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Protein

Multifunctional-autoprocessing repeats-in-toxin

Gene

rtxA

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Multifunctional-autoprocessing repeats-in-toxin: Precursor of a multifunctional toxin that causes destruction of the actin cytoskeleton by covalent cross-linking of actin and inactivation of Rho GTPases when translocated into the host cytoplasm (PubMed:26185092). Upon translocation into the host cell, undergoes autoprocessing in cis mediated by the peptidase C80 domain (also named CPD domain): the protease activity is activated upon binding inositol hexakisphosphate (InsP6) present at the host cell membrane and delivers the Cysteine protease domain-containing toxin F3 chain to the host cytosol (PubMed:17464284, PubMed:18591243, PubMed:18845756, PubMed:19620709, PubMed:19465933). The Cysteine protease domain-containing toxin F3 chain will then further cleave and release effector toxin chains that cause disassembly of the actin cytoskeleton and enhance V.cholerae colonization of the small intestine, possibly by facilitating evasion of phagocytic cells (PubMed:11553575, PubMed:12045243, PubMed:17698573, PubMed:17698571, PubMed:19812690, PubMed:19620709).1 Publication8 Publications
Cysteine protease domain-containing toxin F3: Following autocatalytic cleavage in cis at the Leu-3441-Ala-3442 site, this chain mediates processing in trans to release other individual toxin chains to the host cytosol (PubMed:19620709). Released effector toxin chains cause disassembly of the actin cytoskeleton and enhance V.cholerae colonization of the small intestine, possibly by facilitating evasion of phagocytic cells (PubMed:17698573, PubMed:17698571).3 Publications
Actin cross-linking toxin F1: Actin-directed toxin that catalyzes the covalent cross-linking of host cytoplasmic monomeric actin (PubMed:11032799, PubMed:15199181, PubMed:16954226, PubMed:17951576, PubMed:19015515, PubMed:19656298, PubMed:23029200, PubMed:26228148). Mediates the cross-link between 'Lys-50' of one monomer and 'Glu-270' of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding (PubMed:19015515). The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners (PubMed:26228148). Acts as an acid--amino-acid ligase that transfers the gamma-phosphoryl group of ATP to the 'Glu-270' actin residue, resulting in the formation of an activated acyl phosphate intermediate. This intermediate is further hydrolyzed and the energy of hydrolysis is utilized for the formation of the amide bond between actin subunits (PubMed:23029200).8 Publications
Actin cross-linking toxin F4: Actin-directed toxin that catalyzes the covalent cross-linking of host cytoplasmic monomeric actin (PubMed:11032799, PubMed:15199181, PubMed:16954226, PubMed:17951576, PubMed:19015515, PubMed:19656298, PubMed:23029200, PubMed:26228148). Mediates the cross-link between 'Lys-50' of one monomer and 'Glu-270' of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding (PubMed:19015515). The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners (PubMed:26228148). Acts as an acid--amino-acid ligase that transfers the gamma-phosphoryl group of ATP to the 'Glu-270' actin residue, resulting in the formation of an activated acyl phosphate intermediate. This intermediate is further hydrolyzed and the energy of hydrolysis is utilized for the formation of the amide bond between actin subunits (PubMed:23029200).8 Publications
Rho inactivation domain-containing toxin F2: After delivery to the host cytosol, localizes to the host cell membrane where it modifies some cellular signaling resulting in loss of all active GTP-bound Rho and subsequent actin depolymerization. Although both this chain and the Actin cross-linking toxin F4 chain independently affect polymerized actin, the domains are not synergistic (PubMed:17474905, PubMed:19434753, PubMed:23184949). Its similarity with members of the circular permuted thiol peptidase family, suggests that it acts by mediating modification of some protein at the host cell membrane (PubMed:26185092).1 Publication3 Publications
ABH effector region toxin F5: Indirectly activates the small GTPase CDC42.1 Publication

Cofactori

Mg2+2 PublicationsNote: Binds 2 Mg2+ ions per subunit. Mg2+ is required for actin cross-linking activity. Can also use Mn2+ ions instead of Mg2+.By similarity

Enzyme regulationi

Protease activity is inhibited by N-ethylmaleimide but not other protease inhibitors (PubMed:17464284). Protease activity is inhibited by aza-leucine epoxide (PubMed:19465933). Protease activity is activated upon binding inositol hexakisphosphate (InsP6) via an allosteric mechanism: the active site is disordered or occluded in the absence of InsP6, protecting the protease active-site sulfhydryl until the toxin enters a eukaryotic cell (PubMed:18845756, PubMed:19620709). Upon processing at the Leu-3441-Ala-3442 site, the peptidase C80 domain is converted to a form with much reduced affinity for InsP6, but is reactivated for high affinity binding of InsP6 by cooperative binding of both a new substrate and InsP6. Reactivation allows cleavage at other sites, specifically at Leu residues between the effector domains (PubMed:19620709).4 Publications

