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Conserved domains on  [gi|16130172|ref|NP_416740|]
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putative lipopolysaccharide kinase InaA [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

lipopolysaccharide kinase InaA( domain architecture ID 10013369)

lipopolysaccharide kinase InaA belongs to the protein kinase superfamily and may function as an environmental sensor responsive to several stimuli, including internal pH, proton motive force, temperature, and possibly other unknown factors

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09902 PRK09902
lipopolysaccharide kinase InaA;
1-216 1.80e-171

lipopolysaccharide kinase InaA;


:

Pssm-ID: 182136  Cd Length: 216  Bit Score: 469.54  E-value: 1.80e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130172    1 MAVSAKYDEFNHWWATEGDWVEEPNYRRNGMSGVQCVERNGKKLYVKRMTHHLFHSVRYPFGRPTIVREVAVIKELERAG 80
Cdd:PRK09902   1 MAVSAKYDEFNHWWATEGDWVEEPNYRRNGMSGVQCVERNGKKLYVKRMTHHLFHSVRYPFGRPTIVREVAVIKELERAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130172   81 VIVPKIVFGEAVKIEGEWRALLVTEDMAGFISIADWYAQHAVSPYSDEVRQAMLKAVALAFKKMHSINRQHGCCYVRHIY 160
Cdd:PRK09902  81 VIVPKIVFGEAVKIEGEWRALLVTEDMAGFISIADWYAQHAVSPYSDEVRQAMLKAVALAFKKMHSVNRQHGCCYVRHIY 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130172  161 VKTEGNAEAGFLDLEKSRRRLRRDKAINHDFRQLEKYLEPIPKADWEQVKAYYYAM 216
Cdd:PRK09902 161 VKTEGKAEAGFLDLEKSRRRLRRDKAINHDFRQLEKYLEPIPKADWEQVKAYYYAM 216
 
Name Accession Description Interval E-value
PRK09902 PRK09902
lipopolysaccharide kinase InaA;
1-216 1.80e-171

lipopolysaccharide kinase InaA;


Pssm-ID: 182136  Cd Length: 216  Bit Score: 469.54  E-value: 1.80e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130172    1 MAVSAKYDEFNHWWATEGDWVEEPNYRRNGMSGVQCVERNGKKLYVKRMTHHLFHSVRYPFGRPTIVREVAVIKELERAG 80
Cdd:PRK09902   1 MAVSAKYDEFNHWWATEGDWVEEPNYRRNGMSGVQCVERNGKKLYVKRMTHHLFHSVRYPFGRPTIVREVAVIKELERAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130172   81 VIVPKIVFGEAVKIEGEWRALLVTEDMAGFISIADWYAQHAVSPYSDEVRQAMLKAVALAFKKMHSINRQHGCCYVRHIY 160
Cdd:PRK09902  81 VIVPKIVFGEAVKIEGEWRALLVTEDMAGFISIADWYAQHAVSPYSDEVRQAMLKAVALAFKKMHSVNRQHGCCYVRHIY 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130172  161 VKTEGNAEAGFLDLEKSRRRLRRDKAINHDFRQLEKYLEPIPKADWEQVKAYYYAM 216
Cdd:PRK09902 161 VKTEGKAEAGFLDLEKSRRRLRRDKAINHDFRQLEKYLEPIPKADWEQVKAYYYAM 216
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
 12-213 2.15e-86

Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. enterica.


Pssm-ID: 428872  Cd Length: 206  Bit Score: 253.85  E-value: 2.15e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130172    12 HWWATEGDWVEEPNYRRNGMSGVQCVE-RNGKKLYVKRMTHHLFHS-VRYPFGRPTIVREVAVIKELERAGVIVPKIVFG 89
Cdd:pfam06293   1 AWWALQGRVVGEPNGRRTGWFVVARVGnGVLRKYYRGGMWGHLNRDlYRYPLGRTRAFREFRLIRRLREAGLPVPKPVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130172    90 EAVKIEGEWRALLVTEDMAGFISIADWYAQHAVspYSDEVRQAMLKAVALAFKKMHSINRQHGCCYVRHIYVKTEG--NA 167
Cdd:pfam06293  81 GEVKVGGGYRADLLTERLEGAQSLADWLADWAV--PSGELRRAIWEAVGRLIRQMHRAGVQHGDLYAHHILLQQEGdeGF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 16130172   168 EAGFLDLEKSRRRLRRDKAINHDFRQLEKYL--EPIPKADWEQVKAYY 213
Cdd:pfam06293 159 EAWLIDLDKGRLRLPARRWRNKDLARLLRSFlnIGFTEADWERLLRAY 206
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 67-211 1.87e-05

