKIKYVSLINIIAGSE 316
Cdd:TIGR00215 245 KAEYGPDLQL-HLIDGDAR-KAMFAADAALLASGTAALEAALIKTPMVVGYRMKPLTFLIARRLVKTDYISLPNILANRL 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 380763148  317 IIPEFIQFNCKANLISNKLKELLSNSQKRYNQVVKSKKILQKL 359
Cdd:TIGR00215 323 LVPELLQEECTPHPLAIALLLLLENGLKAYKEMHRERQFFEEL 365
lpxB PRK01021
lipid-A-disaccharide synthase; Reviewed
5-322 1.28e-35

lipid-A-disaccharide synthase; Reviewed


Pssm-ID: 167141 [Multi-domain]  Cd Length: 608  Bit Score: 137.24  E-value: 1.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148   5 YFI-AGEMSGDFIGGHVIQNLKS-NEGLEFTGIGGKYMEEAGnFKSLFTITAINLIGFIEIIPHLLKIKKLIDKTVEHII 82
Cdd:PRK01021 229 CFIsAGEHSGDTLGGNLLKEIKAlYPDIHCFGVGGPQMRAEG-FHPLFNMEEFQVSGFWEVLLALFKLWYRYRKLYKTIL 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  83 NSKADLLITIDSPGFTYRVAKRVRKLLPNLKMIHIVAPSVWAYKADRAVNYAKIYDCLFALLPFEPPYFTKVGLDCRYIG 162
Cdd:PRK01021 308 KTNPRTVICIDFPDFHFLLIKKLRKRGYKGKIVHYVCPSIWAWRPKRKTILEKYLDLLLLILPFEQNLFKDSPLRTVYLG 387
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 163 HPIMEQ-EFYRDKIALRKELKIDENERILCVTLGTRKGEILRHLPIFIDAIQEiSKDYKNLTIIFPLAHPDHEAIIKPFL 241
Cdd:PRK01021 388 HPLVETiSSFSPNLSWKEQLHLPSDKPIVAAFPGSRRGDILRNLTIQVQAFLA-SSLASTHQLLVSSANPKYDHLILEVL 466
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 242 DN--IQFNYLFLSNERLKAYAVSDLALAKSGTNTLEISASGTPMVVA------------YKVNIIsfiiimllikIKYVS 307
Cdd:PRK01021 467 QQegCLHSHIVPSQFRYELMRECDCALAKCGTIVLETALNQTPTIVTcqlrpfdtflakYIFKII----------LPAYS 536
                        330
                 ....*....|....*
gi 380763148 308 LINIIAGSEIIPEFI 322
Cdd:PRK01021 537 LPNIILGSTIFPEFI 551
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
143-285 2.42e-03

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340818 [Multi-domain]  Cd Length: 350  Bit Score: 39.51  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 143 LLPFEPPYFTKVGLDCRYIGHPImEQEFYRDKiALRKELKIDENERILCVT---LGTRKgeilrhlpiFIDAIQEISKDY 219
Cdd:cd03785  139 AVSFPETKKYFPAAKVVVTGNPV-REEILNLR-KELKRFGLPPDKPTLLVFggsQGARA---------INRAVPKALPKL 207
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 220 KNLTIIFPLAH-PDHEAIIKPFLDNIQFNYLFLSNER--LKAYAVSDLALAKSGTNTL-EISASGTPMVV 285
Cdd:cd03785  208 LERGIQVIHQTgKGDYDEVKKLYEDLGINVKVFPFIDdmAAAYAAADLVISRAGASTIaELTAAGKPAIL 277
 
Name Accession Description Interval E-value
LpxB pfam02684
Lipid-A-disaccharide synthetase; This is a family of lipid-A-disaccharide synthetases, EC:2.4. ...
4-374 1.99e-172

Lipid-A-disaccharide synthetase; This is a family of lipid-A-disaccharide synthetases, EC:2.4.2.128. These enzymes catalyze the reaction: UDP-2,3-bis(3-hydroxytetradecanoyl) glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate <=> UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6 -beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. These enzymes catalyze the fist disaccharide step in the synthesis of lipid-A-disaccharide.


