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There are several matches for 'lipoprotein chaperone'.
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917 matches
showing page 1 of 46
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organism
protein
1)
Escherichia coli K12
lolA -
Lipoprotein
chaperone
; Participates in the translocation of
lipoproteins
from the inner membrane to the outer membrane. Only forms a complex with a
lipoprotein
if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the
lipoprotein
should stay in the inner membrane); the inner membrane retention signal functions at the release step.
[a.k.a. b0891, AAC73977.2,
lipoprotein chaperone
,
Lipoprotein chaperone
]
2)
Homo sapiens
LMF1 - Lipase maturation factor 1; Involved in the maturation of specific proteins in the endoplasmic reticulum. Required for maturation and transport of active
lipoprotein
lipase (LPL) through the secretory pathway. Each LMF1 molecule
chaperones
50 or more molecules of LPL.
[a.k.a. B3KS80, UPI000013FC7D, ENST00000566609]
3)
Homo sapiens
MESD - LRP
chaperone
MESD;
Chaperone
specifically assisting the folding of beta- propeller/EGF modules within the family of low-density
lipoprotein
receptors (LDLRs). Acts as a modulator of the Wnt pathway through
chaperoning
the coreceptors of the canonical Wnt pathway, LRP5 and LRP6, to the plasma membrane. Essential for specification of embryonic polarity and mesoderm induction. Plays an essential role in neuromuscular junction (NMJ) formation by promoting cell-surface expression of LRP4 (By similarity). May regulate phagocytosis of apoptotic retinal pigment epithelium (RPE) cells (By simi [...]
[a.k.a. BAA07640.2, 23184, NP_055969]
4)
Mus musculus
Lmf1 - Lipase maturation factor 1; Involved in the maturation of specific proteins in the endoplasmic reticulum. Required for maturation and transport of active
lipoprotein
lipase (LPL) through the secretory pathway. Each LMF1 molecule
chaperones
50 or more molecules of LPL.
[a.k.a. ENSMUST00000137201.7, NP_083900, ENSMUST00000142264]
5)
Mus musculus
Mesd - LRP
chaperone
MESD;
Chaperone
specifically assisting the folding of beta- propeller/EGF modules within the family of low-density
lipoprotein
receptors (LDLRs). Acts as a modulator of the Wnt pathway through
chaperoning
the coreceptors of the canonical Wnt pathway, LRP5 and LRP6, to the plasma membrane. Essential for specification of embryonic polarity and mesoderm induction. Plays an essential role in neuromuscular junction (NMJ) formation by promoting cell- surface expression of LRP4. May regulate phagocytosis of apoptotic retinal pigment epithelium (RPE) cells. Belongs to the MESD family.
[a.k.a. ENSMUST00000153377, MGI:1891421, Q8CCX7]
6)
Drosophila melanogaster
boca - LDLR
chaperone
boca; Boca (boca) encodes an endoplasmic reticulum protein that is evolutionarily conserved. It is required for the intracellular trafficking of members of the low-density
lipoprotein
family of receptors, including the one encoded by arr. As such, boca mutants are compromised for a number of pathways including Wingless signaling.
[a.k.a. FBgn0004132, boca-PA, AY069840]
7)
Escherichia coli K12
lolD - Outer membrane-specific
lipoprotein
transporter subunit; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed
lipoproteins
, from the inner membrane to the periplasmic
chaperone
, LolA. Responsible for the formation of the LolA-
lipoprotein
complex in an ATP-dependent manner. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature
lipoprotein
) and of LolA.
[a.k.a. b1117, AAC74201.2, P75957]
8)
Escherichia coli K12
yedY - Membrane-anchored, periplasmic TMAO, DMSO reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic
chaperone
SurA and the
lipoprotein
Pal. The catalytic subunit Ms [...]
[a.k.a. b1971, AAC75037.1, MSRP_ECOLI]
9)
Escherichia coli K12
yedZ - Inner membrane heme subunit for periplasmic YedYZ reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic
chaperone
SurA and the
lipoprotein
Pal. MsrQ provides el [...]
