Annotations for this protein have been verified by the authors of the corresponding papers



DP00205: Metal-binding protein smbPFASTA viewXML view

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
         |          |          |          |          |          |
MKTTLIKVIA ASVTALFLSM QVYASGHTAH VDEAVKHAEE AVAHGKEGHT DQLLEHAKES - 60
LTHAKAASEA GGNTHVGHGI KHLEDAIKHG EEGHVGVATK HAQEAIEHLR ASEHKSH



Functional narrative    

SmbP play a role in cellular copper management in the ammonia-oxidizing bacterium Nitrosomonas europaea. SmbP binds bivalent metal cations, especially copper.

Region 1: 1-117

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: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:
  1. Size exclusion/gel filtration chromatography (pH: 7.5; )

  2. Circular dichroism (CD) spectroscopy, far-UV (pH: 7.5; )

References:
  1. 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:
 



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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