A0A2S3R7M0 · MARTX_VIBVL
- ProteinMultifunctional-autoprocessing repeats-in-toxin
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids5206 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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. 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. 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.vulnificus colonization of the small intestine, possibly by facilitating evasion of phagocytic cells.
Cysteine protease domain-containing toxin F3
Following autocatalytic cleavage in cis, this chain mediates processing in trans to release other individual toxin chains to the host cytosol. Released effector toxin chains cause disassembly of the actin cytoskeleton and enhance V.vulnificus colonization of the small intestine, possibly by facilitating evasion of phagocytic cells.
Actin cross-linking toxin F1
Actin-directed toxin that catalyzes the covalent cross-linking of host cytoplasmic monomeric actin. 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. 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. 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.
N-epsilon-fatty acyltransferase F2
N-epsilon-fatty acyltransferase that mediates lysine-palmitoylation of host Rho GTPase proteins, with a strong preference for host Rac1. After delivery to the host cytosol, localizes to the host cell membrane where it palmitoylates host Rho GTPase proteins, resulting in loss of all active GTP-bound Rho and subsequent actin depolymerization. Prenylation of host Rac1 at the C-terminus is required for lysine-palmitoylation.
ABH effector region toxin F5
Indirectly activates the small GTPase CDC42.
Catalytic activity
N-epsilon-fatty acyltransferase F2
hexadecanoyl-CoA + L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein] = CoA + H+ + N6-hexadecanoyl-L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein]This reaction proceeds in the forward direction.N-epsilon-fatty acyltransferase F2
dodecanoyl-CoA + L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein] = CoA + H+ + N6-dodecanoyl-L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein]This reaction proceeds in the forward direction.N-epsilon-fatty acyltransferase F2
decanoyl-CoA + L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein] = CoA + H+ + N6-decanoyl-L-lysyl-/S-(2E,6E,10E)-geranylgeranyl-L-cysteinyl-[protein]This reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 Mg2+ ions per subunit. Mg2+ is required for actin cross-linking activity. Can also use Mn2+ ions instead of Mg2+.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 4117-4119 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: ESR | ||||||
Binding site | 4144-4145 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: KH | ||||||
Binding site | 4175 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 4181 | For cysteine protease activity | ||||
Sequence: H | ||||||
Binding site | 4226 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 4230 | Nucleophile; for cysteine protease activity | ||||
Sequence: C | ||||||
Binding site | 4259-4261 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: SVR | ||||||
Binding site | 4272-4273 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: RK | ||||||
Binding site | 4285 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 4290 | 1D-myo-inositol hexakisphosphate (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | host cell cytosol | |
Cellular Component | host cell plasma membrane | |
Cellular Component | membrane | |
Molecular Function | acyltransferase activity | |
Molecular Function | cysteine-type peptidase activity | |
Molecular Function | ligase activity | |
Molecular Function | lipid binding | |
Molecular Function | metal ion binding | |
Molecular Function | toxin activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional-autoprocessing repeats-in-toxin
- EC number
- Short namesMARTX
- Cleaved into 4 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Vibrionales > Vibrionaceae > Vibrio
Accessions
- Primary accessionA0A2S3R7M0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Multifunctional-autoprocessing repeats-in-toxin
Note: Secreted via the type I secretion system.
N-epsilon-fatty acyltransferase F2
Note: Targeted to the host cell membrane via the membrane localization region (MLD).