Kineticsi

  1. KM=7.8 µM for ATP (for actin cross-linking activity)1 Publication
  2. KM=49.9 µM for GTP (for actin cross-linking activity)1 Publication

    pH dependencei

    Optimum pH is 7.0-9.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi2003 – 20031Magnesium 1; catalytic; for actin cross-linking activityBy similarity
    Metal bindingi2003 – 20031Magnesium 2; catalytic; for actin cross-linking activityBy similarity
    Metal bindingi2065 – 20651Magnesium 2; catalytic; for actin cross-linking activityBy similarity
    Metal bindingi2149 – 21491Magnesium 1; catalytic; for actin cross-linking activityBy similarity
    Binding sitei2255 – 22551ATP; via carbonyl oxygenBy similarity
    Metal bindingi2326 – 23261Magnesium 1; catalytic; for actin cross-linking activityBy similarity
    Binding sitei3526 – 35261Inositol hexakisphosphateCombined sources3 Publications
    Active sitei3532 – 35321For cysteine protease activityPROSITE-ProRule annotation1 Publication
    Binding sitei3577 – 35771Inositol hexakisphosphateCombined sources3 Publications
    Active sitei3581 – 35811Nucleophile; for cysteine protease activityPROSITE-ProRule annotation1 Publication
    Binding sitei3581 – 35811InhibitorCombined sources1 Publication
    Binding sitei3636 – 36361Inositol hexakisphosphateCombined sources3 Publications
    Binding sitei3641 – 36411Inositol hexakisphosphateCombined sources3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1999 – 20035ATPBy similarity

    GO - Molecular functioni

    • acid-amino acid ligase activity Source: UniProtKB
    • ATP binding Source: UniProtKB
    • calcium ion binding Source: TIGR
    • cysteine-type endopeptidase activity Source: UniProtKB
    • cysteine-type peptidase activity Source: UniProtKB-KW
    • inositol hexakisphosphate binding Source: UniProtKB
    • ligase activity Source: UniProtKB-KW
    • lipid binding Source: UniProtKB-KW
    • magnesium ion binding Source: UniProtKB

    GO - Biological processi

    • actin filament depolymerization Source: UniProtKB
    • actin filament reorganization Source: InterPro
    • hemolysis by symbiont of host erythrocytes Source: TIGR
    • isopeptide cross-linking Source: UniProtKB
    • isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine Source: UniProtKB
    • killing of cells of other organism Source: TIGR
    • pathogenesis Source: UniProtKB
    • protein autoprocessing Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Ligase, Protease, Thiol protease, Toxin

    Keywords - Biological processi

    Virulence

    Keywords - Ligandi

    ATP-binding, Lipid-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciVCHO:VC1451-MONOMER.

    Protein family/group databases

    MEROPSiC80.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Multifunctional-autoprocessing repeats-in-toxin1 Publication (EC:3.4.22.-1 Publication)
    Short name:
    MARTX1 Publication
    Cleaved into the following 5 chains:
    Actin cross-linking toxin F11 Publication (EC:6.3.2.-1 Publication)
    Actin cross-linking toxin F41 Publication (EC:6.3.2.-1 Publication)
    Rho inactivation domain-containing toxin F21 Publication
    ABH effector region toxin F51 Publication
    Cysteine protease domain-containing toxin F31 Publication (EC:3.4.22.-1 Publication)
    Gene namesi
    Name:rtxA1 Publication
    Synonyms:rtx1 Publication
    Ordered Locus Names:VC_1451Imported
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
    Taxonomic identifieri243277 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    Proteomesi
    • UP000000584 Componenti: Chromosome 1

    Subcellular locationi

    Multifunctional-autoprocessing repeats-in-toxin :
    • Secreted 2 Publications
    • Host cytoplasmhost cytosol 1 Publication

    • Note: Secreted via the type I secretion system.1 Publication
    Rho inactivation domain-containing toxin F2 :
    Actin cross-linking toxin F1 :
    • Host cytoplasmhost cytosol 1 Publication
    Actin cross-linking toxin F4 :
    • Host cytoplasmhost cytosol 1 Publication

    GO - Cellular componenti

    • extracellular region Source: UniProtKB
    • host cell cytosol Source: UniProtKB-SubCell
    • host cell plasma membrane Source: UniProtKB
    • membrane Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Cellular componenti

