LolA-like protein similar to outer membrane lipoprotein carrier protein LolA, a periplasmic molecular chaperone which binds to outer-membrane specific lipoproteins and transports them from inner membrane to outer membrane (OM) through LolB, a lipoprotein anchored to outer membranes
family containing periplasmic molecular chaperone LolA, the outer membrane lipoprotein ...
3-200
3.17e-87
family containing periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the periplasmic protein RseB; This family contains the periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the N-terminal domain of periplasmic protein RseB, all of which have similar unclosed beta-barrel structures that resemble a baseball glove-like scaffold consisting of an 11-stranded antiparallel sheet. There are five Lol proteins (LolA, LolB, LolC, LolD, and LolE) involved in the sorting and membrane localization of lipoprotein and are highly conserved in Gram-negative bacteria. LolA accepts outer membrane (OM)-specific lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB. It is proposed that the LolA/LolB complex forms a tunnel-like structure, where the hydrophobic insides of LolA and LolB are connected, which enables lipoproteins to transfer from LolA to LolB. RseB exerts a crucial role in modulating the stability of RseA, the transmembrane anti-sigma-factor that is degraded during sigma-E-dependent transcription caused by bacterial envelope stress. Its structural similarity to LolA and LolB suggests that RseA may act as a sensor of periplasmic stress with a dual functionality, detecting mislocalized lipoproteins as well as propagating the signal to induce the sigma-E-response.
The actual alignment was detected with superfamily member TIGR00548:
Pssm-ID: 473147 Cd Length: 202 Bit Score: 255.67 E-value: 3.17e-87
outer membrane lipoprotein LolB; This protein, LolB, is known so far only in the gamma and ...
3-200
3.17e-87
outer membrane lipoprotein LolB; This protein, LolB, is known so far only in the gamma and beta subdivisions of the Proteobacteria. It is a processed, lipid-modified outer membrane protein. It is required in E. coli for insertion of the major outer lipoprotein (Lpp) into the outer membrane. Lpp is transferred to LolB from the carrier protein LolA in the periplasm. Previously, this protein was thought to play in role in 5-aminolevulinic acid synthesis and was designated HemM. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 129639 Cd Length: 202 Bit Score: 255.67 E-value: 3.17e-87
LolB, an outer membrane lipoprotein receptor; This family contains the outer membrane ...
38-200
4.26e-66
LolB, an outer membrane lipoprotein receptor; This family contains the outer membrane lipoprotein receptor, LolB, which catalyzes the last step of lipoprotein transfer from the inner to the outer membrane. There are five Lol proteins (LolA, LolB, LolC, LolD, and LolE) involved in the sorting and membrane localization of lipoprotein and are highly conserved in Gram-negative bacteria. LolA transports lipoproteins through the periplasm to LolB, which then localizes them to outer membranes; the protruding loop of LolB has been shown to be essential for the localization of lipoproteins in the anchoring of bacterial triacylated proteins to the outer membrane.
Pssm-ID: 319984 Cd Length: 163 Bit Score: 200.53 E-value: 4.26e-66
outer membrane lipoprotein LolB; This protein, LolB, is known so far only in the gamma and ...
3-200
3.17e-87
outer membrane lipoprotein LolB; This protein, LolB, is known so far only in the gamma and beta subdivisions of the Proteobacteria. It is a processed, lipid-modified outer membrane protein. It is required in E. coli for insertion of the major outer lipoprotein (Lpp) into the outer membrane. Lpp is transferred to LolB from the carrier protein LolA in the periplasm. Previously, this protein was thought to play in role in 5-aminolevulinic acid synthesis and was designated HemM. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 129639 Cd Length: 202 Bit Score: 255.67 E-value: 3.17e-87
LolB, an outer membrane lipoprotein receptor; This family contains the outer membrane ...
38-200
4.26e-66
LolB, an outer membrane lipoprotein receptor; This family contains the outer membrane lipoprotein receptor, LolB, which catalyzes the last step of lipoprotein transfer from the inner to the outer membrane. There are five Lol proteins (LolA, LolB, LolC, LolD, and LolE) involved in the sorting and membrane localization of lipoprotein and are highly conserved in Gram-negative bacteria. LolA transports lipoproteins through the periplasm to LolB, which then localizes them to outer membranes; the protruding loop of LolB has been shown to be essential for the localization of lipoproteins in the anchoring of bacterial triacylated proteins to the outer membrane.
Pssm-ID: 319984 Cd Length: 163 Bit Score: 200.53 E-value: 4.26e-66
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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