Actin cross-linking toxin F1
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MGKPFWRSVEYFFTGNYSA | ||||||
Chain | PRO_0000455659 | 20-1958 | Actin cross-linking toxin F1 | |||
Sequence: DDGNNSIVAIGFGGEIHAYGGDDHVTVGSIGATVYTGSGNDTVVGGSAYLRVEDTTGHLSVKGAAGYADINKSGDGNVSFAGAAGGVSIDHLGNNGDVSYGGAAAYNGITRKGLSGNVTFKGAGGYNALWHETNQGNLSFAGAGAGNKLDRTWFNRYQGSRGDVTFDGAGAANSISSRVETGNITFRGAGADNHLVRKGKVGDITLQGAGASNRIERTRQAEDVYAQTRGNIRFEGVGGYNSLYSDVAHGDIHFSGGGAYNTITRKGSGSSFDAQGMEYAKAEDIVLTAAQMHGLSIDNGNKFHAVTAVKSEREPNTYLFAIADGTYTKINKVRLYNDPETGKLKYYSEAWFKRGNHLAELARSDVSSAGGFEVNPINGGYTLANIAVEHQQSVTVHAVEKNLTEYEWVTYANGTLIDAKDVALSEAKMGGHAISTDGTTVDVQAVKSNRKPNTYVYAKVLGPYTKIVVVELANDPKTGALKYQARSWYKEGDHTANLANEDISSANGYHSMGKGGYSLSDLHYSVNAVRSTSETVADIDEYTDQTLFKPATDSGESSGDVRFNGAGGGNVIKSNVTRGNVYFNGGGIANVILHSSQFGNTEFNGGGAANVIVKSGEEGDLTFRGAGLANVLVHQSKQGKMDVYAGGAVNVLVRIGDGQYLAHLLAYGNISVHKGNGNSRVVMLGGYNTHTQIGSGNGLWLAAGGFNVMTQVGKGDVASVLAGGANVLTKVGDGDLTAGMLGGANVITHISGDNETSNTTAVALGGANILTKKGKGNTLAVMGGGANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGIMLGVGNVLTHVGDGQTLGVMGAAGNIFTKVGDGTSIAVMIGAGNIFTHVGEGNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATKVGNGTTLAAMVGNANIFTHVGSGSTFAAMIGQANIMTKVGNDLTAALMVGKANIYTHVGDGTSLGIFAGEVNVMTKIGNGTTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKVGDDFMGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTTVGLLISDIGNVMTHVGDGTTIGIAKGKANIITKVGDGLGVNVAWGQANVFTQVGDGDRYNFAKGEANIITKVGDGKEVSVVQGKANIITHVGNGDDYTGAWGKANVITKVGNGRNVVLAKGEANIVTQVGDGDSFNALWSKGNIVTKVGDGMQVTAAKGKANITTTVGDGLSVTAAYGDANINTKVGDGVSVNVAWGKYNINTKVGDGLNVAVMKGKANANIHVGDGLNINASYAQNNVAIKVGNGDFYSLAVASSNTSSNKLSALFDNIKQTLLGVGGSQAINYLVQGDEASSSGTQKGRGAIATPEITKLDGFQMEAIEEVGSDLGDSLTGSVTKVDTPDLNKMQNALDVDGSSDQTQAPNLIVNGDFEQGDRGWKSTHGVEASYSGNVYGVNGEGHGARVTELDTYTNTSLYQDLTDLTEGEVIAVSFDFAKRAGLSNNEGIEVLWNGEVVFSSSGDASAWQQKTLKLTAHAGSNRIEFKGTGHNDGLGYILDNVVAKSESSQQANAVSEHATQNQASQNALSDKERAEADRQRLEQEKQKQLDAVAGSQSQLESTDQQALGNNGQAQRDAVKEESEAVTAELTKLAQGLDVLDGQATHTGESGDQWRNDFAGGLLDGVQSQLDDAKQLANDKIAAAKQTQSDNNSKVKESVAKSEAGVAQGEQNRAGAEQDIAEAKADAETRKADAVAKSNDAKQAESDAHSAANDAQSRGDRDAMNAENKANQAQNDAKGTKQNEGDRPDREGVAGSGLSGNAHSVEGAGETGSHITTDSQTNADGRFSEGLSEQEQEALEGATNAVNRLQINAGIRGKNSGSTITSMFTETNSDSIVVPTTASQDVVRKEIRISGVNLEGL | ||||||
Chain | PRO_0000455658 | 20-5206 | Multifunctional-autoprocessing repeats-in-toxin | |||