    Host cell membrane, Host cytoplasm, Host membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2003 – 20031E → A: Abolished actin cross-linking activity and ability to round host cells. 1 Publication
    Mutagenesisi2005 – 20051E → A: Impaired actin cross-linking activity and ability to round host cells. 1 Publication
    Mutagenesisi2005 – 20051E → G: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2035 – 20351L → P: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2038 – 20381D → A: Impaired actin cross-linking activity and ability to round host cells. 1 Publication
    Mutagenesisi2055 – 20551G → E: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2065 – 20651E → A: Abolished actin cross-linking activity. 1 Publication
    Mutagenesisi2065 – 20651E → G: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2068 – 20681T → P: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2089 – 20891L → P: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2096 – 20961H → A: Abolished actin cross-linking activity. 1 Publication
    Mutagenesisi2117 – 21171L → P: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2149 – 21491Q → R: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2153 – 21531A → T: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2175 – 21751W → R: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2206 – 22061L → P: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2209 – 22091V → A: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2250 – 22501W → R: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2259 – 22591V → I: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2326 – 23261E → A: Abolished actin cross-linking activity. 1 Publication
    Mutagenesisi2328 – 23281R → A: Impaired actin cross-linking activity and ability to round host cells. 1 Publication
    Mutagenesisi2328 – 23281R → H: Reduced actin cross-linking activity. 1 Publication
    Mutagenesisi2447 – 24471L → A: Impaired cleavage of the Rho inactivation domain-containing toxin F2 chain; when associated with A-3098. 1 Publication
    Mutagenesisi2596 – 25961Y → F: Abolished localization to the host cell membrane. 1 Publication
    Mutagenesisi2641 – 26411S → T: Abolished localization to the host cell membrane. 1 Publication
    Mutagenesisi2643 – 26431R → K: Abolished localization to the host cell membrane. 1 Publication
    Mutagenesisi2734 – 27341E → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2735 – 27351Y → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2760 – 27601D → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2764 – 27641L → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2766 – 27661K → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2768 – 27681H → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2772 – 27721E → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2776 – 27761S → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2779 – 27791S → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2781 – 27811T → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2786 – 27861K → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2788 – 27881S → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2790 – 27901H → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2791 – 27911S → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2793 – 27931L → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2795 – 27951H → A: Impaired activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2798 – 27981L → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2804 – 28041R → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2820 – 28201Y → A: Impaired activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2820 – 28201Y → F: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2822 – 28221S → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2829 – 28291K → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2830 – 28301S → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2850 – 28501R → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2864 – 28641L → A: Impaired activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2867 – 28671D → A: Impaired activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2871 – 28711E → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2872 – 28721E → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2874 – 28741D → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2887 – 28871R → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2914 – 29141L → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2950 – 29501R → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2956 – 29561R → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2961 – 29611R → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2971 – 29711R → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2977 – 29771R → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2981 – 29811E → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2982 – 29821R → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2991 – 29911K → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2993 – 29931S → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2996 – 29961D → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi2999 – 29991R → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3002 – 30021R → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3005 – 30051L → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3008 – 30081L → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3016 – 30161E → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3019 – 30191R → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3027 – 30271R → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3028 – 30281Y → A: Impaired activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3028 – 30281Y → F: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3031 – 30311L → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3035 – 30351C → A or S: Impaired activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3036 – 30361S → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3037 – 30371S → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3043 – 30431L → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3044 – 30441K → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3049 – 30491D → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3054 – 30541H → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3064 – 30641T → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3077 – 30771E → A: Does not affect the activity of the Rho inactivation domain-containing toxin F2 chain. 1 Publication
    Mutagenesisi3098 – 30981L → A: Impaired cleavage of the Rho inactivation domain-containing toxin F2 chain; when associated with A-2447. 1 Publication
    Mutagenesisi3441 – 34411L → A: Modified autocatalytic cleavage site, leading to cleavage at another site. 1 Publication
    Mutagenesisi3462 – 34621P → A: No effect in autocatalytic cleavage. 1 Publication
    Mutagenesisi3470 – 34701R → A: Decreased autocatalytic cleavage. 1 Publication
    Mutagenesisi3476 – 34761I → A: No effect in autocatalytic cleavage. 1 Publication
    Mutagenesisi3478 – 34781Q → A: No effect in autocatalytic cleavage. 1 Publication
    Mutagenesisi3480 – 34801E → A: No effect in autocatalytic cleavage. Impaired autocatalytic cleavage; when associated with A-3482. 1 Publication
    Mutagenesisi3482 – 34821D → A: No effect in autocatalytic cleavage. Impaired autocatalytic cleavage; when associated with A-3480. 1 Publication
    Mutagenesisi3488 – 34881A → I: Decreased autocatalytic cleavage. 1 Publication
    Mutagenesisi3492 – 34921L → D: Decreased autocatalytic cleavage. 1 Publication
    Mutagenesisi3495 – 34951K → A: Decreased autocatalytic cleavage. 1 Publication
    Mutagenesisi3499 – 35002SS → AA: No effect in autocatalytic cleavage. 1 Publication
    Mutagenesisi3524 – 35241K → A: No effect in autocatalytic cleavage. 1 Publication
    Mutagenesisi3526 – 35261R → A: Decreased autocatalytic cleavage. 1 Publication
    Mutagenesisi3532 – 35321H → A: Abolishes autocatalytic cleavage. 2 Publications
    Mutagenesisi3534 – 35341R → A: Increased autocatalytic cleavage. 1 Publication
    Mutagenesisi3537 – 35371S → A: No effect in autocatalytic cleavage. 1 Publication
    Mutagenesisi3551 – 35511E → A: Does not affect autocatalytic cleavage. 1 Publication
    Mutagenesisi3552 – 35521L → A: No effect in autocatalytic cleavage. 1 Publication
    Mutagenesisi3572 – 35721K → A: No effect in autocatalytic cleavage. 1 Publication
    Mutagenesisi3581 – 35811C → S or A: Abolishes autocatalytic cleavage. 3 Publications
    Mutagenesisi3606 – 36061R → A: Increased autocatalytic cleavage. 1 Publication
    Mutagenesisi3609 – 36091V → A: No effect in autocatalytic cleavage. 1 Publication
    Mutagenesisi3612 – 36121R → A: Decreased autocatalytic cleavage. 1 Publication
    Mutagenesisi3619 – 36191D → A or N: Slightly reduced inositol hexakisphosphate-binding and strongly decreased autocatalytic cleavage. 1 Publication
    Mutagenesisi3620 – 36201E → A: Does not affect inositol hexakisphosphate-binding. 1 Publication
    Mutagenesisi3623 – 36231R → A: Decreased autocatalytic cleavage. 1 Publication
    Mutagenesisi3623 – 36231R → Q: Slightly reduced inositol hexakisphosphate-binding and strongly decreased autocatalytic cleavage. 1 Publication
    Mutagenesisi3624 – 36241K → A: Decreased autocatalytic cleavage. 1 Publication
    Mutagenesisi3624 – 36241K → N: Abolishes inositol hexakisphosphate-binding and autocatalytic cleavage. 1 Publication
    Mutagenesisi3632 – 36321D → A: Does not affect inositol hexakisphosphate-binding. 1 Publication
    Mutagenesisi3633 – 36331W → A: Reduced inositol hexakisphosphate-binding and autocatalytic cleavage. 1 Publication
    Mutagenesisi3633 – 36331W → F: Slightly reduced inositol hexakisphosphate-binding and strongly decreased autocatalytic cleavage. 1 Publication
    Mutagenesisi3636 – 36361K → N: Abolishes inositol hexakisphosphate-binding and autocatalytic cleavage. 1 Publication
    Mutagenesisi3641 – 36411K → A: Decreased autocatalytic cleavage. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Sequence analysisAdd
    BLAST
    Chaini33 – 45584526Multifunctional-autoprocessing repeats-in-toxinPRO_0000434113Add
    BLAST
    Chaini33 – 24472415Actin cross-linking toxin F11 PublicationPRO_0000434114Add
    BLAST
    Chaini1972 – 2447476Actin cross-linking toxin F41 PublicationPRO_0000434115Add
    BLAST
    Chaini2448 – 3098651Rho inactivation domain-containing toxin F21 PublicationPRO_0000434116Add
    BLAST
    Chaini3099 – 3441343ABH effector region toxin F51 PublicationPRO_0000434117Add
    BLAST
    Chaini3442 – 45581117Cysteine protease domain-containing toxin F31 PublicationPRO_0000434118Add
    BLAST

