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Conserved domains on  [gi|1306838510|ref|WP_101005326|]
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lipid A 4'-phosphatase [Helicobacter pylori]

Protein Classification

phosphatase PAP2 family protein( domain architecture ID 10130278)

type 2 phosphatidic acid phosphatase (PAP2) family protein similar to Helicobacter pylori lipid A 4'-phosphatase that removes the 4'-phosphate group from tetra- and hexa-acylated lipid A species

CATH:  1.20.144.10
EC:  3.1.3.-
Gene Ontology:  GO:0016791|GO:0016311|GO:0008610|GO:0006644
PubMed:  9122162|12447906|9260289
SCOP:  3001110|4001226

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 53-166 1.26e-33

PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.


:

Pssm-ID: 239488 [Multi-domain]  Cd Length: 106  Bit Score: 115.51  E-value: 1.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306838510  53 DYRGLGELAVGTLVTQGVIYGLKGAFSNAHKDGARvefakrpccNSWRGMPSGHAGGVFSAAGFVYYRYGW-KPALPVIA 131
Cdd:cd03394     1 DREGLLILAEAAALTAAVTEGLKFAVGRARPDGSN---------NGYRSFPSGHTASAFAAATFLQYRYGWrWYGIPAYA 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1306838510 132 LAILTDASRVVARQHTILQVTIGSLIAWGFAYLFT 166
Cdd:cd03394    72 LASLVGASRVVANRHWLSDVLAGAAIGILVGYLVT 106
 
Name Accession Description Interval E-value
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 53-166 1.26e-33

PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.


Pssm-ID: 239488 [Multi-domain]  Cd Length: 106  Bit Score: 115.51  E-value: 1.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306838510  53 DYRGLGELAVGTLVTQGVIYGLKGAFSNAHKDGARvefakrpccNSWRGMPSGHAGGVFSAAGFVYYRYGW-KPALPVIA 131
Cdd:cd03394     1 DREGLLILAEAAALTAAVTEGLKFAVGRARPDGSN---------NGYRSFPSGHTASAFAAATFLQYRYGWrWYGIPAYA 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1306838510 132 LAILTDASRVVARQHTILQVTIGSLIAWGFAYLFT 166
Cdd:cd03394    72 LASLVGASRVVANRHWLSDVLAGAAIGILVGYLVT 106
PRK09597 PRK09597
lipid A 1-phosphatase LpxE;
38-171 1.49e-12

lipid A 1-phosphatase LpxE;


Pssm-ID: 181978  Cd Length: 190  Bit Score: 63.37  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306838510  38 RFLP-IFVGTVSLAMRDYRGLGELAVGTLVTQGVIYGLKGAFSNAHKDGARVefAKRPCCNSWrGMPSGHAGGVFSAAGF 116
Cdd:PRK09597   59 RFIPtILSVAIPLIQRDAIGLFQVANASIATTLLTHTTKRALNHVTINDQRL--GERPYGGNF-NMPSGHSSMVGLAVAF 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1306838510 117 VYYRYGWKPALPVIALAILTDASRVVARQHTILQVTIGSLIAWGFAYLFTSRYKP 171
Cdd:PRK09597  136 LMRRYSFKKYWWLLPLIPLTMLARIYLDMHTIGAVLAGLGVGMLCVSLFTSPKKK 190
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 60-166 3.63e-07

PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.


Pssm-ID: 426329 [Multi-domain]  Cd Length: 124  Bit Score: 47.03  E-value: 3.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306838510  60 LAVGTLVTQGVIYGLKGAFS----NAHKDGARVEFAKRPCCNSWRGMPSGHAGGVFSAAGFVYYRYGWKPALPV------ 129
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGrprpFFLLLEGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRvllall 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1306838510 130 -IALAILTDASRVVARQHTILQVTIGSLIAWGFAYLFT 166
Cdd:pfam01569  82 lLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVY 119
acidPPc smart00014
Acid phosphatase homologues;
98-165 4.42e-04

