LolA family 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
LolA, a periplasmic chaperone; This family contains periplasmic molecular chaperone LolA which ...
97-220
1.38e-08
LolA, a periplasmic chaperone; This family contains periplasmic molecular chaperone LolA 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. 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 OM-specific lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB. Studies have shown that hydrophobic surface patches large enough to accommodate acyl chains of the OM lipoproteins and the structural flexibility of LolA are important factors for its role as a periplasmic chaperone.
Pssm-ID: 319983 Cd Length: 166 Bit Score: 53.60 E-value: 1.38e-08
LolA, a periplasmic chaperone; This family contains periplasmic molecular chaperone LolA which ...
97-220
1.38e-08
LolA, a periplasmic chaperone; This family contains periplasmic molecular chaperone LolA 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. 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 OM-specific lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB. Studies have shown that hydrophobic surface patches large enough to accommodate acyl chains of the OM lipoproteins and the structural flexibility of LolA are important factors for its role as a periplasmic chaperone.
Pssm-ID: 319983 Cd Length: 166 Bit Score: 53.60 E-value: 1.38e-08
RseB, a sensor in periplasmic stress; This family contains the periplasmic protein RseB (also ...
181-239
1.77e-05
RseB, a sensor in periplasmic stress; This family contains the periplasmic protein RseB (also known as MucB or Mucb/RseB) which 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. RseB binds to RseA and inhibits its sequential cleavage, thereby functioning as a negative modulator of this response. The protein is composed of two domains, the larger N-terminal domain resembling an unclosed beta-barrel that is remarkably similar structurally to LolA and LolB, proteins capable of binding the lipid anchor of lipoproteins, suggesting that RseA acts 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.
Pssm-ID: 319985 Cd Length: 166 Bit Score: 44.48 E-value: 1.77e-05
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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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