proteins similar to periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the periplasmic protein RseB; This family contains uncharacterized proteins similar to the periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639234493 114 TDFI--DYDSKGFVANY----LGKEKIGNVDCFKVELV----KNVN--KTIYYFDANTYMLVREI------NKTDILTYY 175
Cdd:cd16329  102 SDFSyeDLSRSRLLEDYtyklLGEEEVDGRDCYVLELTpkdgADSGysKRVLWVDKDTFLPLKAEyydrsgKLLKTLTFS 181

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 639234493 176 DYRKVGNLLMPFRIESSSQKKEGDYVLLFNKIEVNKVFPNNTF 218
Cdd:cd16329  182 DIKKIGGYWRPTRMEMKDLLTGHKTVLEYSDIKFNVGLPDSLF 224

proteins similar to periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the periplasmic protein RseB; This family contains uncharacterized proteins similar to the periplasmic molecular chaperone LolA, the outer membrane lipoprotein receptor LolB and the 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639234493 114 TDFI--DYDSKGFVANY----LGKEKIGNVDCFKVELV----KNVN--KTIYYFDANTYMLVREI------NKTDILTYY 175
Cdd:cd16329  102 SDFSyeDLSRSRLLEDYtyklLGEEEVDGRDCYVLELTpkdgADSGysKRVLWVDKDTFLPLKAEyydrsgKLLKTLTFS 181

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 639234493 176 DYRKVGNLLMPFRIESSSQKKEGDYVLLFNKIEVNKVFPNNTF 218
Cdd:cd16329  182 DIKKIGGYWRPTRMEMKDLLTGHKTVLEYSDIKFNVGLPDSLF 224