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 38.48  E-value: 4.42e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1306838510   98 SWRGMPSGHAGGVFSAAGFVYY----RYGWKPALPV-IALAILTDASRVVARQHTILQVTIGSLIAWGFAYLF 165
Cdd:smart00014  43 AGYSFPSGHTAFAFAFALFLLLylpaRAGRKLLIFLlLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVL 115
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 101-170 1.46e-03

Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; Membrane-associated phospholipid phosphatase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 440435 [Multi-domain]  Cd Length: 189  Bit Score: 38.10  E-value: 1.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1306838510 101 GMPSGHAGGVFSAAGFVYYRYGWKP-ALPVIALAILTDASRVVARQHTILQVTIGSLIAWGFAYLFTSRYK 170
Cdd:COG0671   118 SFPSGHAAAAFALALVLALLLPRRWlAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALLR 188
 
Name Accession Description Interval E-value
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 53-166 1.26e-33

PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.


Pssm-ID: 239488 [Multi-domain]  Cd Length: 106  Bit Score: 115.51  E-value: 1.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306838510  53 DYRGLGELAVGTLVTQGVIYGLKGAFSNAHKDGARvefakrpccNSWRGMPSGHAGGVFSAAGFVYYRYGW-KPALPVIA 131
Cdd:cd03394     1 DREGLLILAEAAALTAAVTEGLKFAVGRARPDGSN---------NGYRSFPSGHTASAFAAATFLQYRYGWrWYGIPAYA 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1306838510 132 LAILTDASRVVARQHTILQVTIGSLIAWGFAYLFT 166
Cdd:cd03394    72 LASLVGASRVVANRHWLSDVLAGAAIGILVGYLVT 106
PRK09597 PRK09597
lipid A 1-phosphatase LpxE;
38-171 1.49e-12

lipid A 1-phosphatase LpxE;


Pssm-ID: 181978  Cd Length: 190  Bit Score: 63.37  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306838510  38 RFLP-IFVGTVSLAMRDYRGLGELAVGTLVTQGVIYGLKGAFSNAHKDGARVefAKRPCCNSWrGMPSGHAGGVFSAAGF 116
Cdd:PRK09597   59 RFIPtILSVAIPLIQRDAIGLFQVANASIATTLLTHTTKRALNHVTINDQRL--GERPYGGNF-NMPSGHSSMVGLAVAF 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1306838510 117 VYYRYGWKPALPVIALAILTDASRVVARQHTILQVTIGSLIAWGFAYLFTSRYKP 171
Cdd:PRK09597  136 LMRRYSFKKYWWLLPLIPLTMLARIYLDMHTIGAVLAGLGVGMLCVSLFTSPKKK 190
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 54-165 8.58e-10

PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, includes type 2 phosphatidic acid phosphatase or lipid phosphate phosphatase (LPP), Glucose-6-phosphatase, Phosphatidylglycerophosphatase B and bacterial acid phosphatase, vanadium chloroperoxidases, vanadium bromoperoxidases, and several other mostly uncharacterized subfamilies. Several members of this superfamily have been predicted to be transmembrane proteins.


Pssm-ID: 238813 [Multi-domain]  Cd Length: 122  Bit Score: 54.39  E-value: 8.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306838510  54 YRGLGELAVGTLVTQGVIYGLKGAFSNA---HKDGARVEFAKRPCCNSWRGMPSGHAGGVFSAAGFVYYRYG-----WKP 125
Cdd:cd01610     2 RLLALLLLLALLAGLLLTGVLKYLFGRPrpyFLLRCGPDGDPLLLTEGGYSFPSGHAAFAFALALFLALLLPrrllrLLL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1306838510 126 ALPVIALAILTDASRVVARQHTILQVTIGSLIAWGFAYLF 165
Cdd:cd01610    82 GLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLV 121
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 60-166 3.63e-07

PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.


Pssm-ID: 426329 [Multi-domain]  Cd Length: 124  Bit Score: 47.03  E-value: 3.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306838510  60 LAVGTLVTQGVIYGLKGAFS----NAHKDGARVEFAKRPCCNSWRGMPSGHAGGVFSAAGFVYYRYGWKPALPV------ 129
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGrprpFFLLLEGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRvllall 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1306838510 130 -IALAILTDASRVVARQHTILQVTIGSLIAWGFAYLFT 166
Cdd:pfam01569  82 lLVLALLVGLSRLYLGVHFPSDVLAGALIGILLALLVY 119
PAP2_lipid_A_1_phosphatase cd03389
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ...
 97-169 1.96e-06

PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from Francisella novicida selectively dephosphorylates lipid A at the 1-position. Lipid A is the membrane-anchor component of lipopolysaccharides (LPS), the major constituents of the outer membrane in many gram-negative bacteria.