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1971 – 19722Cleavage; by autolysis1 Publication
    Sitei2447 – 24482Cleavage; by autolysis2 Publications
    Sitei3098 – 30992Cleavage; by autolysis2 Publications
    Sitei3441 – 34422Cleavage; by autolysis4 Publications

    Keywords - PTMi

    Autocatalytic cleavage

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-48626N.
    STRINGi243277.VC1451.

    Structurei

    Secondary structure

    1
    4558
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3452 – 34543Combined sources
    Beta strandi3472 – 34787Combined sources
    Helixi3483 – 349513Combined sources
    Helixi3496 – 34994Combined sources
    Beta strandi3500 – 35056Combined sources
    Beta strandi3511 – 35166Combined sources
    Helixi3518 – 35203Combined sources
    Beta strandi3523 – 35308Combined sources
    Beta strandi3533 – 35353Combined sources
    Helixi3549 – 356719Combined sources
    Beta strandi3574 – 35829Combined sources
    Beta strandi3588 – 35914Combined sources
    Helixi3592 – 360211Combined sources
    Beta strandi3608 – 36147Combined sources
    Beta strandi3616 – 36183Combined sources
    Beta strandi3624 – 36274Combined sources
    Beta strandi3629 – 36313Combined sources
    Beta strandi3633 – 36364Combined sources
    Helixi3638 – 36403Combined sources
    Beta strandi3641 – 36444Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EEBX-ray2.10A/B3442-3650[»]
    3FZYX-ray1.95A/B3440-3650[»]
    3GCDX-ray2.35A/B/C/D3442-3650[»]
    ProteinModelPortaliQ9KS12.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9KS12.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati114 – 13118RtxA 1Sequence analysisAdd
    BLAST
    Repeati134 – 15118RtxA 2Sequence analysisAdd
    BLAST
    Repeati154 – 17017RtxA 3Sequence analysisAdd
    BLAST
    Repeati174 – 19724RtxA 4Sequence analysisAdd
    BLAST
    Repeati200 – 21718RtxA 5Sequence analysisAdd
    BLAST
    Repeati220 – 23718RtxA 6Sequence analysisAdd
    BLAST
    Repeati268 – 28518RtxA 7Sequence analysisAdd
    BLAST
    Repeati288 – 30417RtxA 8Sequence analysisAdd
    BLAST
    Repeati594 – 61118RtxA 9Sequence analysisAdd
    BLAST
    Repeati614 – 63017RtxA 10Sequence analysisAdd
    BLAST
    Repeati634 – 65118RtxA 11Sequence analysisAdd
    BLAST
    Repeati654 – 66815RtxA 12Sequence analysisAdd
    BLAST
    Repeati751 – 76313RtxA 13Sequence analysisAdd
    BLAST
    Repeati769 – 78113RtxA 14Sequence analysisAdd
    BLAST
    Repeati792 – 80817RtxA 15Sequence analysisAdd
    BLAST
    Repeati811 – 82616RtxA 16Sequence analysisAdd
    BLAST
    Repeati830 – 84516RtxA 17Sequence analysisAdd
    BLAST
    Repeati851 – 86515RtxA 18Sequence analysisAdd
    BLAST
    Repeati868 – 88518RtxA 19Sequence analysisAdd
    BLAST
    Repeati887 – 90115RtxA 20Sequence analysisAdd
    BLAST
    Repeati906 – 92015RtxA 21Sequence analysisAdd
    BLAST
    Repeati925 – 94218RtxA 22Sequence analysisAdd
    BLAST
    Repeati944 – 96017RtxA 23Sequence analysisAdd
    BLAST
    Repeati982 – 99413RtxA 24Sequence analysisAdd
    BLAST
    Repeati1001 – 101616RtxA 25Sequence analysisAdd
    BLAST
    Repeati1041 – 105313RtxA 26Sequence analysisAdd
    BLAST
    Repeati1077 – 108913RtxA 27Sequence analysisAdd
    BLAST
    Repeati1097 – 111216RtxA 28Sequence analysisAdd
    BLAST
    Repeati1120 – 113213RtxA 29Sequence analysisAdd
    BLAST
    Repeati1135 – 115218RtxA 30Sequence analysisAdd
    BLAST
    Repeati1155 – 116915RtxA 31Sequence analysisAdd
    BLAST
    Repeati1173 – 118917RtxA 32Sequence analysisAdd
    BLAST
    Repeati1194 – 120916RtxA 33Sequence analysisAdd
    BLAST
    Repeati1211 – 122717RtxA 34Sequence analysisAdd
    BLAST
    Repeati1230 – 124617RtxA 35Sequence analysisAdd
    BLAST
    Repeati1252 – 126615RtxA 36Sequence analysisAdd
    BLAST
    Repeati1268 – 128518RtxA 37Sequence analysisAdd
    BLAST
    Repeati1306 – 132318RtxA 38Sequence analysisAdd
    BLAST
    Repeati1325 – 134218RtxA 39Sequence analysisAdd
    BLAST
    Domaini1988 – 2422435ACDPROSITE-ProRule annotation1 PublicationAdd
    BLAST
    Domaini3462 – 3646185Peptidase C80PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2574 – 265885Membrane localization region (MLD)1 PublicationAdd
    BLAST
    Regioni2734 – 3098365Rho inactivation domain (RID)CuratedAdd
    BLAST
    Regioni3195 – 3310116ABH effector regionCuratedAdd
    BLAST
    Regioni3468 – 34703Inositol hexakisphosphate bindingCombined sources3 Publications
    Regioni3495 – 34962Inositol hexakisphosphate bindingCombined sources3 Publications
    Regioni3532 – 35332Inhibitor bindingCombined sources1 Publication
    Regioni3610 – 36123Inositol hexakisphosphate bindingCombined sources3 Publications
    Regioni3616 – 36183Inhibitor bindingCombined sources1 Publication
    Regioni3623 – 36242Inositol hexakisphosphate bindingCombined sources3 Publications