[a.k.a. b1972, AAC75038.1, P76343]
10)
Escherichia coli K12
slyA - Global transcriptional regulator; Transcription regulator that can specifically activate or repress expression of target genes. Activates expression of genes such as molecular
chaperones
(groL, groS, dnaK, grpE, and cbpA), proteins involved in acid resistance (hdeA, hdeB, and gadA), the starvation
lipoprotein
slp, virulence protein hlyE/clyA. Represses expression of genes involved in the histidine biosynthetic pathway such as hisA, hisB, hisD, hisF and hisG. Required for the activation of virulence genes; Belongs to the SlyA family.
[a.k.a. b1642, AAC74714.2, DNA-binding transcriptional dual regulator SlyA]
11)
Escherichia coli K12
bamB - BamABCDE complex OM biogenesis
lipoprotein
; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components,
chaperones
and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into t [...]
[a.k.a. b2512, AAC75565.1, 2YMS]
12)
Accumulibacter sp. SK12
AW08_03090 -
Lipoprotein
chaperone
; Participates in the translocation of
lipoproteins
from the inner membrane to the outer membrane. Only forms a complex with a
lipoprotein
if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the
lipoprotein
should stay in the inner membrane).
[a.k.a. EXI65570.1,
lipoprotein chaperone
, A0A011NMC4,
Lipoprotein chaperone
]
13)
Achromobacter arsenitoxydans
lolA -
Lipoprotein
chaperone
; Participates in the translocation of
lipoproteins
from the inner membrane to the outer membrane. Only forms a complex with a
lipoprotein
if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the
lipoprotein
should stay in the inner membrane).
[a.k.a. KYC_03459, EHK67935.1,
lipoprotein chaperone
,
Lipoprotein chaperone
]
14)
Achromobacter piechaudii
lolA -
Lipoprotein
chaperone
; Participates in the translocation of
lipoproteins
from the inner membrane to the outer membrane. Only forms a complex with a
lipoprotein
if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the
lipoprotein
should stay in the inner membrane).
[a.k.a. EJO31822.1, QWC_08106,
lipoprotein chaperone
,
Lipoprotein chaperone
]
15)
Achromobacter sp. ATCC31444
CUI75310.1 -
Lipoprotein
chaperone
.
[a.k.a. ERS370013_01729,
lipoprotein chaperone
, IPR029046,
Lipoprotein chaperone
]
16)
Actinobacillus equuli
lolA -
Lipoprotein
chaperone
; Participates in the translocation of
lipoproteins
from the inner membrane to the outer membrane. Only forms a complex with a
lipoprotein
if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the
lipoprotein
should stay in the inner membrane).
[a.k.a. AIZ79062.1, ACEE_04600,
lipoprotein chaperone
,
Lipoprotein chaperone
]
17)
Advenella kashmirensis WT001
lolA -
Lipoprotein
chaperone
; Participates in the translocation of
lipoproteins
from the inner membrane to the outer membrane. Only forms a complex with a
lipoprotein
if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the
lipoprotein
should stay in the inner membrane).
[a.k.a. AFK63428.1, TKWG_17660,
lipoprotein chaperone
,
Lipoprotein chaperone
]
18)
Afipia felis
CEG10095.1 -
Lipoprotein
chaperone
; Participates in the translocation of
lipoproteins
from the inner membrane to the outer membrane. Only forms a complex with a
lipoprotein
if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the
lipoprotein
should stay in the inner membrane).
[a.k.a. BN961_03529,
lipoprotein chaperone
, A0A090MRT1,
Lipoprotein chaperone
]
19)
Aggregatibacter aphrophilus
lolA -
Lipoprotein
chaperone
; Participates in the translocation of
lipoproteins
from the inner membrane to the outer membrane. Only forms a complex with a
lipoprotein
if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the
lipoprotein
should stay in the inner membrane).
[a.k.a. ADJ80_06210, AKU63375.1,
lipoprotein chaperone
,
Lipoprotein chaperone
]
20)
Aggregatibacter segnis
lolA - Unannotated protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).
[a.k.a. GCA_001059425_00280, WP_005715826.1, NCTC10977_00670,
Lipoprotein chaperone
]
917 matches
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