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1.B.1.5.4
PorB porin (Song et al. 1998; Tanabe et al., 2010). 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 (Kattner et al. 2012). Regulated by ATP binding (Tanabe et al., 2010).  Exhibits voltage-dependent closure (Jadhav et al. 2013). Its unique solute transport activity with size exclusion limit has been described (Kattner et al. 2015).

Accession Number:P30687
Protein Name:PorB
Length:331
Molecular Weight:35741.00
Species:Neisseria meningitidis (serogroup B) [491]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell outer membrane1 / Multi-pass membrane protein2
Substrate ions, Sugars

Cross database links:

Pfam: PF00267   

Gene Ontology

GO:0009279 C:cell outer membrane
GO:0005886 C:plasma membrane
GO:0046930 C:pore complex
GO:0005215 F:transporter activity
GO:0006811 P:ion transport

References (1)

[1] “Sequence analysis and relationships between meningococcal class 3 serotype proteins and other porins from pathogenic and non-pathogenic Neisseria species.”  Ward M.J.et.al.   1330818

External Searches:

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  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MKKSLIALTL AALPVAAMAD VTLYGTIKAG VETSRSVAHN GAQAASVETG TGIVDLGSKI 
61:	GFKGQEDLGN GLKAIWQVEQ KASIAGTDSG WGNRQSFIGL KGGFGKLRVG RLNSVLKDTG 
121:	DINPWDSKSD YLGVNKIAEP EARLISVRYD SPEFAGLSGS VQYALNDNAG RHNSESYHAG 
181:	FNYKNGGFFV QYGGAYKRHH QVQENVNIEK YQIHRLVSGY DNDALYASVA VQQQDAKLVE 
241:	ENYSHNSQTE VAATLAYRFG NVTPRVSYAH GFKGSFDATN YNNDYDQVVV GAEYDFSKRT 
301:	SALVSAGWLQ EGKGESKFVS TAGGVGLRHK F