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi43 – 301259Gly-richPROSITE-ProRule annotationAdd
    BLAST
    Compositional biasi584 – 1224641Gly-richPROSITE-ProRule annotationAdd
    BLAST
    Compositional biasi3709 – 37124Poly-SerSequence analysis
    Compositional biasi4187 – 4408222Gly-richPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ACD (actin cross-linking) domain.PROSITE-ProRule annotation
    Contains 1 peptidase C80 domain.PROSITE-ProRule annotationCurated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiENOG4105EUK. Bacteria.
    COG2931. LUCA.
    KOiK10953.

    Family and domain databases

    Gene3Di1.20.1440.20. 1 hit.
    2.150.10.10. 3 hits.
    3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR032074. ACD_dom.
    IPR020974. CPD_dom.
    IPR020972. Dermonecrotic/RTX_toxin_C.
    IPR022742. Hydrolase_4.
    IPR023353. LemA-like_dom.
    IPR011509. RtxA_toxin.
    IPR011049. Serralysin-like_metalloprot_C.
    [Graphical view]
    PfamiPF16671. ACD. 1 hit.
    PF12146. Hydrolase_4. 1 hit.
    PF11713. Peptidase_C80. 1 hit.
    PF11647. PMT_C. 1 hit.
    PF07634. RtxA. 39 hits.
    [Graphical view]
    SUPFAMiSSF51120. SSF51120. 2 hits.
    SSF53474. SSF53474. 1 hit.
    PROSITEiPS51772. ACD. 1 hit.
    PS51771. CGT_MARTX_CPD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9KS12-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVFYLIPKRR VWLMGKPFWR SVEYFFTGNY SADDGNNNIV AIGFGGQIHA
    60 70 80 90 100
    YGGDDHVTVG SIGATVYTGS GNDTVVGGSA YLKVEDSTGH LIVKGAAGYA
    110 120 130 140 150
    DINKSGDGNV SFAGAAGGVS IDHLGNHGDV SYGGAAAYNG ITRKGLSGNV
    160 170 180 190 200
    TFAGAGGYNA LWHETNQGNL SFTGAGAGNK LDRTWSNRYQ GSHGDVTFDG
    210 220 230 240 250
    AGAANSISSR VETGNITFRG AGADNHLVRK GKVGDITLQG AGASNRIERT
    260 270 280 290 300
    HQAEDVYTQT RGNIRFEGVG GYNSLYSDVA HGDIHFSGGG AYNTIIRKGS
    310 320 330 340 350
    GNDFAKEGMT NAKADEIVLT KAVMSGSWIG QDHHVTAVKS ASEPNTYLFA
    360 370 380 390 400
    FADSTYTKIN KVQLRNDPQT GELKYYSTAW YKEVNHLSNL ANQDISDNGG
    410 420 430 440 450
    FTAVNINGAY TLSDLKVEHQ QSVTVHAVEK SLTEYEWVTY ANGAVIDAKE
    460 470 480 490 500
    VSLSDAKMGG HAIYADGTKV DVKAVKSNRQ PNTYIYAKVL GPYTKIVVVE
    510 520 530 540 550
    LANDPETGAL KYQARSWYKE GDHTANIANQ DISSATGYNP MGKGGYSLSD
    560 570 580 590 600
    LHYSVNAVRS TSETVADIEE YTDQTLFKPA NDSGESSGDV RFNGAGGGNV
    610 620 630 640 650
    IKSNVTRGNV HFNGGGIANV ILHSSQFGNT EFNGGGAANV IVKSGEEGDL
    660 670 680 690 700
    TFRGAGLANV LVHQSEQGKM DVYAGGAVNV LVRLGDGQYL AHLLAYGNIS
    710 720 730 740 750
    VQKGSGDSRV VMLGGYNTHT QIGSGNGLWL AAGGFNVMTQ VGKGDVAAVL
    760 770 780 790 800
    AGGANVLTKM GEGELTSGML GGANVITHIS NDDQLSNTTA VALGGANILT
    810 820 830 840 850
    KKGKGNTLAV MGGGANVLTH VGDGTTTGVM VGGANILTKV GNGDTTGILL
    860 870 880 890 900
    GVGNVLTHVG DGQTLGVMGA AGNIFTKVGD GTSIAVMIGA GNIFTHVGEG
    910 920 930 940 950
    NAWALMGGLG NVFTKVGNGD ALALMVAEAN VFTHIGDGMS VALMLAKGNV
    960 970 980 990 1000
    ATKVGNGTTL AAMVGNVNIF THIGHGSTFA AMIGQANIMT KVGNDLTAAL
    1010 1020 1030 1040 1050
    MVGKANIMTH VGDGTSLGLF AGEVNVMTKV GNGTTLAAMF GKANIMTHVG