Sequence: DDGNNSIVAIGFGGEIHAYGGDDHVTVGSIGATVYTGSGNDTVVGGSAYLRVEDTTGHLSVKGAAGYADINKSGDGNVSFAGAAGGVSIDHLGNNGDVSYGGAAAYNGITRKGLSGNVTFKGAGGYNALWHETNQGNLSFAGAGAGNKLDRTWFNRYQGSRGDVTFDGAGAANSISSRVETGNITFRGAGADNHLVRKGKVGDITLQGAGASNRIERTRQAEDVYAQTRGNIRFEGVGGYNSLYSDVAHGDIHFSGGGAYNTITRKGSGSSFDAQGMEYAKAEDIVLTAAQMHGLSIDNGNKFHAVTAVKSEREPNTYLFAIADGTYTKINKVRLYNDPETGKLKYYSEAWFKRGNHLAELARSDVSSAGGFEVNPINGGYTLANIAVEHQQSVTVHAVEKNLTEYEWVTYANGTLIDAKDVALSEAKMGGHAISTDGTTVDVQAVKSNRKPNTYVYAKVLGPYTKIVVVELANDPKTGALKYQARSWYKEGDHTANLANEDISSANGYHSMGKGGYSLSDLHYSVNAVRSTSETVADIDEYTDQTLFKPATDSGESSGDVRFNGAGGGNVIKSNVTRGNVYFNGGGIANVILHSSQFGNTEFNGGGAANVIVKSGEEGDLTFRGAGLANVLVHQSKQGKMDVYAGGAVNVLVRIGDGQYLAHLLAYGNISVHKGNGNSRVVMLGGYNTHTQIGSGNGLWLAAGGFNVMTQVGKGDVASVLAGGANVLTKVGDGDLTAGMLGGANVITHISGDNETSNTTAVALGGANILTKKGKGNTLAVMGGGANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGIMLGVGNVLTHVGDGQTLGVMGAAGNIFTKVGDGTSIAVMIGAGNIFTHVGEGNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATKVGNGTTLAAMVGNANIFTHVGSGSTFAAMIGQANIMTKVGNDLTAALMVGKANIYTHVGDGTSLGIFAGEVNVMTKIGNGTTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKVGDDFMGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTTVGLLISDIGNVMTHVGDGTTIGIAKGKANIITKVGDGLGVNVAWGQANVFTQVGDGDRYNFAKGEANIITKVGDGKEVSVVQGKANIITHVGNGDDYTGAWGKANVITKVGNGRNVVLAKGEANIVTQVGDGDSFNALWSKGNIVTKVGDGMQVTAAKGKANITTTVGDGLSVTAAYGDANINTKVGDGVSVNVAWGKYNINTKVGDGLNVAVMKGKANANIHVGDGLNINASYAQNNVAIKVGNGDFYSLAVASSNTSSNKLSALFDNIKQTLLGVGGSQAINYLVQGDEASSSGTQKGRGAIATPEITKLDGFQMEAIEEVGSDLGDSLTGSVTKVDTPDLNKMQNALDVDGSSDQTQAPNLIVNGDFEQGDRGWKSTHGVEASYSGNVYGVNGEGHGARVTELDTYTNTSLYQDLTDLTEGEVIAVSFDFAKRAGLSNNEGIEVLWNGEVVFSSSGDASAWQQKTLKLTAHAGSNRIEFKGTGHNDGLGYILDNVVAKSESSQQANAVSEHATQNQASQNALSDKERAEADRQRLEQEKQKQLDAVAGSQSQLESTDQQALGNNGQAQRDAVKEESEAVTAELTKLAQGLDVLDGQATHTGESGDQWRNDFAGGLLDGVQSQLDDAKQLANDKIAAAKQTQSDNNSKVKESVAKSEAGVAQGEQNRAGAEQDIAEAKADAETRKADAVAKSNDAKQAESDAHSAANDAQSRGDRDAMNAENKANQAQNDAKGTKQNEGDRPDREGVAGSGLSGNAHSVEGAGETGSHITTDSQTNADGRFSEGLSEQEQEALEGATNAVNRLQINAGIRGKNSGSTITSMFTETNSDSIVVPTTASQDVVRKEIRISGVNLEGLGEASHDSAESLVAARAEKVANLYRWLDTDNDVATDKYVPVPGFERVDVDVSDEVKQRMIQSMSGYIEHTDNQVPKDQAEALATLFVESTLDYDWDKRVEFLTKLESYGYSFEAPHAEKSIVSFWSGKNFKQYRDILDNAQTDGKKVVYDIDVKGNAFAIDLNKHLMRWGGLFLDPDNAEQNQLKSSIDAATFSNTGFWSSVYATGAQNDVYVIAEGGVRLGNYFWNVELPALRQLQREGLVGEIRLLDKPVSEYKDLPADQIGRRLTDAGVAVKVRFDALSHERQAELLADNPDGYKADTLVELDVKLSAIDSMLRESLPFYSLRTERNLLVQEGEEGFEVRSWPGIDGKSKTILLDNPEDAAQQKSIERFILANFDNFEQMPDELFLVDNKVLSHHDGRTRIIAQKEDGAWTYNTNVELMSVTELLDAAHVNGKVRGDSYQQVIDALTEYHASTVEHADYELESVEKLLNLRKQIEGYVLGHPDSGRVEAMNSLLNQVNSRLEEVSVLAVSEQSIKAHDSFSRLYDQLDNANLKESKHLYLDGNGDFVTKGKGNLATIDQLGGSDAVLEKVKAAVTHEYGQVVADTIFARLSANDLAKDGKGIDIAGLNKVHQAIEQHMSPVSATMYIWKPSDHSTLGHAALQIGQGRTQLEGQAAADFNKQNYVSWWPLGSKSSNIRNIFNVATEDQPDLKLRWSDFSQPAHQNDTLEHDMASEENDGFGLKDGETKLKRFIEKLNAAKGIDASYKDASEGYASVLLGNPDMLASTGIPAHVFQPFVDQWNDTSYDMMDVANRFAEELQKQAQASGDPALVEKRIDNVVRLFAERALEEIEAFKASQADEGRVFRINLEGLDVAAMQAEWNRLSNDPDARYQLLTKNCSSTVAKVLKAGGADKLIGHTWRPKFGVWTPTELFNFGQALQEAQLEIAAKKQSHQVTDVLDALSGNEKHKENVTIENDGTPPRDKESLSPLTRFLNNELYGEKDARRKIGEITQTLLDHAVENGESQKVTLKGEAGRLTGYYHQGAASSEGETSATSGKVVLFLHGSGSSAEEQASAIRNHYQKQGIDMLAVNLRGYGESDGGPSEKGLYQDARTMFNYLVNDKGIDPSNIIIHGYSMGGPIAADLARYAAQNGQAVSGLLLDRPMPSMTKAITAHEMANPAGIVGAIAKAVNGQFSVEKNLKGLPKETPILLLTDNEGLGEEGEKLRAKLAIAGYNVTGEQTFYGHEASNRLMGQYADQIVSGLFNAEQAAVEAGEVLKGLEKDFKRYGDALKPDTSVPGKSKDIRTTKDFLNGYKNDHAKEIVDGFRSDMSIKQLVDLFVKGNWSAEQKGALAWEIESRALKVTFQNKSEKYNRLFREIASAGVVDAKATEQLAPQLMLLNLSNDGFGGRCDPLSKLVLVAKQLENDGQVGVARQLLEKMYSAAAVLSNPTLYSDSEKANASKLLSSLAAIHAKNPMHDTSMKVWQEKLEGKQALTVNGVVEKITDASANGKPVLLELDAPGHAMAAWAKDSGDDRVYGFYDPNAGIVEFSSAEKFGDYLTRFFGKSDLDMAQSYKLGKNDAGEAIFNRVVVMDGNTLASYKPTFGDKTTMQGILDLPVFDATPIKKPTGGVASDLEALGDKTKVVVDLAQIFTVQELKERAKVFAKPIGASYQGILDQLDLVHQAKGRDQIAASFELNKKINDYIAEHPTSGRNQALTQLKEQVTSALFIGKMQVAQAGIDAIAQTRPELAARIFMVAIEEANGKHVGLTDMMVRWANEDPYLAPKHGYKGETPSDLGFDAKYHVDLGEHYADFKQWLETSQSNGLLSKATLDESTKTVHLGYSYQELQDLTGAESVQMAFYFLKEAAKKADPISGDSAEMILLKKFADQSYLSQLDSDRMDQIEGIYRSSHETDIDAWDRRYSGTGYDELTNKLASATGVDEQLAVLLDDRKGLLIGEVHGSDVNGLRFVNEQMDALKKQGVTVIGLEHLRSDLAQPLIDRYLATGVMSSELSAMLKTKHLDVTLFENARANGIRIVALDANSSARPNVQGTEHGLMYRAGAANNIAVEVLQNLPDGEKFVAIYGKAHLQSHKGIEGFVPGITHRLDLPALKVSDSNQFTVEQDDVSLRVVYDDVANKPKITFKDSLSGANTALHNQNVNDWERVVVTPTADGGESRFDGQIIVQMENDDVVAKAAANLAGKHPESSVVVQIDSDGNYRVVYGDPSKLDGKLRWQLVGHGRDDSESNNTRLSGYSADELAVKLAKFQQSFNQAENINNKPDHISIVGCSLVSDDKQKGFGHQFINAMDANGLRVDVSVRSSELAVDEAGRKHTKDANGDWVQKAENNKVSLSWDEQGEVVAKDERIRNGIAEGDIDLSRIGVSDVDEPARGAIGDNNDVFDAPEKRKAETETSSSSANNKLSYSGNIQVNVGDGEFTAVNWGTSNVGIKVGTGGFKSLAFGDNNVMVHIGNGESKHSFDIGGYQALEGAQMFIGNRNVSFNLGRSNDLIVMMDKSIPTPPLVNPFDGAARISGVLQSIATSGEGQDWLAAQEQQWTLSGAKKFVKDMSGLDQSSSVDYTSLVELDSQNERSSRGLKHDAEAALNKQYNQWLSGNSDSDTSKLSRADKLRQANEKLAFNFAVGGQGADIQVTTGNWNFMFGDNIQSILDTNLGSLFGLMTQQFSATGQAKTTFTYTPEDLPRQLKNKLLGQLAGVGAETTLADIFGVDYTASGQIVSRNGEAVDGVAILKEMLEVIGEFSGDQLQAFVDPAKLLDSLKSGINMGADGIKSFAETHGLKEKAPEEEEDNSSVSVNGASVNSAQGATVADGSTETAETPDRAFGFNSLNLPNLFATIFSQDKQKEMKSLVENLKENLTADLLNMKEKTFDFLRNSGHLQGDGDINISLGNYNFNWGGDGKDLGAYLGDNNNFWGGRGDDVFYATGTSNIFTGGEGNDMGVLMGRENMMFGGDGNDTAVVAGRINHVFLGAGDDQSFVFGEGGEIDTGSGRDYVVTSGNFNRVDTGDDQDYSVTIGNNNQVELGAGNDFANVFGNYNRINASAGNDVVKLMGYHAVLNGGEGEDHLIAAAISKFSQFNGGEGRDLMVLGGYQNTFKGGTDVDSFVVSGDVIDNLVEDIRSEDNIVFNGIDWQKLWFERSGYDLKLSILRDPASDSDQAKFEHIGSVTFSDYFNGNRAQVIIAMGEKDATGEREYTTLSESAIDALVQAMSGFDPQAGDNGFMDNLDSKSRVAITTAWADVVHKKGITV | ||||||
Chain | PRO_0000455660 | 2296-2901 | N-epsilon-fatty acyltransferase F2 | |||
Sequence: GFEVRSWPGIDGKSKTILLDNPEDAAQQKSIERFILANFDNFEQMPDELFLVDNKVLSHHDGRTRIIAQKEDGAWTYNTNVELMSVTELLDAAHVNGKVRGDSYQQVIDALTEYHASTVEHADYELESVEKLLNLRKQIEGYVLGHPDSGRVEAMNSLLNQVNSRLEEVSVLAVSEQSIKAHDSFSRLYDQLDNANLKESKHLYLDGNGDFVTKGKGNLATIDQLGGSDAVLEKVKAAVTHEYGQVVADTIFARLSANDLAKDGKGIDIAGLNKVHQAIEQHMSPVSATMYIWKPSDHSTLGHAALQIGQGRTQLEGQAAADFNKQNYVSWWPLGSKSSNIRNIFNVATEDQPDLKLRWSDFSQPAHQNDTLEHDMASEENDGFGLKDGETKLKRFIEKLNAAKGIDASYKDASEGYASVLLGNPDMLASTGIPAHVFQPFVDQWNDTSYDMMDVANRFAEELQKQAQASGDPALVEKRIDNVVRLFAERALEEIEAFKASQADEGRVFRINLEGLDVAAMQAEWNRLSNDPDARYQLLTKNCSSTVAKVLKAGGADKLIGHTWRPKFGVWTPTELFNFGQALQEAQLEIAAKKQSHQVTDVLDAL | ||||||
Chain | PRO_0000455661 | 2902-3400 | ABH effector region toxin F5 | |||
Sequence: SGNEKHKENVTIENDGTPPRDKESLSPLTRFLNNELYGEKDARRKIGEITQTLLDHAVENGESQKVTLKGEAGRLTGYYHQGAASSEGETSATSGKVVLFLHGSGSSAEEQASAIRNHYQKQGIDMLAVNLRGYGESDGGPSEKGLYQDARTMFNYLVNDKGIDPSNIIIHGYSMGGPIAADLARYAAQNGQAVSGLLLDRPMPSMTKAITAHEMANPAGIVGAIAKAVNGQFSVEKNLKGLPKETPILLLTDNEGLGEEGEKLRAKLAIAGYNVTGEQTFYGHEASNRLMGQYADQIVSGLFNAEQAAVEAGEVLKGLEKDFKRYGDALKPDTSVPGKSKDIRTTKDFLNGYKNDHAKEIVDGFRSDMSIKQLVDLFVKGNWSAEQKGALAWEIESRALKVTFQNKSEKYNRLFREIASAGVVDAKATEQLAPQLMLLNLSNDGFGGRCDPLSKLVLVAKQLENDGQVGVARQLLEKMYSAAAVLSNPTLYSDSEKAN | ||||||
Chain | PRO_0000455662 | 4091-5206 | Cysteine protease domain-containing toxin F3 | |||
Sequence: GANTALHNQNVNDWERVVVTPTADGGESRFDGQIIVQMENDDVVAKAAANLAGKHPESSVVVQIDSDGNYRVVYGDPSKLDGKLRWQLVGHGRDDSESNNTRLSGYSADELAVKLAKFQQSFNQAENINNKPDHISIVGCSLVSDDKQKGFGHQFINAMDANGLRVDVSVRSSELAVDEAGRKHTKDANGDWVQKAENNKVSLSWDEQGEVVAKDERIRNGIAEGDIDLSRIGVSDVDEPARGAIGDNNDVFDAPEKRKAETETSSSSANNKLSYSGNIQVNVGDGEFTAVNWGTSNVGIKVGTGGFKSLAFGDNNVMVHIGNGESKHSFDIGGYQALEGAQMFIGNRNVSFNLGRSNDLIVMMDKSIPTPPLVNPFDGAARISGVLQSIATSGEGQDWLAAQEQQWTLSGAKKFVKDMSGLDQSSSVDYTSLVELDSQNERSSRGLKHDAEAALNKQYNQWLSGNSDSDTSKLSRADKLRQANEKLAFNFAVGGQGADIQVTTGNWNFMFGDNIQSILDTNLGSLFGLMTQQFSATGQAKTTFTYTPEDLPRQLKNKLLGQLAGVGAETTLADIFGVDYTASGQIVSRNGEAVDGVAILKEMLEVIGEFSGDQLQAFVDPAKLLDSLKSGINMGADGIKSFAETHGLKEKAPEEEEDNSSVSVNGASVNSAQGATVADGSTETAETPDRAFGFNSLNLPNLFATIFSQDKQKEMKSLVENLKENLTADLLNMKEKTFDFLRNSGHLQGDGDINISLGNYNFNWGGDGKDLGAYLGDNNNFWGGRGDDVFYATGTSNIFTGGEGNDMGVLMGRENMMFGGDGNDTAVVAGRINHVFLGAGDDQSFVFGEGGEIDTGSGRDYVVTSGNFNRVDTGDDQDYSVTIGNNNQVELGAGNDFANVFGNYNRINASAGNDVVKLMGYHAVLNGGEGEDHLIAAAISKFSQFNGGEGRDLMVLGGYQNTFKGGTDVDSFVVSGDVIDNLVEDIRSEDNIVFNGIDWQKLWFERSGYDLKLSILRDPASDSDQAKFEHIGSVTFSDYFNGNRAQVIIAMGEKDATGEREYTTLSESAIDALVQAMSGFDPQAGDNGFMDNLDSKSRVAITTAWADVVHKKGITV |
Keywords
- PTM
Family & Domains
Features
Showing features for repeat, compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 101-118 | RtxA 1 | ||||
Sequence: GAAGGVSIDHLGNNGDVS | ||||||
Repeat | 121-138 | RtxA 2 | ||||
Sequence: GAAAYNGITRKGLSGNVT | ||||||
Repeat | 141-157 | RtxA 3 | ||||
Sequence: GAGGYNALWHETNQGNL | ||||||
Repeat | 161-184 | RtxA 4 | ||||
Sequence: GAGAGNKLDRTWFNRYQGSRGDVT | ||||||
Repeat | 187-204 | RtxA 5 | ||||
Sequence: GAGAANSISSRVETGNIT | ||||||
Repeat | 207-224 | RtxA 6 | ||||
Sequence: GAGADNHLVRKGKVGDIT | ||||||
Repeat | 255-272 | RtxA 7 | ||||
Sequence: GVGGYNSLYSDVAHGDIH | ||||||
Repeat | 275-291 | RtxA 8 | ||||
Sequence: GGGAYNTITRKGSGSSF | ||||||
Repeat | 584-601 | RtxA 9 | ||||
Sequence: GAGGGNVIKSNVTRGNVY | ||||||
Repeat | 604-620 | RtxA 10 | ||||
Sequence: GGGIANVILHSSQFGNT | ||||||
Repeat | 624-641 | RtxA 11 | ||||
Sequence: GGGAANVIVKSGEEGDLT | ||||||
Repeat | 644-658 | RtxA 12 | ||||
Sequence: GAGLANVLVHQSKQG | ||||||
Repeat | 741-753 | RtxA 13 | ||||
Sequence: AGGANVLTKVGDG | ||||||
Repeat | 759-771 | RtxA 14 | ||||
Sequence: MLGGANVITHISG | ||||||
Repeat | 782-798 | RtxA 15 | ||||
Sequence: ALGGANILTKKGKGNTL | ||||||
Repeat | 801-816 | RtxA 16 | ||||
Sequence: MGGGANVLTHVGDGTT | ||||||
Repeat | 820-835 | RtxA 17 | ||||
Sequence: MVGGANILTKVGNGDT | ||||||
Repeat | 841-855 | RtxA 18 | ||||
Sequence: GVGNVLTHVGDGQTL | ||||||
Repeat | 858-875 | RtxA 19 | ||||
Sequence: MGAAGNIFTKVGDGTSIA | ||||||
