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|---|---|
| Accession Number: | P61316 |
| Protein Name: | LolA |
| Length: | 203 |
| Molecular Weight: | 22497.00 |
| Species: | Escherichia coli [83333] |
| Number of TMSs: | 1 |
| Location1 / Topology2 / Orientation3: | Periplasm1 |
| Substrate | lipoprotein |
Cross database links:
| DIP: | DIP-35675N |
|---|---|
| RefSeq: | AP_001521.1 NP_415411.2 |
| Entrez Gene ID: | 948989 |
| Pfam: | PF03548 |
| BioCyc: | EcoCyc:G6465-MONOMER ECOL168927:B0891-MONOMER |
| KEGG: | ecj:JW0874 eco:b0891 |
Gene Ontology
GO:0030288
C:outer membrane-bounded periplasmic space
GO:0005515
F:protein binding
GO:0008565
F:protein transporter activity
GO:0042953
P:lipoprotein transport
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References (13)[1] “A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane.” Matsuyama S.et.al. 7628437 [2] “A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.” Oshima T.et.al. 8905232 [3] “The complete genome sequence of Escherichia coli K-12.” Blattner F.R.et.al. 9278503 [4] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.” Hayashi K.et.al. 16738553 [5] “Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.” Link A.J.et.al. 9298646 [6] “Characterization of the RcsC->YojN->RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli.” Chen M.H.et.al. 11758943 [7] “Lipoprotein sorting signals evaluated as the LolA-dependent release of lipoproteins from the cytoplasmic membrane of Escherichia coli.” Terada M.et.al. 11592971 [8] “Elucidation of the function of lipoprotein-sorting signals that determine membrane localization.” Masuda K.et.al. 12032293 [9] “Aminoacylation of the N-terminal cysteine is essential for Lol-dependent release of lipoproteins from membranes but does not depend on lipoprotein sorting signals.” Fukuda A.et.al. 12198129 [10] “Mutant of LolA, a lipoprotein-specific molecular chaperone of Escherichia coli, defective in the transfer of lipoproteins to LolB.” Miyamoto A.et.al. 11587539 [11] “Dominant negative mutant of a lipoprotein-specific molecular chaperone, LolA, tightly associates with LolCDE.” Miyamoto A.et.al. 12297303 [12] “A practical phasing procedure using the MAD method without the aid of XAFS measurements: successful solution in the structure determination of the outer-membrane lipoprotein carrier LolA.” Takeda K.et.al. 12876347 [13] “Crystal structures of bacterial lipoprotein localization factors, LolA and LolB.” Takeda K.et.al. 12839983
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| Structure: | |
External Searches:
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Analyze:
| Predict TMSs (Predict number of transmembrane segments) | ||||
| FASTA formatted sequence |
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1: MKKIAITCAL LSSLVASSVW ADAASDLKSR LDKVSSFHAS FTQKVTDGSG AAVQEGQGDL 61: WVKRPNLFNW HMTQPDESIL VSDGKTLWFY NPFVEQATAT WLKDATGNTP FMLIARNQSS 121: DWQQYNIKQN GDDFVLTPKA SNGNLKQFTI NVGRDGTIHQ FSAVEQDDQR SSYQLKSQQN 181: GAVDAAKFTF TPPQGVTVDD QRK