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Entry version 148 (17 Jun 2020)
Sequence version 1 (01 Jan 1990)
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Protein

Listeriolysin O

Gene

hly

Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

A cholesterol-dependent pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome-independent degradation of UBE2I (the SUMO-conjugating enzyme UBC9) and a proteasome-dependent degradation of some sumoylated proteins. Finally, is necessary and sufficient for spacious Listeria-containing phagosomes (SLAPs) formation, suggesting a role for listeriolysin O in promoting L.monocytogenes replication in vacuoles, leading to persistent infection. Recognized by serum from healthy humans exposed to L.monocytogenes as well from patients who have recovered from listeriosis (PubMed:9284184).8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activity of listeriolysin O is regulated on multiple levels. It should be high in the phagosome, thereby allowing escape of the bacteria from the phagosomal compartment. Then, once inside the host cytosol, the activity must be controlled to prevent lysis of the host plasma membrane and loss of the intracellular environment. Multiple regulatory mechanisms include translational repression, which is required to minimize levels of listeriolysin O in the host cytosol. In addition, cytolytic activity is pH-dependent. Activity is high in the acidic environment of the phagosome and is turned off in the neutral pH of the cytosol. Listeriolysin O is also ubiquitinated and rapidly degraded by host proteasome in cytosol. The lytic activity is activated by reducing agents and suppressed by oxidation. Also inhibited by very low amounts of cholesterol.4 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 5.5. Cytolytic activity is undetectable at pH 7.0.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionToxin
Biological processCytolysis, Hemolysis, Virulence
LigandLipid-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
LMON169963:LMO0202-MONOMER

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.C.12.1.7 the thiol-activated cholesterol-dependent cytolysin (cdc) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Listeriolysin O1 Publication
Alternative name(s):
LLO
Thiol-activated cytolysin
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:hly
Synonyms:hlyA, lisA
Ordered Locus Names:lmo0202
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri169963 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000817 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei214 – 227Beta strandedBy similarityAdd BLAST14
Transmembranei234 – 243Beta strandedBy similarity10
Transmembranei312 – 321Beta strandedBy similarity10
Transmembranei329 – 341Beta strandedBy similarityAdd BLAST13

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi38 – 52Missing : 2.5-fold increase in hemolytic activity. 1 PublicationAdd BLAST15
Mutagenesisi40A → W: 2.5-fold increase in hemolytic activity. 1 Publication1
Mutagenesisi44S → A: 1500-fold decrease in virulence. 1 Publication1
Mutagenesisi44S → D or E: 2-fold increase in hemolytic activity. 1 Publication1
Mutagenesisi49P → A: Does not affect secretion and hemolytic activity. No defect in phagosomal escape. Shows a clear attenuation in virulence. 1 Publication1
Mutagenesisi50K → A: Does not affect secretion and hemolytic activity. Slight decrease in phagosomal escape. Shows a clear attenuation in virulence. 1 Publication1
Mutagenesisi52P → A: Does not affect secretion and hemolytic activity. Slight decrease in phagosomal escape. Shows a clear attenuation in virulence. 1 Publication1
Mutagenesisi175K → E: Loss of hemolytic activity. 1 Publication1
Mutagenesisi176S → W: Loss of hemolytic activity. 1 Publication1
Mutagenesisi230N → W: 50% hemolytic activity. 1 Publication1
Mutagenesisi262E → K: Loss of hemolytic activity. 1 Publication1
Mutagenesisi262E → W: No change in hemolytic activity. 1 Publication1
Mutagenesisi394D → W: 3-fold increase in hemolytic activity. 1 Publication1
Mutagenesisi461L → T: 10-fold increase in hemolytic activity at neutral pH, but 100-fold decrease in virulence. 1 Publication1
Mutagenesisi484C → A: 25% decrease in hemolytic activity, but still able to stimulate MAP kinase tyrosine phosphorylation in host cells. Does not affect membrane-binding capacity. 2 Publications1
Mutagenesisi484C → S: 80% decrease in hemolytic activity, but still able to stimulate MAP kinase tyrosine phosphorylation in host cells. Does not affect membrane-binding capacity. 2 Publications1
Mutagenesisi488A → F: Decreases toxicity by about 40%, decreases cholesterol binding by 25%. 1 Publication1
Mutagenesisi491W → A: 95% decrease in hemolytic activity and no stimulation of MAP kinase activity. Does not affect membrane-binding capacity. 2 Publications1
Mutagenesisi492W → A: 99.9% decrease in hemolytic activity and no stimulation of MAP kinase activity. Does not affect membrane-binding capacity. 2 Publications1

