UniProt functional annotation for Q9K0U9



	UniProt functional annotation for Q9K0U9

UniProt code: Q9K0U9.

Organism: Neisseria meningitidis serogroup B (strain MC58).

Taxonomy: Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; Neisseria.

Function: Neisseria acquires iron by extracting it from serum transferrin (TF) in its human host. Acts as a TF receptor and is required for TF utilization. Binds both apo- and holo-TF, via the TF C- terminus. {ECO:0000269|PubMed:22327295}.

Subunit: Binds both human apo- and holo-transferrin (TF), via the TF C- terminus. Forms a large complex with TF and TbpB. {ECO:0000269|PubMed:22327295}.

Subcellular location: Cell outer membrane {ECO:0000305|PubMed:22327295}; Multi-pass membrane protein {ECO:0000305|PubMed:22327295}.

Domain: The N-terminal periplasmic domain encodes a plug that inserts into the 22 beta-strand barrel, the extracellular loops extend up to 60 Angstroms away from the outer membrane. Part of the plug (the plug loop, resides 121-139) interacts with transferrin (TF), as does the L3 helix finger in extracellular loop 3 (residues 351-361). When the L3 helix finger inserts into TF it disturbs the conformation of TF and its coordination of iron 2. Electron microscopy suggests that in the TbpA- TbpB-TF complex, TF is captured directly above the loop domain of TbpA in a chamber of about 1000 Angstroms(3) formed by the 3 proteins, where interactions between the proteins serve to abstract iron 2 from TF. {ECO:0000269|PubMed:22327295}.

Miscellaneous: Present in outer membrane vesicle formulations which are used as vaccines in human. {ECO:0000269|PubMed:16645985}.

Miscellaneous: N.meningitidis cells will only bind to human TF, not bovine or porcine TF, explaining at least in part the bacteria's inability to cause infection in non-human hosts. {ECO:0000269|PubMed:2110858}.

Similarity: Belongs to the TonB-dependent receptor family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Neisseria meningitidis serogroup B (strain MC58).
Taxonomy:		Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; Neisseria.



Function:		Neisseria acquires iron by extracting it from serum transferrin (TF) in its human host. Acts as a TF receptor and is required for TF utilization. Binds both apo- and holo-TF, via the TF C- terminus. {ECO:0000269\|PubMed:22327295}.


Subunit:		Binds both human apo- and holo-transferrin (TF), via the TF C- terminus. Forms a large complex with TF and TbpB. {ECO:0000269\|PubMed:22327295}.
Subcellular location:		Cell outer membrane {ECO:0000305\|PubMed:22327295}; Multi-pass membrane protein {ECO:0000305\|PubMed:22327295}.
Domain:		The N-terminal periplasmic domain encodes a plug that inserts into the 22 beta-strand barrel, the extracellular loops extend up to 60 Angstroms away from the outer membrane. Part of the plug (the plug loop, resides 121-139) interacts with transferrin (TF), as does the L3 helix finger in extracellular loop 3 (residues 351-361). When the L3 helix finger inserts into TF it disturbs the conformation of TF and its coordination of iron 2. Electron microscopy suggests that in the TbpA- TbpB-TF complex, TF is captured directly above the loop domain of TbpA in a chamber of about 1000 Angstroms(3) formed by the 3 proteins, where interactions between the proteins serve to abstract iron 2 from TF. {ECO:0000269\|PubMed:22327295}.
Miscellaneous:		Present in outer membrane vesicle formulations which are used as vaccines in human. {ECO:0000269\|PubMed:16645985}.
Miscellaneous:		N.meningitidis cells will only bind to human TF, not bovine or porcine TF, explaining at least in part the bacteria's inability to cause infection in non-human hosts. {ECO:0000269\|PubMed:2110858}.
Similarity:		Belongs to the TonB-dependent receptor family. {ECO:0000305}.