    1060 1070 1080 1090 1100
    DGLTGVLALG EANIVTKLGD DFMGVVAAAK ANVVTHVGDA TTAAVLAGKG
    1110 1120 1130 1140 1150
    NILTKVGEGT TVGLLISDVG NVMTHVGDGT TIGIAKGKAN LITKVGDGLG
    1160 1170 1180 1190 1200
    VNVTWGQANV FTQVGDGDRY NFAKGEANLI TKVGDGQEVS VVQGEANIIT
    1210 1220 1230 1240 1250
    HVGNGDDYTG AWGKANVITK VGHGQNVVLA KGEANIVTQV GDGDSFNALW
    1260 1270 1280 1290 1300
    SKGNIVTKVG DGMQVTAAKG QANITTTVGN GLNVTAAYGD ANINTKVGDG
    1310 1320 1330 1340 1350
    VSVNVAWGKY NINTKVGDGL NVAVMKGKAN ANIHVGDGLN INASYAQNNV
    1360 1370 1380 1390 1400
    AIKVGNGDFY SLAVASSNTS SNKLSALFDN IKQTVLGVGG SQAINYLVQG
    1410 1420 1430 1440 1450
    DEASSSGTHK GRGAIATPEI TKLDGFQMDA IKEVSSDLGD SLTGSVTKVD
    1460 1470 1480 1490 1500
    TPDLNKMQHA LNVDDSSVQA PNLIVNGDFE LGEHGWQSTH GVEASYAGSV
    1510 1520 1530 1540 1550
    YGVEGEGHGA RVTELDTYTN TSLYQDLANL AQGEVIAVSF DFAKRAGLSN
    1560 1570 1580 1590 1600
    NEGIEVLWNG EVVFSSSGDE SAWQQKNLKL TAQAGSNRIE FKGTGHNDGL
    1610 1620 1630 1640 1650
    GYILDNVVAT SESSQQANAI REHATQNPAA QNALSDKERA EADRQRLEQE
    1660 1670 1680 1690 1700
    KQKQLDAVAG SQSQLESTDQ QALENNGQAQ RDAVKEESEA VTAELAKLAQ
    1710 1720 1730 1740 1750
    GLDVLDGQAT HTGESGDQWR NDFAGGLLDG VQSQLDDAKQ LANDKIAAAK
    1760 1770 1780 1790 1800
    QTLSDNNSKV KESVAKSEAG VAQGEQNRAG VEQDIADAQA DAEKRKADAL
    1810 1820 1830 1840 1850
    AKGKDAQQAE SDAHHAVNNA QSRGDRDVQL AENKANQAQA DAQGAKQNEG
    1860 1870 1880 1890 1900
    DRPDRQGVTG SGLSGNAHSV EGAGETDSHV NTDSQTNADG RFSEGLTEQE
    1910 1920 1930 1940 1950
    QEALEGATNA VNRLQINAGI RAKNSVSSMT SMFSETNSKS IVVPTKVSPE
    1960 1970 1980 1990 2000
    PERQEVTRRD VRISGVNLES LSAVQGSQPT GQLASKSVPG FKSHFASTSI
    2010 2020 2030 2040 2050
    GIENELSGLV VVLPKNSAQT FGYVHDSQGN PLFMLTKDMN QGGYSNPVGI
    2060 2070 2080 2090 2100
    NDIQGVNNWQ THTIELVTYP SEISDTAAVE SRKEAMLWLA KEFTDHINQS
    2110 2120 2130 2140 2150
    NHQSLPHLVS DDGRFTLVIS NSKHLIAAGN GTSIDAQGKT IGMTPSGQQA
    2160 2170 2180 2190 2200
    TMAISAKEFG TSSSPEVRLL ESAPWYQAGL RDEFLANAKN TTLDDPATAQ
    2210 2220 2230 2240 2250
    NVYAYLTSVY SKTADLAKEY GIYINDWDPA SEGFSPNAQG LTDPKVKNAW
    2260 2270 2280 2290 2300
    SILPRTKPVR MLELLSAEDS RYVRQQIAEK LKGTYSESLA KNVFEYFQYG
    2310 2320 2330 2340 2350
    GEVAGHGINN ATTGSVQQPE PAILFEFRSV PSALSDFVPK TASTVKVDVK
    2360 2370 2380 2390 2400
    ALDHFDSASR KAIITEVNAL VSGSEDFDAW YQEYRASKGQ PPVKNPKSSA
    2410 2420 2430 2440 2450
    SANHKAEWLM TQHAEQWAKI TAPYTDNHET LTSTKLASND KEELHALGET
    2460 2470 2480 2490 2500
    SNLENNKQQE NVASIINTML NDMLPFYALR TERNLLVQEG DEGFEVRAWP
    2510 2520 2530 2540 2550
    GTEDKSKTII LEDPEDAAQH KAIERFILAN FDNFEQMPDE LFLVDNKVIS
    2560 2570 2580 2590 2600
    HHEGRTHVLA QKVDGAWQYN ATVELMSVTE LLDAANVTGK IRGESYQQVI
    2610 2620 2630 2640 2650
    DALTDYHASI TEHADYEPES VEKLLNLRKK IEGYVLGHPD SGRVEAMNSL
    2660 2670 2680 2690 2700
    LNQVNTRLDE VSLLSVAEQT IQAQNSFSRL YDQLEAANLK ESKHLYLDQN
    2710 2720 2730 2740 2750
    GDFVTKGKGN LANIDLLGSR EAVLEKVKLT VSNEYGQTVA DTIFAGLSAK
    2760 2770 2780 2790 2800
    DLAKDGKGVD IAGLNKVHQA IEQHLSPVSA TLYIWKPSDH SALGHAALQI