Miscellaneous databases

Pathogen-Host Interaction database

More...
PHI-basei
PHI:6618
PHI:7897

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24Sequence analysisAdd BLAST24
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003410225 – 529Listeriolysin OAdd BLAST505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei44Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated. Phosphorylation does not appear to be required for ubiquitination or degradation.1 Publication
Ubiquitinated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P13128

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P13128

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homooligomeric pore complex of 35-50 subunits; when inserted in the host membrane.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P13128
With#Exp.IntAct
itself4EBI-6407357,EBI-6407357

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P13128, 1 interactor

Molecular INTeraction database

More...
MINTi
P13128

STRING: functional protein association networks

More...
STRINGi
169963.lmo0202

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P13128

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi483 – 493Conserved undecapeptideCuratedAdd BLAST11
Motifi515 – 516Cholesterol bindingBy similarity2

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal region is not required for secretion and hemolytic activity, but is involved in phagosomal escape of bacteria in infected cells and is critical for bacterial virulence. This region contains a PEST-like sequence, which does not mediate proteasomal degradation, but controls listeriolysin O production in the cytosol.3 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105E5P Bacteria
ENOG410XQPX LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_026912_0_0_9

KEGG Orthology (KO)

More...
KOi
K11031

Identification of Orthologs from Complete Genome Data

More...
OMAi
NDRTYPG

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.1430, 1 hit
3.90.840.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR035390 Thiol_cytolys_C
IPR038700 Thiol_cytolys_C_sf
IPR001869 Thiol_cytolysin
IPR036363 Thiol_cytolysin_ab_sf
IPR036359 Thiol_cytolysin_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17440 Thiol_cytolys_C, 1 hit
PF01289 Thiol_cytolysin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01400 TACYTOLYSIN

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56978 SSF56978, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00481 THIOL_CYTOLYSINS, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P13128-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKIMLVFIT LILVSLPIAQ QTEAKDASAF NKENSISSMA PPASPPASPK
60 70 80 90 100
TPIEKKHADE IDKYIQGLDY NKNNVLVYHG DAVTNVPPRK GYKDGNEYIV
110 120 130 140 150
VEKKKKSINQ NNADIQVVNA ISSLTYPGAL VKANSELVEN QPDVLPVKRD
160 170 180 190 200
SLTLSIDLPG MTNQDNKIVV KNATKSNVNN AVNTLVERWN EKYAQAYPNV
210 220 230 240 250
SAKIDYDDEM AYSESQLIAK FGTAFKAVNN SLNVNFGAIS EGKMQEEVIS
260 270 280 290 300
FKQIYYNVNV NEPTRPSRFF GKAVTKEQLQ ALGVNAENPP AYISSVAYGR
310 320 330 340 350
QVYLKLSTNS HSTKVKAAFD AAVSGKSVSG DVELTNIIKN SSFKAVIYGG
360 370 380 390 400
SAKDEVQIID GNLGDLRDIL KKGATFNRET PGVPIAYTTN FLKDNELAVI
410 420 430 440 450
KNNSEYIETT SKAYTDGKIN IDHSGGYVAQ FNISWDEVNY DPEGNEIVQH
460 470 480 490 500
KNWSENNKSK LAHFTSSIYL PGNARNINVY AKECTGLAWE WWRTVIDDRN
510 520
LPLVKNRNIS IWGTTLYPKY SNKVDNPIE
Length:529
Mass (Da):58,688
Last modified:January 1, 1990 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i83B6B0C11C033FB1
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA69528 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence AAA69531 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti35S → L in strain: F4233 / Serotype 1/2b, F5782 / Serotype 4b, F6789 / Serotype 1/2b and 12067. 1
Natural varianti438V → I in strain: F4233 / Serotype 1/2b, F5782 / Serotype 4b, F6789 / Serotype 1/2b and 12067. 1
Natural varianti523K → S in strain: F4233 / Serotype 1/2b, F5782 / Serotype 4b, F6789 / Serotype 1/2b and 12067. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X15127 Genomic DNA Translation: CAA33223.1
M24199 Unassigned DNA Translation: AAA03018.1
X60035 Genomic DNA Translation: CAA42639.1
U25446 Genomic DNA Translation: AAA69528.1 Different initiation.
U25449 Genomic DNA Translation: AAA69531.1 Different initiation.
U25452 Genomic DNA Translation: AAA69534.1
AL591974 Genomic DNA Translation: CAD00729.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A43505
AC1100
S24231