Pssm-ID: 397004  Cd Length: 374  Bit Score: 485.41  E-value: 1.99e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148    4 IYFIAGEMSGDFIGGHVIQNLKSN-EGLEFTGIGGKYMEeAGNFKSLFTITAINLIGFIEIIPHLLKIKKLIDKTVEHII 82
Cdd:pfam02684   1 IFLSAGEVSGDILGGELIKELKEHyPNLEFVGVGGPKME-AEGFESLAAMEEISVMGFIEVLPRLPKLLKIYQKLVRNIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148   83 NSKADLLITIDSPGFTYRVAKRVRKLLPNLKMIHIVAPSVWAYKADRAVNYAKIYDCLFALLPFEPPYFTKVGLDCRYIG 162
Cdd:pfam02684  80 KKKPDTLILIDAPDFNLRLAKKLRKLGPKLKIIHYVSPSVWAWKPKRATKIAKYTDLLLAILPFEKAFYQKFGLDCRYVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  163 HPIMEQEFYRDKIALRKELK-IDENERILCVTLGTRKGEILRHLPIFIDAIQEISKDYKNLTIIFPLAHPDHEA--IIKP 239
Cdd:pfam02684 160 HPLLDAIKLFKPRANAKELLgIDHNEPFLALLPGSRKSEIRRLLPPFLVAAQQLSSQFPNLKLLVPLVNKFYEHqiEEIK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  240 FLDNIQFNYLFLSNERLKAYAVSDLALAKSGTNTLEISASGTPMVVAYKVNIISFIIIMLLIKIKYVSLINIIAGSEIIP 319
Cdd:pfam02684 240 ALNNPDVQLLEISGERYKAMFAADAALIKSGTATLEAALSGTPMVVAYRVKPLTFFLAKRLVKIDYISLPNILLNREIVP 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 380763148  320 EFIQFNCKANLISNKLKELLSNSQKRYNQVVKSKKILQKLGFESNRSPSYIAAKI 374
Cdd:pfam02684 320 EFIQEECDAQLEAVALLLLLLNGSKAKKEKDSCRKFYQLLRFIACNADEQAALIV 374
LpxB COG0763
Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide ...
3-375 3.35e-133

Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440526  Cd Length: 378  Bit Score: 385.96  E-value: 3.35e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148   3 KIYFIAGEMSGDFIGGHVIQNLKS-NEGLEFTGIGGKYMEEAGnFKSLFTITAINLIGFIEIIPHLLKIKKLIDKTVEHI 81
Cdd:COG0763    2 KIFIVAGEASGDLLGANLIRALKArDPDAEFVGIGGPRMQAAG-LESLFDMEELSVMGFVEVLKHLPRLLRLRRQLKRAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  82 INSKADLLITIDSPGFTYRVAKRVRKLlpNLKMIHIVAPSVWAYKADRAVNYAKIYDCLFALLPFEPPYFTKVGLDCRYI 161
Cdd:COG0763   81 LAEKPDVVILIDYPGFNLRLAKRLKKA--GIPVVYYVSPQVWAWRPGRVKKIARAVDHVLAIFPFEPEFYRKHGVPVTFV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 162 GHPIMEQ-EFYRDKIALRKELKIDENERILCVTLGTRKGEILRHLPIFIDAIQEISKDYKNLTIIFPLAHPDHEAIIKPF 240
Cdd:COG0763  159 GHPLADEiPLEPDRAAARARLGLDPDKPVIALLPGSRRSEIKRLLPVFLEAAKLLAARRPDLQFVVPLAPSLRRELIEAA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 241 LDNIQFNYLFLSNERLKAYAVSDLALAKSGTNTLEISASGTPMVVAYKVNIISFIIIMLLIKIKYVSLINIIAGSEIIPE 320
Cdd:COG0763  239 LADWPLPVTLVDGQTYDAMAAADAALVASGTATLEAALLGVPMVVAYKVSPLTYWIAKRLVKVPYISLPNLLAGREVVPE 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 380763148 321 FIQFNCKANLISNKLKELLSNSQKRYNQVVKSKKILQKLGfesNRSPSYIAAKII 375
Cdd:COG0763  319 LLQDDATPENLAAALLRLLDDPAARAAQLAAFAELRQLLG---EGGASERAAEAI 370
lpxB TIGR00215
lipid-A-disaccharide synthase; Lipid-A precursor biosynthesis producing lipid A disaccharide ...
4-359 1.43e-70