    2810 2820 2830 2840 2850
    GQGRTQLEGQ AAADFNQQNY VSWWPLGSKS SNISNILNVA TKDQPDLKLR
    2860 2870 2880 2890 2900
    WSDFSQPAHQ NDTLEHDVAS EENDGFGLHD GDIKLKRFIE KLNAAKGIDA
    2910 2920 2930 2940 2950
    SFKEASEGYA SVLLGNPDML ETTSIPAHVF QPFVEQWNDT SYDMMDVAHR
    2960 2970 2980 2990 3000
    FAQELRLQAQ RSDDPELLEK RIGNVIRQFA ERALEEIETF KASQADQGRV
    3010 3020 3030 3040 3050
    FRINLEGLDV AAMQAEWHRL SNDPDARYQL LTKNCSSTVA KVLKAGGADK
    3060 3070 3080 3090 3100
    LIGHTWLPKF GVWTPTELFN FGQALQEAQL EIAAKKQSHQ VTDVLDALSG
    3110 3120 3130 3140 3150
    NEKPKENVAI ENDGTPPRDK ESLSPLTRFL NNELYGDKEA RRKIGEITQT
    3160 3170 3180 3190 3200
    LLDHAVEKGE SQKITLQGEA GRLTGYYHQG TAPSEGETSS PSGKVVLFLH
    3210 3220 3230 3240 3250
    GSGSSAEEQA SAIRNHYQKQ GIDMLAVNLR GYGESDGGPS EKGLYQDART
    3260 3270 3280 3290 3300
    MFNYLVNDKG IDPSNIIIHG YSMGGPIAAD LARYAAQNGQ AVSGLLLDRP
    3310 3320 3330 3340 3350
    MPSMTKAITA HEVANPAGIV GAIAKAVNGQ FSVEKNLEGL PKETSILLLT
    3360 3370 3380 3390 3400
    DNEGLGNEGE KLRTKLTASG YNVTGEQTFY GHEASNRLMS QYADQIVSGL
    3410 3420 3430 3440 3450
    SSSASVDEDL DQQGLDTTST KDQGISNKND HLQVVDSKEA LADGKILHNQ
    3460 3470 3480 3490 3500
    NVNSWGPITV TPTTDGGETR FDGQIIVQME NDPVVAKAAA NLAGKHAESS
    3510 3520 3530 3540 3550
    VVVQLDSDGN YRVVYGDPSK LDGKLRWQLV GHGRDHSETN NTRLSGYSAD
    3560 3570 3580 3590 3600
    ELAVKLAKFQ QSFNQAENIN NKPDHISIVG CSLVSDDKQK GFGHQFINAM
    3610 3620 3630 3640 3650
    DANGLRVDVS VRSSELAVDE AGRKHTKDAN GDWVQKAENN KVSLSWDAQG
    3660 3670 3680 3690 3700
    EVVAKDERIR NGIAEGDIDL SRIGVNNVDE PARGAIGDNN DVFDAPEKRK
    3710 3720 3730 3740 3750
    PETEVIANSS SSNQFSYSGN IQVNVGEGEF TAVNWGTSNV GIKVGTGGFK
    3760 3770 3780 3790 3800
    SLAFGDNNVM VHIGDGESKH SVDIGGYQAL EGAQMFLGNR NVSFNFGHSN
    3810 3820 3830 3840 3850
    DLILMMDKSI PTPPLVNPFD GAARISGVLQ GIATSGEGED WLAAQEQQWT
    3860 3870 3880 3890 3900
    LSGAKKFVKD MSGLDQSSSV DYTTLVELDS QNERDSRGLK HDAEATLNKQ
    3910 3920 3930 3940 3950
    YNQWLSGNGN SGTSQLSRAD KLRQANEKLA FNFAVGGQGA DIQVTTGNWN
    3960 3970 3980 3990 4000
    FMFGDNIQSI LDTNLGSLFG LMTQQFTATG QAKTTFTYTP QDLPRQLKNK
    4010 4020 4030 4040 4050
    LLGQLAGVGA ETTLADIFGV DYTASGQIVS RNGQAVDGVA ILKEMLEVIG
    4060 4070 4080 4090 4100
    EFSGDQLQAF VDPAKLLDSL KAGIDMGADG IKSFAETHGL KEKAPEEEKD
    4110 4120 4130 4140 4150
    NSSVSVNGAN VNSAQGATVA DGNTETAETQ DRAFGFNSLN LPNLFATIFS
    4160 4170 4180 4190 4200
    QDKQKEMKSL VENLKQNLTA DLLNMKEKTF DFLRNSGHLQ GDGDINISLG
    4210 4220 4230 4240 4250
    NYNFNWGGDG KDLGAYLGDN NNFWGGRGDD VFYATGKSNI FTGGEGNDMG
    4260 4270 4280 4290 4300
    VLMGRENMMF GGDGNDTAVV AGRINHVFLG AGDDQSFVFG EGGEIDTGSG
    4310 4320 4330 4340 4350
    RDYVVTSGNF NRVDTGDDQD YSVTIGNNNQ VELGAGNDFA NIFGNYNRIN
    4360 4370 4380 4390 4400
    AGAGNDVVKL MGYHAVLNGG DGDDHLIATA ISKFSQFNGG EGRDLMVLGG
    4410 4420 4430 4440 4450
    YQNTFKGGTD VDSFVVSGDV IDNLVEDIRS EDNIVFNGID WQKLWFERSG
    4460 4470 4480 4490 4500
    YDLKLSILRD PSNDSDQSKF EHIGSVTFSD YFNGNRAQVV IGMSEKDLSG
    4510 4520 4530 4540 4550
    EREYTMLSDS AIDALVQAMS GFEPQAGDNG FIDSLESKSQ AAISMAWSDV