NCBI Reference Sequences

More...
RefSeqi
NP_463733.1, NC_003210.1
WP_003722731.1, NC_003210.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAD00729; CAD00729; CAD00729

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
39647307
987033

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
lmo:lmo0202

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|169963.11.peg.207

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15127 Genomic DNA Translation: CAA33223.1
M24199 Unassigned DNA Translation: AAA03018.1
X60035 Genomic DNA Translation: CAA42639.1
U25446 Genomic DNA Translation: AAA69528.1 Different initiation.
U25449 Genomic DNA Translation: AAA69531.1 Different initiation.
U25452 Genomic DNA Translation: AAA69534.1
AL591974 Genomic DNA Translation: CAD00729.1
PIRiA43505
AC1100
S24231
RefSeqiNP_463733.1, NC_003210.1
WP_003722731.1, NC_003210.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CDBX-ray2.15A39-526[»]
SMRiP13128
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP13128, 1 interactor
MINTiP13128
STRINGi169963.lmo0202

Protein family/group databases

TCDBi1.C.12.1.7 the thiol-activated cholesterol-dependent cytolysin (cdc) family

PTM databases

iPTMnetiP13128

Proteomic databases

PaxDbiP13128

Genome annotation databases

EnsemblBacteriaiCAD00729; CAD00729; CAD00729
GeneIDi39647307
987033
KEGGilmo:lmo0202
PATRICifig|169963.11.peg.207

Phylogenomic databases

eggNOGiENOG4105E5P Bacteria
ENOG410XQPX LUCA
HOGENOMiCLU_026912_0_0_9
KOiK11031
OMAiNDRTYPG

Enzyme and pathway databases

BioCyciLMON169963:LMO0202-MONOMER

Miscellaneous databases

PHI-baseiPHI:6618
PHI:7897

Family and domain databases

Gene3Di2.60.40.1430, 1 hit
3.90.840.10, 1 hit
InterProiView protein in InterPro
IPR035390 Thiol_cytolys_C
IPR038700 Thiol_cytolys_C_sf
IPR001869 Thiol_cytolysin
IPR036363 Thiol_cytolysin_ab_sf
IPR036359 Thiol_cytolysin_sf
PfamiView protein in Pfam
PF17440 Thiol_cytolys_C, 1 hit
PF01289 Thiol_cytolysin, 1 hit
PRINTSiPR01400 TACYTOLYSIN
SUPFAMiSSF56978 SSF56978, 1 hit
PROSITEiView protein in PROSITE
PS00481 THIOL_CYTOLYSINS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTACY_LISMO
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P13128
Secondary accession number(s): Q48747, Q57096, Q57206
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 17, 2020
This is version 148 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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