UniProt functional annotation for P0DJM0



	UniProt functional annotation for P0DJM0

UniProt code: P0DJM0.

Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).

Taxonomy: Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.

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:1905979, PubMed:8601315, PubMed:10406800). 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). {ECO:0000269|PubMed:10406800, ECO:0000269|PubMed:1905979, ECO:0000269|PubMed:8601315}.

Activity regulation: Bacterial uptake is inhibited by EDTA and by anti- E-cadherin antibodies. {ECO:0000269|PubMed:8601315}.

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). {ECO:0000269|PubMed:12526809, ECO:0000269|PubMed:17540170, ECO:0000269|PubMed:17715295}.

Subcellular location: Secreted, cell wall {ECO:0000255|PROSITE- ProRule:PRU00477, ECO:0000269|PubMed:10736172, ECO:0000269|PubMed:11929538, ECO:0000269|PubMed:20176794, ECO:0000269|PubMed:21725001, ECO:0000269|PubMed:22837151}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:10736172, ECO:0000269|PubMed:11929538}. Secreted {ECO:0000269|PubMed:11854224, ECO:0000269|PubMed:20176794}. Note=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). {ECO:0000269|PubMed:21725001, ECO:0000269|PubMed:22837151}.

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). {ECO:0000269|PubMed:16247833, ECO:0000269|PubMed:20176794, ECO:0000269|PubMed:21725001}.

Domain: Consists of an N-terminal cap, a leucine-rich repeat domain (LRR), and an Ig-like interrepeat domain. {ECO:0000269|PubMed:12526809, ECO:0000269|PubMed:17540170, ECO:0000269|PubMed:17715295}.

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:11929538, PubMed:8601315, PubMed:10406800). {ECO:0000269|PubMed:10406800, ECO:0000269|PubMed:11929538, ECO:0000269|PubMed:1905979, ECO:0000269|PubMed:8601315}.

Similarity: Belongs to the internalin family. {ECO:0000305}.

Sequence caution: Sequence=AAA25289.1; Type=Frameshift; Evidence={ECO:0000305|PubMed:7934917};

Annotations taken from UniProtKB at the EBI.


Organism:		Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
Taxonomy:		Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.



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:1905979, PubMed:8601315, PubMed:10406800). 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). {ECO:0000269\|PubMed:10406800, ECO:0000269\|PubMed:1905979, ECO:0000269\|PubMed:8601315}.


Activity regulation:		Bacterial uptake is inhibited by EDTA and by anti- E-cadherin antibodies. {ECO:0000269\|PubMed:8601315}.
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). {ECO:0000269\|PubMed:12526809, ECO:0000269\|PubMed:17540170, ECO:0000269\|PubMed:17715295}.
Subcellular location:		Secreted, cell wall {ECO:0000255\|PROSITE- ProRule:PRU00477, ECO:0000269\|PubMed:10736172, ECO:0000269\|PubMed:11929538, ECO:0000269\|PubMed:20176794, ECO:0000269\|PubMed:21725001, ECO:0000269\|PubMed:22837151}; Peptidoglycan-anchor {ECO:0000255\|PROSITE-ProRule:PRU00477, ECO:0000269\|PubMed:10736172, ECO:0000269\|PubMed:11929538}. Secreted {ECO:0000269\|PubMed:11854224, ECO:0000269\|PubMed:20176794}. Note=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). {ECO:0000269\|PubMed:21725001, ECO:0000269\|PubMed:22837151}.
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). {ECO:0000269\|PubMed:16247833, ECO:0000269\|PubMed:20176794, ECO:0000269\|PubMed:21725001}.
Domain:		Consists of an N-terminal cap, a leucine-rich repeat domain (LRR), and an Ig-like interrepeat domain. {ECO:0000269\|PubMed:12526809, ECO:0000269\|PubMed:17540170, ECO:0000269\|PubMed:17715295}.
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:11929538, PubMed:8601315, PubMed:10406800). {ECO:0000269\|PubMed:10406800, ECO:0000269\|PubMed:11929538, ECO:0000269\|PubMed:1905979, ECO:0000269\|PubMed:8601315}.
Similarity:		Belongs to the internalin family. {ECO:0000305}.
Sequence caution:		Sequence=AAA25289.1; Type=Frameshift; Evidence={ECO:0000305\|PubMed:7934917};