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Conserved domains on  [gi|16129633|ref|NP_416192|]
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murein lipoprotein [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

PRK15396 family protein( domain architecture ID 10015102)

PRK15396 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15396 PRK15396
major outer membrane lipoprotein;
1-78 2.30e-38

major outer membrane lipoprotein;


:

Pssm-ID: 185294  Cd Length: 78  Bit Score: 121.92  E-value: 2.30e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129633   1 MKATKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNMATKYRK 78
Cdd:PRK15396  1 MNRTKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNQATKYRK 78
 
Name Accession Description Interval E-value
PRK15396 PRK15396
major outer membrane lipoprotein;
1-78 2.30e-38

major outer membrane lipoprotein;


Pssm-ID: 185294  Cd Length: 78  Bit Score: 121.92  E-value: 2.30e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129633   1 MKATKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNMATKYRK 78
Cdd:PRK15396  1 MNRTKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNQATKYRK 78
Lpp COG4238
Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis];
4-78 3.46e-31

Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443380 [Multi-domain]  Cd Length: 77  Bit Score: 103.89  E-value: 3.46e-31
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129633  4 TKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNMATKYRK 78
Cdd:COG4238  3 RKLLLGAAILSSLLLAGCSNNSKIDQLSSDVQSLNAKVDQLSNDVSALRADVQAAKEEAARANQRLDNQATSYKK 77
LPP pfam04728
Lipoprotein leucine-zipper; This is leucine-zipper is found in the enterobacterial outer ...
 26-78 3.25e-18

Lipoprotein leucine-zipper; This is leucine-zipper is found in the enterobacterial outer membrane lipoprotein LPP. It is likely that this domain oligomerises and is involved in protein-protein interactions. As such it is a bundle of alpha-helical coiled-coils, which are known to play key roles in mediating specific protein-protein interactions for in molecular recognition and the assembly of multi-protein complexes.


Pssm-ID: 428092 [Multi-domain]  Cd Length: 53  Bit Score: 70.46  E-value: 3.25e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16129633   26 KIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNMATKYRK 78
Cdd:pfam04728  1 KVDQLSSQVSSLKSKVDQLSSDVNSAKADVQAAKEEAARANQRLDNQASSYKK 53
Ala_zip_lipo NF040598
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ...
 4-75 8.67e-13

Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more narrowly focused. All member sequences of the seed alignment are bacterial lipoproteins between 78 and 103 amino acids in length. Members include OprI (major outer membrane lipoprotein I) from Pseudomonas aeruginosa, and Lpp (Braun's lipoprotein), called the most abundant protein in Escherichia coli. Lpp becomes covalently linked to the cell wall, while anchored in the inner leaflet of the outer membrane, providing structural stability to the cell envelope.


Pssm-ID: 468572 [Multi-domain]  Cd Length: 90  Bit Score: 57.69  E-value: 8.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129633   4 TKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRS--------------DVQAAKDDAARANQRL 69
Cdd:NF040598  1 KKLKLSALALSLALLAGCATTSDLENLQSQVQELDAKVDQASSDAAAAQSradeaaakaeqaeaAANAAQQEADEANERA 80


                ....*.
gi 16129633  70 DNMATK 75
Cdd:NF040598 81 DRMFKK 86
 
Name Accession Description Interval E-value
PRK15396 PRK15396
major outer membrane lipoprotein;
1-78 2.30e-38

major outer membrane lipoprotein;


Pssm-ID: 185294  Cd Length: 78  Bit Score: 121.92  E-value: 2.30e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129633   1 MKATKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNMATKYRK 78
Cdd:PRK15396  1 MNRTKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNQATKYRK 78
Lpp COG4238
Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis];
4-78 3.46e-31

Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443380 [Multi-domain]  Cd Length: 77  Bit Score: 103.89  E-value: 3.46e-31
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129633  4 TKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNMATKYRK 78
Cdd:COG4238  3 RKLLLGAAILSSLLLAGCSNNSKIDQLSSDVQSLNAKVDQLSNDVSALRADVQAAKEEAARANQRLDNQATSYKK 77
PRK09973 PRK09973
lipoprotein YqhH;
4-70 1.20e-19

lipoprotein YqhH;


Pssm-ID: 170188  Cd Length: 85  Bit Score: 75.03  E-value: 1.20e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129633   4 TKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLD 70
Cdd:PRK09973  3 TIFTVGAVVLATCLLSGCVNEQKVNQLASNVQTLNAKIARLEQDMKALRPQIYAAKSEANRANTRLD 69
LPP pfam04728
Lipoprotein leucine-zipper; This is leucine-zipper is found in the enterobacterial outer ...
 26-78 3.25e-18

Lipoprotein leucine-zipper; This is leucine-zipper is found in the enterobacterial outer membrane lipoprotein LPP. It is likely that this domain oligomerises and is involved in protein-protein interactions. As such it is a bundle of alpha-helical coiled-coils, which are known to play key roles in mediating specific protein-protein interactions for in molecular recognition and the assembly of multi-protein complexes.


Pssm-ID: 428092 [Multi-domain]  Cd Length: 53  Bit Score: 70.46  E-value: 3.25e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16129633   26 KIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNMATKYRK 78
Cdd:pfam04728  1 KVDQLSSQVSSLKSKVDQLSSDVNSAKADVQAAKEEAARANQRLDNQASSYKK 53
Ala_zip_lipo NF040598
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ...
 4-75 8.67e-13

Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more narrowly focused. All member sequences of the seed alignment are bacterial lipoproteins between 78 and 103 amino acids in length. Members include OprI (major outer membrane lipoprotein I) from Pseudomonas aeruginosa, and Lpp (Braun's lipoprotein), called the most abundant protein in Escherichia coli. Lpp becomes covalently linked to the cell wall, while anchored in the inner leaflet of the outer membrane, providing structural stability to the cell envelope.


Pssm-ID: 468572 [Multi-domain]  Cd Length: 90  Bit Score: 57.69  E-value: 8.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129633   4 TKLVLGAVILGSTLLAGCSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRS--------------DVQAAKDDAARANQRL 69
Cdd:NF040598  1 KKLKLSALALSLALLAGCATTSDLENLQSQVQELDAKVDQASSDAAAAQSradeaaakaeqaeaAANAAQQEADEANERA 80


                ....*.
gi 16129633  70 DNMATK 75
Cdd:NF040598 81 DRMFKK 86
 
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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