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 43.41  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130172  67 VREVAVIKELERAGVIVPKIVfgeAVKIEgewRALLVTEDMAGfISIADWYAQhavspysDEVRQAMLKAVALAFKKMHS 146
Cdd:COG3642   4 RREARLLRELREAGVPVPKVL---DVDPD---DADLVMEYIEG-ETLADLLEE-------GELPPELLRELGRLLARLHR 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130172 147 INRQHGCCYVRHIYVkteGNAEAGFLDLEKSRRRLR-RDKAInhDFRQLEKYLEPI-PKADWEQVKA 211
Cdd:COG3642  70 AGIVHGDLTTSNILV---DDGGVYLIDFGLARYSDPlEDKAV--DLAVLKRSLESThPDPAEELWEA 131
 
Name Accession Description Interval E-value
PRK09902 PRK09902
lipopolysaccharide kinase InaA;
1-216 1.80e-171

lipopolysaccharide kinase InaA;


Pssm-ID: 182136  Cd Length: 216  Bit Score: 469.54  E-value: 1.80e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130172    1 MAVSAKYDEFNHWWATEGDWVEEPNYRRNGMSGVQCVERNGKKLYVKRMTHHLFHSVRYPFGRPTIVREVAVIKELERAG 80
Cdd:PRK09902   1 MAVSAKYDEFNHWWATEGDWVEEPNYRRNGMSGVQCVERNGKKLYVKRMTHHLFHSVRYPFGRPTIVREVAVIKELERAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130172   81 VIVPKIVFGEAVKIEGEWRALLVTEDMAGFISIADWYAQHAVSPYSDEVRQAMLKAVALAFKKMHSINRQHGCCYVRHIY 160
Cdd:PRK09902  81 VIVPKIVFGEAVKIEGEWRALLVTEDMAGFISIADWYAQHAVSPYSDEVRQAMLKAVALAFKKMHSVNRQHGCCYVRHIY 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130172  161 VKTEGNAEAGFLDLEKSRRRLRRDKAINHDFRQLEKYLEPIPKADWEQVKAYYYAM 216
Cdd:PRK09902 161 VKTEGKAEAGFLDLEKSRRRLRRDKAINHDFRQLEKYLEPIPKADWEQVKAYYYAM 216
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
 12-213 2.15e-86

Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. enterica.


Pssm-ID: 428872  Cd Length: 206  Bit Score: 253.85  E-value: 2.15e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130172    12 HWWATEGDWVEEPNYRRNGMSGVQCVE-RNGKKLYVKRMTHHLFHS-VRYPFGRPTIVREVAVIKELERAGVIVPKIVFG 89
Cdd:pfam06293   1 AWWALQGRVVGEPNGRRTGWFVVARVGnGVLRKYYRGGMWGHLNRDlYRYPLGRTRAFREFRLIRRLREAGLPVPKPVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130172    90 EAVKIEGEWRALLVTEDMAGFISIADWYAQHAVspYSDEVRQAMLKAVALAFKKMHSINRQHGCCYVRHIYVKTEG--NA 167
Cdd:pfam06293  81 GEVKVGGGYRADLLTERLEGAQSLADWLADWAV--PSGELRRAIWEAVGRLIRQMHRAGVQHGDLYAHHILLQQEGdeGF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 16130172   168 EAGFLDLEKSRRRLRRDKAINHDFRQLEKYL--EPIPKADWEQVKAYY 213
Cdd:pfam06293 159 EAWLIDLDKGRLRLPARRWRNKDLARLLRSFlnIGFTEADWERLLRAY 206
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 67-211 1.87e-05

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 43.41  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130172  67 VREVAVIKELERAGVIVPKIVfgeAVKIEgewRALLVTEDMAGfISIADWYAQhavspysDEVRQAMLKAVALAFKKMHS 146
Cdd:COG3642   4 RREARLLRELREAGVPVPKVL---DVDPD---DADLVMEYIEG-ETLADLLEE-------GELPPELLRELGRLLARLHR 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130172 147 INRQHGCCYVRHIYVkteGNAEAGFLDLEKSRRRLR-RDKAInhDFRQLEKYLEPI-PKADWEQVKA 211
Cdd:COG3642  70 AGIVHGDLTTSNILV---DDGGVYLIDFGLARYSDPlEDKAV--DLAVLKRSLESThPDPAEELWEA 131
PRK15123 PRK15123
lipopolysaccharide core heptose(I) kinase RfaP; Provisional
 68-185 9.88e-05

lipopolysaccharide core heptose(I) kinase RfaP; Provisional


Pssm-ID: 237915  Cd Length: 268  Bit Score: 42.25  E-value: 9.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130172   68 REVAVIKELERAGV-IVPKIVFGEavkiEGEW----RALLVTEDMAGFISIADWYAQHAVSPYSDEVRQAMLKAVALAFK 142
Cdd:PRK15123  77 REWRAIHRLHEVGVdTMTGVAFGE----RGSNpatrTSFIITEDLAPTISLEDYCADWATNPPDPRLKRMLIKRVATMVR 152

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16130172  143 KMHSINRQHGCCYVRHIYVKTEGNAEAG-----FLDLEKSRRRLR-----RDK 185
Cdd:PRK15123 153 DMHAAGINHRDCYICHFLLHLPFPGREEdlklsVIDLHRAQIRARvprrwRDK 205
 
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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