Repeat | 877-891 | RtxA 20 | ||||
Sequence: MIGAGNIFTHVGEGN | ||||||
Repeat | 896-910 | RtxA 21 | ||||
Sequence: MGGLGNVFTKVGNGD | ||||||
Repeat | 915-932 | RtxA 22 | ||||
Sequence: MVAEANVFTHIGDGMSVA | ||||||
Repeat | 934-950 | RtxA 23 | ||||
Sequence: MLAKGNVATKVGNGTTL | ||||||
Repeat | 972-984 | RtxA 24 | ||||
Sequence: MIGQANIMTKVGN | ||||||
Repeat | 991-1006 | RtxA 25 | ||||
Sequence: MVGKANIYTHVGDGTS | ||||||
Repeat | 1031-1043 | RtxA 26 | ||||
Sequence: GKANIMTHVGDGL | ||||||
Repeat | 1067-1079 | RtxA 27 | ||||
Sequence: AAAKANVVTHVGD | ||||||
Repeat | 1087-1102 | RtxA 28 | ||||
Sequence: AGKGNILTKVGEGTTV | ||||||
Repeat | 1110-1122 | RtxA 29 | ||||
Sequence: GNVMTHVGDGTTI | ||||||
Repeat | 1125-1142 | RtxA 30 | ||||
Sequence: AKGKANIITKVGDGLGVN | ||||||
Repeat | 1145-1159 | RtxA 31 | ||||
Sequence: WGQANVFTQVGDGDR | ||||||
Repeat | 1163-1179 | RtxA 32 | ||||
Sequence: AKGEANIITKVGDGKEV | ||||||
Repeat | 1184-1199 | RtxA 33 | ||||
Sequence: GKANIITHVGNGDDYT | ||||||
Repeat | 1201-1217 | RtxA 34 | ||||
Sequence: AWGKANVITKVGNGRNV | ||||||
Repeat | 1220-1236 | RtxA 35 | ||||
Sequence: AKGEANIVTQVGDGDSF | ||||||
Repeat | 1242-1256 | RtxA 36 | ||||
Sequence: KGNIVTKVGDGMQVT | ||||||
Repeat | 1258-1275 | RtxA 37 | ||||
Sequence: AKGKANITTTVGDGLSVT | ||||||
Repeat | 1296-1313 | RtxA 38 | ||||
Sequence: AWGKYNINTKVGDGLNVA | ||||||
Repeat | 1315-1332 | RtxA 39 | ||||
Sequence: MKGKANANIHVGDGLNIN | ||||||
Compositional bias | 1606-1627 | Polar residues | ||||
Sequence: SQQANAVSEHATQNQASQNALS | ||||||
Region | 1606-1682 | Disordered | ||||
Sequence: SQQANAVSEHATQNQASQNALSDKERAEADRQRLEQEKQKQLDAVAGSQSQLESTDQQALGNNGQAQRDAVKEESEA | ||||||
Compositional bias | 1628-1645 | Basic and acidic residues | ||||
Sequence: DKERAEADRQRLEQEKQK | ||||||
Compositional bias | 1647-1670 | Polar residues | ||||
Sequence: LDAVAGSQSQLESTDQQALGNNGQ | ||||||
Compositional bias | 1738-1752 | Polar residues | ||||
Sequence: IAAAKQTQSDNNSKV | ||||||
Region | 1738-1895 | Disordered | ||||
Sequence: IAAAKQTQSDNNSKVKESVAKSEAGVAQGEQNRAGAEQDIAEAKADAETRKADAVAKSNDAKQAESDAHSAANDAQSRGDRDAMNAENKANQAQNDAKGTKQNEGDRPDREGVAGSGLSGNAHSVEGAGETGSHITTDSQTNADGRFSEGLSEQEQEA | ||||||
Compositional bias | 1774-1801 | Basic and acidic residues | ||||
Sequence: EQDIAEAKADAETRKADAVAKSNDAKQA | ||||||
