| General information | | DisProt: | DP00121 | | Name: | Protein L precursor | | Synonym(s): | Q51912_PEPMA
| | First appeared in release: | Release 2.0 (02/14/2005) | | UniProt: | Q51912 | | UniGene: | | | SwissProt: | Q51912_PEPMA | | TrEMBL: | | | NCBI (GI): | 75504278 | | Source organism: | Peptostreptococcus magnus (Finegoldia magna) | | Sequence length: | 719 | | Percent disordered: | 11% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MAALAGAIVV TGGVGSYAAD EPIDLEKLEE KRDKENVGNL PKFDNEVKDG SENPMAKYPD - 60
FDDEASTRFE TENNEFEEKK VVSDNFFDQS EHPFVENKEE TPETPETDSE EEVTIKANLI - 120
FANGSTQTAE FKGTFEKATS EAYAYADTLK KDNGEYTVDV ADKGYTLNIK FAGKEKTPEE - 180
PKEEVTIKAN LIYADGKTQT AEFKGTFEEA TAEAYRYADA LKKDNGEYTV DVADKGYTLN - 240
IKFAGKEKTP EEPKEEVTIK ANLIYADGKT QTAEFKGTFE EATAEAYRYA DLLAKENGKY - 300
TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FAEATAEAYR - 360
YADLLAKENG KYTADLEDGG YTINIRFAGK KVDEKPEEKE QVTIKENIYF EDGTVQTATF - 420
KGTFAEATAE AYRYADLLSK EHGKYTADLE DGGYTINIRF AGKEEPEETP EKPEVQDGYA - 480
SYEEAEAAAK EALKNDDVNK SYTIRQGADG RYYYVLSPVE AEEEKPEAQN GYATYEEAEA - 540
AAKKALENDP INKSYSIRQG ADGRYYYVLS PVEAETPEKP VEPSEPSTPD VPSNPSNPST - 600
PDVPSTPDVP SNPSTPEVPS NPSTPGNEEK PGNEQKPGNE QKPGNEQKPG NEQKPGNEQK - 660
PDQPSKPEKE ENGKGGVDSP KKKEKAALPK AGSEAEILTL AAASLSSVAG AFISLKKRK
|
| Functional narrative |
Protein L is a cell surface antigen utilized by bacteria to gain access to host cells. It is attached by an amide bond to the cell wall peptidoglycan. The presence of Protein L on the surface of bacteria can indicate virulence. Several disordered regions are involved in protein-protein interactions, however, functions of these disordered regions either have not been determined or do not occur in the full native structure of this protein.
|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered - Extended | | Name: | | | Location: | 1 - 17 | | Length: | 17 | | Region sequence: |
MAALAGAIVVTGGVGSY | | Modification type: | Engineered
Fragment
| | PDB: | 2PTL:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR)
| References:
- Wikstroem M, Sjoebring U, Kastern W, Bjoerck L. "Proton nuclear magnetic resonance sequential assignments and secondary structure of an immunoglobulin light chain-binding domain of protein L." 1993; 32: 3381.
| Comments:
|
| Region 2 | | Type: | Disordered - Extended | | Name: | | | Location: | 95 - 115 | | Length: | 21 | | Region sequence: |
VENKEETPETPETDSEEEVTI | | Modification type: | Engineered
Fragment
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (pH: 4.1; )
| References:
- Ramirez-Alvarado M, Serrano L, Blanco FJ. "Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold." Protein Sci. 1997; 6(1): 162-174. PubMed: 9007989
| Comments:
|
| Region 3 | | Type: | Disordered - Extended | | Name: | | | Location: | 114 - 123 | | Length: | 10 | | Region sequence: |
TIKANLIFAN | | Modification type: | Engineered
Fragment
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (TFE)
| References:
- Ramirez-Alvarado M, Serrano L, Blanco FJ. "Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold." Protein Sci. 1997; 6(1): 162-174. PubMed: 9007989
| Comments:
|
| Region 4 | | Type: | Disordered - Extended | | Name: | | | Location: | 114 - 138 | | Length: | 25 | | Region sequence: |
TIKANLIFANGSTQTAEFKGTFEKA | | Modification type: | Engineered
Fragment
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV
- Nuclear magnetic resonance (NMR)
| References:
- Ramirez-Alvarado M, Serrano L, Blanco FJ. "Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold." Protein Sci. 1997; 6(1): 162-174. PubMed: 9007989
| Comments:
|
| Region 5 | | Type: | Disordered - Extended | | Name: | | | Location: | 135 - 138 | | Length: | 4 | | Region sequence: |
FEKA | | Modification type: | Engineered
Fragment
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (TFE)
| References:
- Ramirez-Alvarado M, Serrano L, Blanco FJ. "Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold." Protein Sci. 1997; 6(1): 162-174. PubMed: 9007989
| Comments:
|
| Region 6 | | Type: | Disordered - Extended | | Name: | | | Location: | 136 - 155 | | Length: | 20 | | Region sequence: |
EKATSEAYAYADTLKKDNGE | | Modification type: | Engineered
Fragment
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV
- Nuclear magnetic resonance (NMR) (295 K; )
| References:
- Ramirez-Alvarado M, Serrano L, Blanco FJ. "Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold." Protein Sci. 1997; 6(1): 162-174. PubMed: 9007989
| Comments:
|
| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|
