| General information | | DisProt: | DP00205 | | Name: | Metal-binding protein smbP | | Synonym(s): | SMBP_NITEU
| | First appeared in release: | Release 2.1 (03/14/2005) | | UniProt: | Q82S91 | | UniGene: | | | SwissProt: | SMBP_NITEU | | TrEMBL: | | | NCBI (GI): | 75539977 | | Source organism: | Nitrosomonas europaea | | Sequence length: | 117 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MKTTLIKVIA ASVTALFLSM QVYASGHTAH VDEAVKHAEE AVAHGKEGHT DQLLEHAKES - 60
LTHAKAASEA GGNTHVGHGI KHLEDAIKHG EEGHVGVATK HAQEAIEHLR ASEHKSH
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| Functional narrative |
SmbP play a role in cellular copper management in the ammonia-oxidizing bacterium Nitrosomonas europaea. SmbP binds bivalent metal cations, especially copper.
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| 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.
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| Region 1 | | Type: | Disordered - Extended | | Name: | Small metal binding protein | | Location: | 1 - 117 | | Length: | 117 | | Region sequence: |
MKTTLIKVIAASVTALFLSMQVYASGHTAHVDEAVKHAEEAVAHGKEGHTDQLLEHAKES
LTHAKAASEAGGNTHVGHGIKHLEDAIKHGEEGHVGVATKHAQEAIEHLRASEHKSH | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Metal sponge
| | Functional subclasses: | Metal binding
| Detection methods:
- Size exclusion/gel filtration chromatography (pH: 7.5; )
- Circular dichroism (CD) spectroscopy, far-UV (pH: 7.5; )
| References:
- Barney BM, LoBrutto R, Francisco WA. "Characterization of a small metal binding protein from Nitrosomonas europaea." Biochemistry. 2004; 43(35): 11206-13. PubMed: 15366930
| Comments:
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| Comments |
SmbP is characterized by an unusually high number of histidine residues (17%). The apoprotein has negligible absorbance between 260 and 280 nm resulting from the lack of tryptophan, tyrosine, and phenylalanine residues. The protein also does not contain any methionine or cysteine residues. Besides histidine, the protein is primarily an assembly of alanine (16%), glutamate (14%), glycine (11%), and lysine (9%), accounting for 67% of the amino acid composition. The percentage of nonpolar amino acids is also very low, although a nonpolar residue is the predominant amino acid for the second position of the seven-unit repeat and likely contributes to the stabilization of a hydrophobic core.
This unique protein is distinguished by 10 sequential repeats of a seven amino acid motif characterized by an absolutely conserved histidine residue in the fourth position and conserved residues at each of the other six positions. Extensive searches of the current databases did not identify any proteins with significant homology. The protein, as isolated from N. europaea, had approximately one copper atom bound per protein molecule.
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