    VHKKGLMV
    Length:4,558
    Mass (Da):485,355
    Last modified:October 14, 2015 - v2
    Checksum:i800DD5D1D119AE19
    GO

    Sequence cautioni

    The sequence AAD21057 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF119150 Genomic DNA. Translation: AAD21057.1. Different initiation.
    AE003852 Genomic DNA. Translation: AAF94608.1.
    PIRiC82199.
    RefSeqiNP_231094.1. NC_002505.1.
    WP_010895441.1. NC_002505.1.

    Genome annotation databases

    EnsemblBacteriaiAAF94608; AAF94608; VC_1451.
    GeneIDi2613957.
    KEGGivch:VC1451.
    PATRICi20081964. VBIVibCho83274_1381.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF119150 Genomic DNA. Translation: AAD21057.1. Different initiation.
    AE003852 Genomic DNA. Translation: AAF94608.1.
    PIRiC82199.
    RefSeqiNP_231094.1. NC_002505.1.
    WP_010895441.1. NC_002505.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EEBX-ray2.10A/B3442-3650[»]
    3FZYX-ray1.95A/B3440-3650[»]
    3GCDX-ray2.35A/B/C/D3442-3650[»]
    ProteinModelPortaliQ9KS12.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-48626N.
    STRINGi243277.VC1451.

    Protein family/group databases

    MEROPSiC80.001.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAF94608; AAF94608; VC_1451.
    GeneIDi2613957.
    KEGGivch:VC1451.
    PATRICi20081964. VBIVibCho83274_1381.

    Phylogenomic databases

    eggNOGiENOG4105EUK. Bacteria.
    COG2931. LUCA.
    KOiK10953.

    Enzyme and pathway databases

    BioCyciVCHO:VC1451-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiQ9KS12.

    Family and domain databases

    Gene3Di1.20.1440.20. 1 hit.
    2.150.10.10. 3 hits.
    3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR032074. ACD_dom.
    IPR020974. CPD_dom.
    IPR020972. Dermonecrotic/RTX_toxin_C.
    IPR022742. Hydrolase_4.
    IPR023353. LemA-like_dom.
    IPR011509. RtxA_toxin.
    IPR011049. Serralysin-like_metalloprot_C.
    [Graphical view]
    PfamiPF16671. ACD. 1 hit.
    PF12146. Hydrolase_4. 1 hit.
    PF11713. Peptidase_C80. 1 hit.
    PF11647. PMT_C. 1 hit.
    PF07634. RtxA. 39 hits.
    [Graphical view]
    SUPFAMiSSF51120. SSF51120. 2 hits.
    SSF53474. SSF53474. 1 hit.
    PROSITEiPS51772. ACD. 1 hit.
    PS51771. CGT_MARTX_CPD. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMARTX_VIBCH
    AccessioniPrimary (citable) accession number: Q9KS12
    Secondary accession number(s): Q9X4W2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 14, 2015
    Last sequence update: October 14, 2015
    Last modified: September 7, 2016
    This is version 100 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.