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1.B.1.5.5
PorB (Class 2). The 2.3 Å structure has been determined by x-ray crystallography. There are three putative solute translocation pathways through the channel pore: One pathway transports anions nonselectively, one tranports cations nonselectively, and one facilitates the specific uptake of sugars. Regulated by ATP binding (Tanabe et al., 2010).  Exhibits voltage-dependent closure (Jadhav et al. 2013).

Accession Number:Q51271
Protein Name:Serotype 15 outer membrane protein
Length:331
Molecular Weight:35726.00
Species:Neisseria meningitidis [487]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell outer membrane1 / Multi-pass membrane protein2
Substrate ions, Sugars

Cross database links:

Structure:
3wi4   3wi5     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
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FASTA formatted sequence
1:	MKKSLIALTL AALPVAAMAD VTLYGTIKAG VETSRSVFHQ NGQVTEVTTA TGIVDLGSKI 
61:	GFKGQEDLGN GLKAIWQVEQ KASIAGTDSG WGNRQSFIGL KGGFGKLRVG RLNSVLKDTG 
121:	DINPWDSKSD YLGVNKIAEP EARLISVRYD SPEFAGLSGS VQYALNDNAG RHNSESYHAG 
181:	FNYKNGGFFV QYGGAYKRHH QVQEGLNIEK YQIHRLVSGY DNDALYASVA VQQQDAKLTD 
241:	ASNSHNSQTE VAATLAYRFG NVTPRVSYAH GFKGLVDDAD IGNEYDQVVV GAEYDFSKRT 
301:	SALVSAGWLQ EGKGENKFVA TAASVGLRHK F