|znuB||Involved in the high-affinity zinc uptake transport system (261 aa)|| |
Predicted Functional Partners:
Involved in the high-affinity zinc uptake transport system
| || || ||0.999
Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system.
Mediates zinc uptake. May also transport other divalent cations such as copper and cadmium ions
| || || || || || ||0.891
May function as a periplasmic zinc chaperone or mediate direct transport of zinc from the periplasm to the cytoplasm under zinc-limited conditions. Binds zinc with high affinity, and can also bind cadmium, mercury or nickel. Preferentially binds Zn(2+) over Cd(2+). Contains one high affinity metal binding site, and can bind additional metal ions at other sites
| || || || || ||0.864
Belongs to the Mg-chelatase subunits D/I family. ComM subfamily
| || || || || ||0.787
In the presence of manganese, represses expression of mntH and mntS. Up-regulates expression of mntP.
| || || || || || ||0.738
A murein DD-endopeptidase with specificity for D-Ala-meso- diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Partially suppresses an mepS disruption mutant
| || || || || || ||0.703
Confers resistance to zinc, cadmium and lead (PubMed:9405611, PubMed:9364914, PubMed:9830000, PubMed:10660539, PubMed:17326661). Couples the hydrolysis of ATP with the export of zinc, cadmium or lead, with highest activity when the metals are present as metal-thiolate complexes . Can also bind nickel, copper, cobalt and mercury (PubMed:10660539, PubMed:17326661). ECO:0000269|PubMed:17326661, ECO:0000269|PubMed:9364914,
| || || || || || ||0.672
Acts as a negative controlling element, employing Zn(2+) as a cofactor to bind the operator of the repressed genes (znuACB)
| || || || || ||0.661
Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. Can probably also catalyze the transfer of myristate to Kdo(2)-(palmitoleoyl)-lipid IV(A) to form the cold-adapted Kdo(2)-lipid A. In vitro, can acylate Kdo(2)-lipid IV(A), but acylation of (KDO)2- (lauroyl)-lipid IV(A) is about 100 times faster. In vitro, can use lauroyl-ACP but displays a slight kinetic preference for myristoyl-ACP.
| || || || || ||0.570