NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|691056712|ref|WP_032001760|]
View 

phosphoethanolamine transferase domain-containing protein, partial [Acinetobacter baumannii]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
OpgE super family cl43638
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
 1-143 5.89e-51

Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG2194:

Pssm-ID: 441797 [Multi-domain]  Cd Length: 537  Bit Score: 169.65  E-value: 5.89e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691056712   1 VKFKQEKVSRLLLKKVFSLVASFAVVGVLLFTYYVDFAAIFREHRDLKGMISPQNSISSLMSYYHKKAPKKNLPLVIYGQ 80
Cdd:COG2194  137 VRIRYRPLLRELGQRLALLLLALLVIVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPLGA 216

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 691056712  81 DAHQVQRVQKnlPKLMILVVGETARAESFSLNGYAKNTNPELSKQ-DIFNFSQVSSCGTATAVS 143
Cdd:COG2194  217 DAKLAAAGAK--PTLVVLVVGETARADNFSLNGYARDTTPELAKEkNLVSFRDVTSCGTATAVS 278
 
Name Accession Description Interval E-value
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
 1-143 5.89e-51

Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441797 [Multi-domain]  Cd Length: 537  Bit Score: 169.65  E-value: 5.89e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691056712   1 VKFKQEKVSRLLLKKVFSLVASFAVVGVLLFTYYVDFAAIFREHRDLKGMISPQNSISSLMSYYHKKAPKKNLPLVIYGQ 80
Cdd:COG2194  137 VRIRYRPLLRELGQRLALLLLALLVIVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPLGA 216

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 691056712  81 DAHQVQRVQKnlPKLMILVVGETARAESFSLNGYAKNTNPELSKQ-DIFNFSQVSSCGTATAVS 143
Cdd:COG2194  217 DAKLAAAGAK--PTLVVLVVGETARADNFSLNGYARDTTPELAKEkNLVSFRDVTSCGTATAVS 278
PRK11598 PRK11598
putative metal dependent hydrolase; Provisional
 10-143 8.70e-41

putative metal dependent hydrolase; Provisional


Pssm-ID: 183224 [Multi-domain]  Cd Length: 545  Bit Score: 142.51  E-value: 8.70e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691056712  10 RLLLKKVFSLVASFAVVGVLLFTYYVDFAAIFREHRDLKGMISPQNSISSLMSYYHKKApKKNLPLVIYGQDAHQVQRVQ 89
Cdd:PRK11598 151 RSVLFRLANILVSVLLILLVAALFYKDYASLFRNNKELVKSLTPSNSIVASWSWYSHQR-LANLPLVRIGEDAHKNPLMQ 229

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 691056712  90 KNLPK-LMILVVGETARAESFSLNGYAKNTNPELSKQDIFNFSQVSSCGTATAVS 143
Cdd:PRK11598 230 NQKRKnLTILVVGETSRAENFSLGGYPRETNPRLAKDNVIYFPHTTSCGTATAVS 284
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 93-143 5.10e-20

Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.


Pssm-ID: 293741 [Multi-domain]  Cd Length: 288  Bit Score: 83.06  E-value: 5.10e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 691056712  93 PKLMILVVGETARAESFSLNGYAKNTNPELSKQ--DIFNFSQVSSCGTATAVS 143
Cdd:cd16017    2 PKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLkkNLIVFDNVISCGTSTAVS 54
EptA_B_N pfam08019
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ...
 1-67 5.53e-13

Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of bacterial phosphoethanolamine transferases, including eptA from Helicobacter pylori and eptB from Escherichia coli EC:2.7.8.42. This domain is found immediately N-terminal to the sulphatase domain in many sulphatases.


Pssm-ID: 429788 [Multi-domain]  Cd Length: 151  Bit Score: 61.77  E-value: 5.53e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 691056712    1 VKFKQEKVSRLLLKKVFSLVASFAVVGVLLFTYYVDFAAIFREHRDLKGMISPQNSISSLMSYYHKK 67
Cdd:pfam08019  85 VRIRYRPWLRELLSRLALILVSLLVIGLVAFLFYKDYASFFRNHKELRYLINPTNYIYSTVKYAKHQ 151
 
Name Accession Description Interval E-value
OpgE COG2194
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ...
 1-143 5.89e-51

Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441797 [Multi-domain]  Cd Length: 537  Bit Score: 169.65  E-value: 5.89e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691056712   1 VKFKQEKVSRLLLKKVFSLVASFAVVGVLLFTYYVDFAAIFREHRDLKGMISPQNSISSLMSYYHKKAPKKNLPLVIYGQ 80
Cdd:COG2194  137 VRIRYRPLLRELGQRLALLLLALLVIVLLALLFYKDYASFFRNHKELRYLINPSNFIYALGKYAKARYFAAPLPLQPLGA 216

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 691056712  81 DAHQVQRVQKnlPKLMILVVGETARAESFSLNGYAKNTNPELSKQ-DIFNFSQVSSCGTATAVS 143
Cdd:COG2194  217 DAKLAAAGAK--PTLVVLVVGETARADNFSLNGYARDTTPELAKEkNLVSFRDVTSCGTATAVS 278
PRK11598 PRK11598
putative metal dependent hydrolase; Provisional
 10-143 8.70e-41

putative metal dependent hydrolase; Provisional


Pssm-ID: 183224 [Multi-domain]  Cd Length: 545  Bit Score: 142.51  E-value: 8.70e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691056712  10 RLLLKKVFSLVASFAVVGVLLFTYYVDFAAIFREHRDLKGMISPQNSISSLMSYYHKKApKKNLPLVIYGQDAHQVQRVQ 89
Cdd:PRK11598 151 RSVLFRLANILVSVLLILLVAALFYKDYASLFRNNKELVKSLTPSNSIVASWSWYSHQR-LANLPLVRIGEDAHKNPLMQ 229

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 691056712  90 KNLPK-LMILVVGETARAESFSLNGYAKNTNPELSKQDIFNFSQVSSCGTATAVS 143
Cdd:PRK11598 230 NQKRKnLTILVVGETSRAENFSLGGYPRETNPRLAKDNVIYFPHTTSCGTATAVS 284
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
 93-143 5.10e-20

Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.


Pssm-ID: 293741 [Multi-domain]  Cd Length: 288  Bit Score: 83.06  E-value: 5.10e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 691056712  93 PKLMILVVGETARAESFSLNGYAKNTNPELSKQ--DIFNFSQVSSCGTATAVS 143
Cdd:cd16017    2 PKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLkkNLIVFDNVISCGTSTAVS 54
EptA_B_N pfam08019
Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of ...
 1-67 5.53e-13

Phosphoethanolamine transferase EptA/EptB; This entry represents a domain found in a group of bacterial phosphoethanolamine transferases, including eptA from Helicobacter pylori and eptB from Escherichia coli EC:2.7.8.42. This domain is found immediately N-terminal to the sulphatase domain in many sulphatases.


Pssm-ID: 429788 [Multi-domain]  Cd Length: 151  Bit Score: 61.77  E-value: 5.53e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 691056712    1 VKFKQEKVSRLLLKKVFSLVASFAVVGVLLFTYYVDFAAIFREHRDLKGMISPQNSISSLMSYYHKK 67
Cdd:pfam08019  85 VRIRYRPWLRELLSRLALILVSLLVIGLVAFLFYKDYASFFRNHKELRYLINPTNYIYSTVKYAKHQ 151
Sulfatase pfam00884
Sulfatase;
94-143 8.36e-10

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 55.12  E-value: 8.36e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 691056712   94 KLMILVVGETARAESFSLNGYAKNTNPELSK--QDIFNFSQVSSCGTATAVS 143
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRlaEEGLLFSNFYSGGTLTAPS 52
PRK11560 PRK11560
kdo(2)-lipid A phosphoethanolamine 7''-transferase;
97-143 3.00e-05

kdo(2)-lipid A phosphoethanolamine 7''-transferase;


Pssm-ID: 183198 [Multi-domain]  Cd Length: 558  Bit Score: 42.33  E-value: 3.00e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 691056712  97 ILVVGETARAESFSLNGYAKNTNPELSKQDIFNFSQVSSCGTATAVS 143
Cdd:PRK11560 251 VFIIGETTRWDHMGILGYERNTTPKLAQEKNLAAFRGYSCDTATKLS 297
PRK10649 PRK10649
phosphoethanolamine transferase CptA;
55-124 2.35e-04

phosphoethanolamine transferase CptA;


Pssm-ID: 182617 [Multi-domain]  Cd Length: 577  Bit Score: 39.69  E-value: 2.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691056712  55 NSISSLMSYYHKKAPKKNLplviygQDAHQVQrvqknlPKLMILVVGETARAESFSLNGYAKNTNPELSK 124
Cdd:PRK10649 210 NSLQKLLNENAALPPLANL------KDESGNA------PRTLVLVIGESTQRGRMSLYGYPRETTPELDA 267
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH