Description
Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
Family
Belongs to the GlnE family.
Species
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
Sequence
MKNAFLKTQLLPLRPLDESGSQWLKDITEQARKENLESLVSSLSNQGKQINFLNAVMTLSPFLREVLIANPSYLSPLLYVDIETRLSEIIEDITLIDKNKSIHETTLMAALRRKKREAHVLIALADLGGVFTYEISCAWLTRLGEAALGVALRFLLREAHDHGKINLSNREDPEKDCGLIILGMGKFGAGELNYSSDIDLIVFIDEMSPHVGNLSESIDVFSKMVRRLIRIIQERTAEGYVFRLDFRLRPDPGSTPLALPVRTALRYYEGRGQNWERAAMIKARPVAGDKSAGFNFLKELFPYVWRKYLDYAAIADIHSIKRQIHAYKNYDQISAYGHNIKLGRGGIREIEFFVQTQQLIAGGRFPQLRGRQTVAMLAELHRLGWISEKTRDSLVKSYAFLRNVEHRIQMLADEQTHILPIDVSQFTSVAYLMGYQETNSFICDLLKTLQVVEKHYAALFENEQELGLEIGNLVFTGEEDDPETLITLRRLGFERASDICRIMRTLHCGRYKSTQSAEARERLTELTPALLKAFGATKRADEVMLRFDSFLQGLPSGIQLFSLLQSNPSLLDMLVLIMGAAPRLAEIITHKPHVFDGMLDPTIFSELPTKTYLKNRLEYFLEGVISYEEILDHLRVFADEQRFLIGIRILNGAITGKKAGFAFTALADLIIAKTFATVQEEFSRLHGNIKGGRVGILGMGKLGSCELTAGSDVDLILLYEHDEDAEISDGGKPLYIFQYYTRLTQRLVAALSTLTSQGILYAVDLRLRPLGNKGPVAVSFEFFRKYYRKEAWIWEHLALTRARGIAGDLDFLQKLENEVYEIIAFSRNKKDVIKAVCEMHVLIGKGKPPENRWDLKRMPGGIMHLEFIAQFALITHVIVFQIGATTADILTQLPNSFLNQSFISDLHHAYGLYTNLSQIIRLCLNDALDLNNMPPGLSDLLLSSVGEPDLLRVEKLIEETGQLVYSIFKQVMKY
Simulated SDS-PAGE

(Note: Representative image - actual molecular weight may vary depending on tag type and expression method)
Safety
Upon ordering, we will perform rigorous biosecurity and export control screening to ensure that order fulfillment is consistent with all legal and regulatory guidance.
Protein synthesis service