UniProt:P0DJM0 inlA

chain
  • signal peptide:1-35
  • chain:36-770
  • propeptide:771-800
checksum 4D1B03A5CF7CCDE3
comment
  • FUNCTION Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells (PubMed:10406800, PubMed:1905979, PubMed:8601315). Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin-2 function as receptors (PubMed:8601315). Mouse cadherin-1 is not a receptor, however mutating a single surface-exposed residue (Glu-172 to Pro in mouse) allows cadherin-1 to act as a receptor for InlA (PubMed:10406800).ACTIVITY REGULATION Bacterial uptake is inhibited by EDTA and by anti-E-cadherin antibodies.SUBUNIT Interacts with host (human) cadherin-1 (CDH1) (PubMed:12526809, PubMed:17540170, PubMed:17715295). The formation of the complex between inlA and cadherin-1 is calcium-dependent (PubMed:12526809). Mutagenesis studies show it is possible to increase the affinity of InlA for CDH1 by rational engineering of InlA residues (PubMed:17715295).INTERACTION In the absence of SrtA in exponential phase some protein is still anchored to the cell wall and a very small amount is secreted while overall protein levels are the same in the srtA mutant; in stationary phase almost no protein accumulates (PubMed:22837151). During exponential growth detected on the cell surface as a series of dots in a helical pattern, it is excluded from the septum; if expression is increased it accumulates at cell poles (PubMed:21725001). The helical pattern of InlA does not overlap with that of InlH, InlJ or Hbp2 (SvpA) (PubMed:21725001). In stationary phase colocalizes with InlH at cell poles and at the septum, the location shift requires SigB (PubMed:21725001).INDUCTION More prevalent in stationary than exponential phase (at protein level) (PubMed:16247833, PubMed:21725001). Levels maybe post-transcriptionally decreased by InlH; disruption of inlH in some strains (EGD-e and EGD-2) leads to increased levels of InlA (at protein level) (PubMed:20176794).DOMAIN Consists of an N-terminal cap, a leucine-rich repeat domain (LRR), and an Ig-like interrepeat domain.DISRUPTION PHENOTYPE Deletion of both inlA and inlB prevents bacterial uptake by human enterocyte-like cell line Caco-2 (PubMed:1905979). Deletion of inlA alone decreases host cell entry; the reduction varies from 98% to none depending on the cell line tested (PubMed:10406800, PubMed:11929538, PubMed:8601315).SIMILARITY Belongs to the internalin family.
created [InstanceEdit:8876503] Orlic-Milacic, Marija, 2016-06-15
crossReference
databaseName UniProt
dbId 8876506
description
  • recommendedName: fullName evidence="16"Internalin A
displayName UniProt:P0DJM0 inlA
geneName
  • inlA
  • lmo0433
identifier P0DJM0
isSequenceChanged false
keyword
  • 3D-structure
  • Cell wall
  • Direct protein sequencing
  • Leucine-rich repeat
  • Peptidoglycan-anchor
  • Reference proteome
  • Repeat
  • Secreted
  • Signal
  • Virulence
modified [InstanceEdit:9917590] Weiser, Joel, 2024-08-09
moleculeType Protein
name
  • inlA
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • INLA_LISMO
  • P25146
  • Q45GD5
  • Q45GD6
  • Q48748
  • Q48749
  • Q48750
  • Q48752
  • Q9EXG2
sequenceLength 800
species [Species:8875364] Listeria monocytogenes serovar 1/2a
stId uniprot:P0DJM0
url http://purl.uniprot.org/uniprot/P0DJM0
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