lipid-A-disaccharide synthase; Lipid-A precursor biosynthesis producing lipid A disaccharide in a condensation reaction. transcribed as part of an operon including lpxA [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 129319 [Multi-domain]  Cd Length: 385  Bit Score: 225.93  E-value: 1.43e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148    4 IYFIAGEMSGDFIGGHVIQNLKS-NEGLEFTGIGGKYMEEAGnFKSLFTITAINLIGFIEIIPHLLKIKKLIDKTVEHII 82
Cdd:TIGR00215   8 IALVAGEASGDILGAGLRQQLKEhYPNARFIGVAGPRMAAEG-CEVLYSMEELSVMGLREVLGRLGRLLKIRKEVVQLAK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148   83 NSKADLLITIDSPGFTyrVAKRVRKLLPNLKMIHIVAPSVWAYKADRAVNYAKIYDCLFALLPFEPPYFTKVGLDCRYIG 162
Cdd:TIGR00215  87 QAKPDLLVGIDAPDFN--LTKELKKKDPGIKIIYYISPQVWAWRKWRAKKIEKATDFLLAILPFEKAFYQKKNVPCRFVG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  163 HPIMEQ--EFYRDKIALRKELKIDENERILCVTLGTRKGEILRHLPIFIDAIQEISKDYKNLTIIFPLA----HPDHEAI 236
Cdd:TIGR00215 165 HPLLDAipLYKPDRKSAREKLGIDHNGETLALLPGSRGSEVEKLFPLFLKAAQLLEQQEPDLRRVLPVVnfkrRLQFEQI 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  237 IKPFLDNIQFnYLFLSNERlKAYAVSDLALAKSGTNTLEISASGTPMVVAYKVNIISFIIIMLLIKIKYVSLINIIAGSE 316
Cdd:TIGR00215 245 KAEYGPDLQL-HLIDGDAR-KAMFAADAALLASGTAALEAALIKTPMVVGYRMKPLTFLIARRLVKTDYISLPNILANRL 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 380763148  317 IIPEFIQFNCKANLISNKLKELLSNSQKRYNQVVKSKKILQKL 359
Cdd:TIGR00215 323 LVPELLQEECTPHPLAIALLLLLENGLKAYKEMHRERQFFEEL 365
lpxB PRK01021
lipid-A-disaccharide synthase; Reviewed
5-322 1.28e-35

lipid-A-disaccharide synthase; Reviewed


Pssm-ID: 167141 [Multi-domain]  Cd Length: 608  Bit Score: 137.24  E-value: 1.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148   5 YFI-AGEMSGDFIGGHVIQNLKS-NEGLEFTGIGGKYMEEAGnFKSLFTITAINLIGFIEIIPHLLKIKKLIDKTVEHII 82
Cdd:PRK01021 229 CFIsAGEHSGDTLGGNLLKEIKAlYPDIHCFGVGGPQMRAEG-FHPLFNMEEFQVSGFWEVLLALFKLWYRYRKLYKTIL 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  83 NSKADLLITIDSPGFTYRVAKRVRKLLPNLKMIHIVAPSVWAYKADRAVNYAKIYDCLFALLPFEPPYFTKVGLDCRYIG 162
Cdd:PRK01021 308 KTNPRTVICIDFPDFHFLLIKKLRKRGYKGKIVHYVCPSIWAWRPKRKTILEKYLDLLLLILPFEQNLFKDSPLRTVYLG 387
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 163 HPIMEQ-EFYRDKIALRKELKIDENERILCVTLGTRKGEILRHLPIFIDAIQEiSKDYKNLTIIFPLAHPDHEAIIKPFL 241
Cdd:PRK01021 388 HPLVETiSSFSPNLSWKEQLHLPSDKPIVAAFPGSRRGDILRNLTIQVQAFLA-SSLASTHQLLVSSANPKYDHLILEVL 466
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 242 DN--IQFNYLFLSNERLKAYAVSDLALAKSGTNTLEISASGTPMVVA------------YKVNIIsfiiimllikIKYVS 307
Cdd:PRK01021 467 QQegCLHSHIVPSQFRYELMRECDCALAKCGTIVLETALNQTPTIVTcqlrpfdtflakYIFKII----------LPAYS 536
                        330
                 ....*....|....*
gi 380763148 308 LINIIAGSEIIPEFI 322
Cdd:PRK01021 537 LPNIILGSTIFPEFI 551
SpsG COG3980
Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall ...
75-285 1.04e-06

Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443179 [Multi-domain]  Cd Length: 342  Bit Score: 49.92  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148  75 DKTVEHIINSKADLLItIDSPGFTYRVAKRVRKLlpNLKMIHIvapsvwaykaDRAVNYAKIYDCLF-ALLPFEPPYFTK 153
Cdd:COG3980   70 EELLELLKDLQPDWLV-VDHYALDAEYEKALKAL--GKKLVVI----------DDLGDRAHPADLVInQNLGASAEDYRG 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 154 VGLDCRY-IGHP--IMEQEFYRDKIALRKelKIDENERILcVTLG-------TRKgeILRHLpifidaiQEISKDYKnLT 223
Cdd:COG3980  137 VPPGTKLlLGPEyaLLRPEFLALRPASRR--ISEEVRRIL-VTFGgsdpdnlTLK--VLRAL-------LQLDPDLK-IT 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380763148 224 IIFPLAHPdHEAIIKPFLDNIQFNYLFLSN-ERLKA-YAVSDLALAKSGTNTLEISASGTPMVV 285
Cdd:COG3980  204 VVVGPGYP-HLDELRALAAERPLNIELHRNvKDMAElMAQADLAISAAGTTTYELAALGLPTIV 266
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
143-285 2.42e-03

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340818 [Multi-domain]  Cd Length: 350  Bit Score: 39.51  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 143 LLPFEPPYFTKVGLDCRYIGHPImEQEFYRDKiALRKELKIDENERILCVT---LGTRKgeilrhlpiFIDAIQEISKDY 219
Cdd:cd03785  139 AVSFPETKKYFPAAKVVVTGNPV-REEILNLR-KELKRFGLPPDKPTLLVFggsQGARA---------INRAVPKALPKL 207
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 220 KNLTIIFPLAH-PDHEAIIKPFLDNIQFNYLFLSNER--LKAYAVSDLALAKSGTNTL-EISASGTPMVV 285
Cdd:cd03785  208 LERGIQVIHQTgKGDYDEVKKLYEDLGINVKVFPFIDdmAAAYAAADLVISRAGASTIaELTAAGKPAIL 277
MurG COG0707
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ...
158-284 4.39e-03

UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440471 [Multi-domain]  Cd Length: 363  Bit Score: 38.96  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380763148 158 CRYIGHPIMEQEFYRDKIALRKELKIDENERILCVT---LGTRK-GE-ILRHLPIFIDA------------IQEISKDYK 220
Cdd:COG0707  157 AVVTGNPVRKEILELDRPEARAKLGLDPDKPTLLVFggsQGARAlNEaVPAALAALLEArlqvvhqtgkgdYEEVRAAYA 236
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380763148 221 nltiifplAHPDHEAIIKPFLDNIQfnylflsnerlKAYAVSDLALAKSGTNTL-EISASGTPMV 284
Cdd:COG0707  237 --------AAIRPNAEVFPFIDDMA-----------DAYAAADLVISRAGASTVaELAALGKPAI 282
 
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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