Pssm-ID: 239483  Cd Length: 186  Bit Score: 46.16  E-value: 1.96e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1306838510  97 NSWRGMPSGH---AGGVFSAAGFVYYRYGWkpalPVIALAILTDASRVVARQHTILQVTIGSLIAWGFAYLFTSRY 169
Cdd:cd03389   115 YAFTSFPSGHsatAGAAAAALALLFPRYRW----AFILLALLIAFSRVIVGAHYPSDVIAGSLLGAVTALALYQRF 186
PAP2_diacylglycerolkinase cd03383
PAP2_like proteins, diacylglycerol_kinase like sub-family. In some prokaryotes, PAP2_like ...
 101-164 3.76e-05

PAP2_like proteins, diacylglycerol_kinase like sub-family. In some prokaryotes, PAP2_like phosphatase domains appear fused to E. coli DAGK-like trans-membrane diacylglycerol kinase domains. The cellular function of these architectures remains to be determined.


Pssm-ID: 239478 [Multi-domain]  Cd Length: 109  Bit Score: 41.16  E-value: 3.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1306838510 101 GMPSGHAGGVFSAAGFV-YYRYGWKPALPVIALAILTDASRVVARQHTILQVTIGSLIAWGFAYL 164
Cdd:cd03383    40 GMPSGHAAIAFSIATAIsLITNNPIISILSVLLAVMVAHSRVEMKIHTMWEVVVGAILGALITLL 104
acidPPc smart00014
Acid phosphatase homologues;
98-165 4.42e-04

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 38.48  E-value: 4.42e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1306838510   98 SWRGMPSGHAGGVFSAAGFVYY----RYGWKPALPV-IALAILTDASRVVARQHTILQVTIGSLIAWGFAYLF 165
Cdd:smart00014  43 AGYSFPSGHTAFAFAFALFLLLylpaRAGRKLLIFLlLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVL 115
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 101-170 1.46e-03

Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; Membrane-associated phospholipid phosphatase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 440435 [Multi-domain]  Cd Length: 189  Bit Score: 38.10  E-value: 1.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1306838510 101 GMPSGHAGGVFSAAGFVYYRYGWKP-ALPVIALAILTDASRVVARQHTILQVTIGSLIAWGFAYLFTSRYK 170
Cdd:COG0671   118 SFPSGHAAAAFALALVLALLLPRRWlAALLLALALLVGLSRVYLGVHYPSDVLAGALLGLAIALLLLALLR 188
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 39-166 1.57e-03

PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a membrane-associated protein located in the endoplasmic reticulum and hydrolyzes dolichyl pyrophosphate, as well as dolichylmonophosphate at a low rate. The enzyme is necessary for maintaining proper levels of dolichol-linked oligosaccharides and protein N-glycosylation, and might play a role in re-utilization of the glycosyl carrier lipid for additional rounds of lipid intermediate biosynthesis after its release during protein N-glycosylation reactions.


Pssm-ID: 239477  Cd Length: 159  Bit Score: 37.64  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1306838510  39 FLPIFVG----TVSLAMRDYRGLgELAVGTLVTQGVIYGLKGAFSNA----HKDGARVEFakrpccnswrGMPSGHAG-- 108
Cdd:cd03382    23 LLPVAILvgyaTLILFRRELEAI-YLFIGLLANEALNYVLKRIIKEPrpcsGAYFVRSGY----------GMPSSHSQfm 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1306838510 109 GVFSAAGFVYYRYGWKP----------ALPVIALAILTDASRVVARQHTILQVTIGSLIAWGFAYLFT 166
Cdd:cd03382    92 GFFAVYLLLFIYLRLGRlnslvsrfllSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVGILLGILWF 159
 
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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