Compositional bias | 1867-1886 | Polar residues | ||||
Sequence: ETGSHITTDSQTNADGRFSE | ||||||
Region | 2377-2461 | Membrane localization region (MLD) | ||||
Sequence: ELMSVTELLDAAHVNGKVRGDSYQQVIDALTEYHASTVEHADYELESVEKLLNLRKQIEGYVLGHPDSGRVEAMNSLLNQVNSRL | ||||||
Region | 2537-2901 | Rho inactivation domain (RID) | ||||
Sequence: EYGQVVADTIFARLSANDLAKDGKGIDIAGLNKVHQAIEQHMSPVSATMYIWKPSDHSTLGHAALQIGQGRTQLEGQAAADFNKQNYVSWWPLGSKSSNIRNIFNVATEDQPDLKLRWSDFSQPAHQNDTLEHDMASEENDGFGLKDGETKLKRFIEKLNAAKGIDASYKDASEGYASVLLGNPDMLASTGIPAHVFQPFVDQWNDTSYDMMDVANRFAEELQKQAQASGDPALVEKRIDNVVRLFAERALEEIEAFKASQADEGRVFRINLEGLDVAAMQAEWNRLSNDPDARYQLLTKNCSSTVAKVLKAGGADKLIGHTWRPKFGVWTPTELFNFGQALQEAQLEIAAKKQSHQVTDVLDAL | ||||||
Region | 2998-3113 | ABH effector region | ||||
Sequence: VVLFLHGSGSSAEEQASAIRNHYQKQGIDMLAVNLRGYGESDGGPSEKGLYQDARTMFNYLVNDKGIDPSNIIIHGYSMGGPIAADLARYAAQNGQAVSGLLLDRPMPSMTKAITA | ||||||
Domain | 4111-4295 | Peptidase C80 | ||||
Sequence: PTADGGESRFDGQIIVQMENDDVVAKAAANLAGKHPESSVVVQIDSDGNYRVVYGDPSKLDGKLRWQLVGHGRDDSESNNTRLSGYSADELAVKLAKFQQSFNQAENINNKPDHISIVGCSLVSDDKQKGFGHQFINAMDANGLRVDVSVRSSELAVDEAGRKHTKDANGDWVQKAENNKVSLSW | ||||||
Region | 4333-4362 | Disordered | ||||
Sequence: GAIGDNNDVFDAPEKRKAETETSSSSANNK | ||||||
Region | 4738-4779 | Disordered | ||||
Sequence: LKEKAPEEEEDNSSVSVNGASVNSAQGATVADGSTETAETPD | ||||||
Compositional bias | 4749-4779 | Polar residues | ||||
Sequence: NSSVSVNGASVNSAQGATVADGSTETAETPD |
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length5,206
- Mass (Da)556,341
- Last updated2018-07-18 v1
- Checksum85BB805918FD1C5A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1606-1627 | Polar residues | ||||
Sequence: SQQANAVSEHATQNQASQNALS | ||||||
Compositional bias | 1628-1645 | Basic and acidic residues | ||||
Sequence: DKERAEADRQRLEQEKQK | ||||||
Compositional bias | 1647-1670 | Polar residues | ||||
Sequence: LDAVAGSQSQLESTDQQALGNNGQ | ||||||
Compositional bias | 1738-1752 | Polar residues | ||||
Sequence: IAAAKQTQSDNNSKV | ||||||
Compositional bias | 1774-1801 | Basic and acidic residues | ||||
Sequence: EQDIAEAKADAETRKADAVAKSNDAKQA | ||||||
Compositional bias | 1867-1886 | Polar residues | ||||
Sequence: ETGSHITTDSQTNADGRFSE | ||||||
Compositional bias | 4749-4779 | Polar residues | ||||
Sequence: NSSVSVNGASVNSAQGATVADGSTETAETPD |
Keywords
- Technical term