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Conserved domains on  [gi|490531805|ref|WP_004396978|]
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MULTISPECIES: Lpp/OprI family alanine-zipper lipoprotein [Vibrio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lpp super family cl47342
Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis];
2-82 1.18e-09

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


The actual alignment was detected with superfamily member COG4238:

Pssm-ID: 443380 [Multi-domain]  Cd Length: 77  Bit Score: 49.58  E-value: 1.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490531805  2 NKMLLAAAASSVLLLAGCASgpdeatTTKLDQLNNQVSQLNSQIAALKSENASLTDAALAAQEEAARANERIDNIAQSYT 81
Cdd:COG4238   3 RKLLLGAAILSSLLLAGCSN------NSKIDQLSSDVQSLNAKVDQLSNDVSALRADVQAAKEEAARANQRLDNQATSYK 76


                .
gi 490531805 82 K 82
Cdd:COG4238  77 K 77
 
Name Accession Description Interval E-value
Lpp COG4238
Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis];
2-82 1.18e-09

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


Pssm-ID: 443380 [Multi-domain]  Cd Length: 77  Bit Score: 49.58  E-value: 1.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490531805  2 NKMLLAAAASSVLLLAGCASgpdeatTTKLDQLNNQVSQLNSQIAALKSENASLTDAALAAQEEAARANERIDNIAQSYT 81
Cdd:COG4238   3 RKLLLGAAILSSLLLAGCSN------NSKIDQLSSDVQSLNAKVDQLSNDVSALRADVQAAKEEAARANQRLDNQATSYK 76


                .
gi 490531805 82 K 82
Cdd:COG4238  77 K 77
LPP pfam04728
Lipoprotein leucine-zipper; This is leucine-zipper is found in the enterobacterial outer ...
 30-82 3.51e-05

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: 37.34  E-value: 3.51e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490531805  30 KLDQLNNQVSQLNSQIAALKSENASLTDAALAAQEEAARANERIDNIAQSYTK 82
Cdd:pfam04728  1 KVDQLSSQVSSLKSKVDQLSSDVNSAKADVQAAKEEAARANQRLDNQASSYKK 53
PRK11530 PRK11530
hypothetical protein; Provisional
 4-56 1.49e-04

hypothetical protein; Provisional


Pssm-ID: 236923  Cd Length: 183  Bit Score: 37.70  E-value: 1.49e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490531805   4 MLLAAAASSVLLLAGCASGPdeatttKLDQLNNQVSQLNSQIAALKSENASLT 56
Cdd:PRK11530   5 YLRLLLLGSLLLLAGCAQQS------EVRQMHNSVSTLNQEMTQLTQQAVAIE 51
Ala_zip_lipo NF040598
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ...
 2-82 1.64e-03

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: 33.81  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490531805  2 NKMLLAAAASSVLLLAGCASGPD-EATTTKLDQLNNQVSQLNSQIAALKSENASLTDAALAAQEEAAR-------ANERI 73
Cdd:NF040598  1 KKLKLSALALSLALLAGCATTSDlENLQSQVQELDAKVDQASSDAAAAQSRADEAAAKAEQAEAAANAaqqeadeANERA 80

                        90
                ....*....|
gi 490531805 74 DNI-AQSYTK 82
Cdd:NF040598 81 DRMfKKSMRK 90
 
Name Accession Description Interval E-value
Lpp COG4238
Outer membrane murein-binding lipoprotein Lpp [Cell wall/membrane/envelope biogenesis];
2-82 1.18e-09

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


Pssm-ID: 443380 [Multi-domain]  Cd Length: 77  Bit Score: 49.58  E-value: 1.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490531805  2 NKMLLAAAASSVLLLAGCASgpdeatTTKLDQLNNQVSQLNSQIAALKSENASLTDAALAAQEEAARANERIDNIAQSYT 81
Cdd:COG4238   3 RKLLLGAAILSSLLLAGCSN------NSKIDQLSSDVQSLNAKVDQLSNDVSALRADVQAAKEEAARANQRLDNQATSYK 76


                .
gi 490531805 82 K 82
Cdd:COG4238  77 K 77
LPP pfam04728
Lipoprotein leucine-zipper; This is leucine-zipper is found in the enterobacterial outer ...
 30-82 3.51e-05

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: 37.34  E-value: 3.51e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490531805  30 KLDQLNNQVSQLNSQIAALKSENASLTDAALAAQEEAARANERIDNIAQSYTK 82
Cdd:pfam04728  1 KVDQLSSQVSSLKSKVDQLSSDVNSAKADVQAAKEEAARANQRLDNQASSYKK 53
PRK11530 PRK11530
hypothetical protein; Provisional
 4-56 1.49e-04

hypothetical protein; Provisional


Pssm-ID: 236923  Cd Length: 183  Bit Score: 37.70  E-value: 1.49e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490531805   4 MLLAAAASSVLLLAGCASGPdeatttKLDQLNNQVSQLNSQIAALKSENASLT 56
Cdd:PRK11530   5 YLRLLLLGSLLLLAGCAQQS------EVRQMHNSVSTLNQEMTQLTQQAVAIE 51
PRK15396 PRK15396
major outer membrane lipoprotein;
2-82 4.99e-04

major outer membrane lipoprotein;


Pssm-ID: 185294  Cd Length: 78  Bit Score: 35.25  E-value: 4.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490531805  2 NKMLLAAAASSVLLLAGCASgpdeatTTKLDQLNNQVSQLNSQIAALKSENASLTDAALAAQEEAARANERIDNIAQSYT 81
Cdd:PRK15396  4 TKLVLGAVILGSTLLAGCSS------NAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNQATKYR 77


                .
gi 490531805 82 K 82
Cdd:PRK15396 78 K 78
Ala_zip_lipo NF040598
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ...
 2-82 1.64e-03

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: 33.81  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490531805  2 NKMLLAAAASSVLLLAGCASGPD-EATTTKLDQLNNQVSQLNSQIAALKSENASLTDAALAAQEEAAR-------ANERI 73
Cdd:NF040598  1 KKLKLSALALSLALLAGCATTSDlENLQSQVQELDAKVDQASSDAAAAQSRADEAAAKAEQAEAAANAaqqeadeANERA 80

                        90
                ....*....|
gi 490531805 74 DNI-AQSYTK 82
Cdd:NF040598 81 DRMfKKSMRK 90
SlyB COG3133
Outer membrane lipoprotein SlyB [Cell wall/membrane/envelope biogenesis];
1-23 7.49e-03

Outer membrane lipoprotein SlyB [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442367  Cd Length: 152  Bit Score: 32.87  E-value: 7.49e-03
                         10        20
                 ....*....|....*....|...
gi 490531805   1 MNKMLLAAAASSVLLLAGCASGP 23
Cdd:COG3133    1 MKKLLLAAALLAALLLAGCANSS 23
 
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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