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Conserved domains on  [gi|446762694|ref|WP_000839950|]
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enterohemolysin-activating lysine-acyltransferase EhxC [Escherichia coli]

Protein Classification

protein-lysine palmitoyltransferase( domain architecture ID 10006837)

protein-lysine palmitoyltransferase catalyzes palmitoylation of the protoxin (CyaA) at two internal lysine residues, thereby converting it to the active toxin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HlyC COG2994
ACP:hemolysin acyltransferase (hemolysin-activating protein) [Posttranslational modification, ...
 4-140 5.14e-56

ACP:hemolysin acyltransferase (hemolysin-activating protein) [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 442233  Cd Length: 143  Bit Score: 172.85  E-value: 5.14e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446762694   4 NAFDVMGKVAWLWACSPLHKKWPLSVFAINVIPAIQTNQFALL-IKDELPVAFCSWASLDLECEVKYINDVTSLYAKDWM 82
Cdd:COG2994    4 NEAEALGAVVWLMMQSPLHRHYPLSDLEWRILPAIQLGQFKLYfDEDGRPIAFVSWAWLSEEAEAKLLTDDRELTAEEWN 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446762694  83 SGERKWFIDWIAPFGHNMELYKYMRKK-YPYELFRAIRLDESSKTG-KIAEFHGGGIDKK 140
Cdd:COG2994   84 SGDRLWIIDFIAPFGHARQMLRDLRKNlFPGEKIRALRHRPDKGSIrKVMRFKGSQVSKE 143
 
Name Accession Description Interval E-value
HlyC COG2994
ACP:hemolysin acyltransferase (hemolysin-activating protein) [Posttranslational modification, ...
 4-140 5.14e-56

ACP:hemolysin acyltransferase (hemolysin-activating protein) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442233  Cd Length: 143  Bit Score: 172.85  E-value: 5.14e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446762694   4 NAFDVMGKVAWLWACSPLHKKWPLSVFAINVIPAIQTNQFALL-IKDELPVAFCSWASLDLECEVKYINDVTSLYAKDWM 82
Cdd:COG2994    4 NEAEALGAVVWLMMQSPLHRHYPLSDLEWRILPAIQLGQFKLYfDEDGRPIAFVSWAWLSEEAEAKLLTDDRELTAEEWN 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446762694  83 SGERKWFIDWIAPFGHNMELYKYMRKK-YPYELFRAIRLDESSKTG-KIAEFHGGGIDKK 140
Cdd:COG2994   84 SGDRLWIIDFIAPFGHARQMLRDLRKNlFPGEKIRALRHRPDKGSIrKVMRFKGSQVSKE 143
HlyC pfam02794
RTX toxin acyltransferase family; Members of this family are enzymes EC:2.3.1.-. involved in ...
 8-132 5.37e-38

RTX toxin acyltransferase family; Members of this family are enzymes EC:2.3.1.-. involved in fatty acylation of the protoxins (HlyA) at lysine residues, thereby converting them to the active toxin. Acyl-acyl carrier protein (ACP) is the essential acyl donor. This family show a number of conserved residues that are possible candidates for participation in acyl transfer. Site-directed mutagenesis of the single conserved histidine residue in Swiss:P06736 resulted in complete inactivation of the enzyme.


Pssm-ID: 426986  Cd Length: 127  Bit Score: 126.68  E-value: 5.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446762694    8 VMGKVAWLWACSPLHKKWPLSVFAINVIPAIQTNQFALLIKDELPVAFCSWASLDLECEVKYINDVTSLYAKDWMSGERK 87
Cdd:pfam02794   1 ALGEIVWLWMHSPLHRDVPVAELSWNLLPAIKLGQFRLYRKNGKPVAFCTWAFVDEEVEQKLLAGDRNLGPEDWNSGERL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 446762694   88 WFIDWIAPFGHNMELYKYMRKKY-PYELFRAIRLDESSKTG-KIAEF 132
Cdd:pfam02794  81 WLIDWIAPFGHARKMRRDLRRNLfPGRKVRALRVHKGSGKGlRVMEW 127
 
Name Accession Description Interval E-value
HlyC COG2994
ACP:hemolysin acyltransferase (hemolysin-activating protein) [Posttranslational modification, ...
 4-140 5.14e-56

ACP:hemolysin acyltransferase (hemolysin-activating protein) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442233  Cd Length: 143  Bit Score: 172.85  E-value: 5.14e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446762694   4 NAFDVMGKVAWLWACSPLHKKWPLSVFAINVIPAIQTNQFALL-IKDELPVAFCSWASLDLECEVKYINDVTSLYAKDWM 82
Cdd:COG2994    4 NEAEALGAVVWLMMQSPLHRHYPLSDLEWRILPAIQLGQFKLYfDEDGRPIAFVSWAWLSEEAEAKLLTDDRELTAEEWN 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446762694  83 SGERKWFIDWIAPFGHNMELYKYMRKK-YPYELFRAIRLDESSKTG-KIAEFHGGGIDKK 140
Cdd:COG2994   84 SGDRLWIIDFIAPFGHARQMLRDLRKNlFPGEKIRALRHRPDKGSIrKVMRFKGSQVSKE 143
HlyC pfam02794
RTX toxin acyltransferase family; Members of this family are enzymes EC:2.3.1.-. involved in ...
 8-132 5.37e-38

RTX toxin acyltransferase family; Members of this family are enzymes EC:2.3.1.-. involved in fatty acylation of the protoxins (HlyA) at lysine residues, thereby converting them to the active toxin. Acyl-acyl carrier protein (ACP) is the essential acyl donor. This family show a number of conserved residues that are possible candidates for participation in acyl transfer. Site-directed mutagenesis of the single conserved histidine residue in Swiss:P06736 resulted in complete inactivation of the enzyme.


Pssm-ID: 426986  Cd Length: 127  Bit Score: 126.68  E-value: 5.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446762694    8 VMGKVAWLWACSPLHKKWPLSVFAINVIPAIQTNQFALLIKDELPVAFCSWASLDLECEVKYINDVTSLYAKDWMSGERK 87
Cdd:pfam02794   1 ALGEIVWLWMHSPLHRDVPVAELSWNLLPAIKLGQFRLYRKNGKPVAFCTWAFVDEEVEQKLLAGDRNLGPEDWNSGERL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 446762694   88 WFIDWIAPFGHNMELYKYMRKKY-PYELFRAIRLDESSKTG-KIAEF 132
Cdd:pfam02794  81 WLIDWIAPFGHARKMRRDLRRNLfPGRKVRALRVHKGSGKGlRVMEW 127
 
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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