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


DP00161: Cell division protein zipAFASTA viewXML view

General information
DisProt:DP00161
Name:Cell division protein zipA
Synonym(s):ZIPA_ECOLI
First appeared in release:Release 1.1 (12/01/2003)
UniProt:P77173
UniGene: 
SwissProt: ZIPA_ECOLI
TrEMBL:  
NCBI (GI): 34395999
Source organism:Escherichia coli (strain K12)
Sequence length:328
Percent disordered:45%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MMQDLRLILI IVGAIAIIAL LVHGFWTSRK ERSSMFRDRP LKRMKSKRDD DSYDEDVEDD - 60
EGVGEVRVHR VNHAPANAQE HEAARPSPQH QYQPPYASAQ PRQPVQQPPE AQVPPQHAPH - 120
PAQPVQQPAY QPQPEQPLQQ PVSPQVAPAP QPVHSAPQPA QQAFQPAEPV AAPQPEPVAE - 180
PAPVMDKPKR KEAVIIMNVA AHHGSELNGE LLLNSIQQAG FIFGDMNIYH RHLSPDGSGP - 240
ALFSLANMVK PGTFDPEMKD FTTPGVTIFM QVPSYGDELQ NFKLMLQSAQ HIADEVGGVV - 300
LDDQRRMMTP QKLREYQDII REVKDANA

Region 1: 39-185

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
Name: 
Location:39 - 185
Length:147
Region sequence:

RPLKRMKSKRDDDSYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYAS
AQPRQPVQQPPEAQVPPQHAPHPAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQ
PAQQAFQPAEPVAAPQPEPVAEPAPVM

Modification type:  
PDB:  
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
  1. Rotory shadowing electron microscopy (modeling as a worm-like chain)
References:
  1. Ohashi T, Hale CA, de Boer PA, Erickson HP. "Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain." J Bacteriol. 2002; 184(15): 4313-4315. PubMed: 12107152
Comments:
The EM used in this study is a novel approach to demonstrate an unstructured protein. The unstructured protein is placed between two small globular domains and imaged by EM. Knowing the contour length, one can determine the persistance lengh from the average spacing of the two globular domains. A persistence length of 0.3-0.6 nm is characteristic of an unstructrured protein.

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