| IED ID | IndEnz0002015276 |
| Enzyme Type ID | protease015276 |
| Protein Name |
Protein adenylyltransferase and cysteine protease IbpA HMW IgBP p120 Cleaved into: Protein p76 IgBP 76 kDa antigen Includes: Protein adenylyltransferase IbpA EC 2.7.7.n1 AMPylator IbpA ; Cysteine protease IbpA EC 3.4.22.- |
| Gene Name | ibpA p76 HSM_1489 |
| Organism | Histophilus somni (strain 2336) (Haemophilus somnus) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pasteurellales Pasteurellaceae Histophilus Histophilus somni (Haemophilus somnus) Histophilus somni (strain 2336) (Haemophilus somnus) |
| Enzyme Sequence | MNKNCYKLIFSKTRGCLVPVAECITSAVDSGSSDSVVVSEKTDEEDRQGSIEDYRLSNVCLSVKTFLNPVSSALCLNWKSVSVLLLSMVAAPNFAQSAEEAAKAEKTPKLTEIQNGNDGIQLETKNQNIGVGAGTTENNHPTKLYKTENNVIVIDIAKPNDKGISDNRFQKFNIPNGAVFKNNKDQQRSELVGYLEGNKNLADKEAKVILNQVTGSELSQIKGALEILGTKADLVIANQHGINLNGVQTINAGRFVATTSKLIDPNKMEFDVTQGTVTIDVNGFATDNLPYLDIVAKKIEQKGTIGNKEKEKNKTSETEITFIAGKGKIKYNIENDGKTKLEVQKDSNTSQPSDKEEVAITGASTGAMHGKSIKLIVTEQGAGVKHDGIILSENDIKIESNKGDIDLGDKLQAKNEISLNNAKRITIANEITADKSITITADDVKLKNNKEASATEEAKLKGKGKLASKKVKVEAKKSLVLDDETKVVATDLELKSQTLTNQGRIYGNKVKIDTDKLVNKKEIYAEDNLDITTKGKTVTVSVNKDNKRKADVKEETVADLDVGFENTGTIESKSKAKLTFKDNTSFVSKGNKFIKAKDELTIDAQNVVISENDELQTTARLTINAAGNVVNNGLLASGKTLTINAKQGSIYNEKGILGAREQLTLSAKGNNKETEGNIINGADSLLHSEGKMELDAENTVYNLGNIFAKSDLTVKANELINDVKLSGSITKKSPYSVLNRYRRSDIASHGWHNNDYRLWINPIEFEKAEVKVEKAGLIRAEGNFKFEGKKGDNQQDATLTNHGVINVKNTFEAQNAKVVNNMKAYQANLLTEFFKQKQDITFNYQPRARLFLSALSGQAERKFNSLEELFDGLFSEQPITNSSSYYADNSQAVHLLEEIKSPTFQKAMTLVFGANWKNEDHKKLSQRWKEFKEKQDAHFDYRPTDKAKILAQRINGKIDELKNGSTGGFSESERITVGQHKFDLSKVEFRSEVNRKENLNNSNVDLSALSDLLSIPNLFVDNSVQLDKTVDKNIEIDEEDEFLLKPHTGEEPDLLNENELSENGKFLDKLLGEIGEKTYIREVSDDWERDPDEPDEPDYKTESRLETRDRFDTLPSEVQDKLRQKFNEYKEKAQQKRQAEALQAKTKNEQLQSDLETGYKEEEKRQAKNDLEKQAELQQLDQQEKEKLAKEKELQGKINEEKQQEALAKQKQEQQKQADAKAKIEEEKRLEEYRKELAKDHQIEEALSKNQFLKEVDDTRPKVETDPLYRTKLQYINQDEYFGSKYFLNKVGSSTDAGKKVAVIGDNYLEHQLITKSIEKKVDNHLALKYQVNDAQLVKKLIDNSYFESKELGLKVGEALTKEQQNQLKQDIVWYVKANINNKEVLLPQVYFANKTLRDAEKFKGLGDALIRANEINLKTRDVLNSGTISGKNIDIEAENKIKNRGDILSEESTRLVGHKGIDNTARSFVNGNGDVEVQRASIRTEGHLHLEADEDSDINSKGSDIKGKTGFVKARNFNTTDTHRTEHSVEKGRIFSKKGEILGYRKESTQKAISVGSNTEFDHVHFAIKNDVNQEGSKIKAKVVTGVVQGDYNTKAGRNAQQTERYIRLDQEYSSGHISGAGFTVSHERDSQNGEKTNIGGASSNTGTGFTLGGSFSETREKETSLTHTNSDLQVDHGILHVLKKAEIGGVDINKHKFTGKAVEEDEAKAEQQAKAKAAPDATDNAAQKEEPKFKVLSQSEVDDLMTEKSANDLFNKYKKVKEDEGFELSAKEITSNKQKDEYHLDSERSVLKFGIETEGHSAIADAVSHVAKEIVEAQRGVKQDGTVALQHISDVANIVTGELVGGSSKFGFERNYETNKVKETSDIRTKIAGNITLSAHGGNLQLKNVESDANSKLTLQAKRNVDILDGETTRESTERQSRQKFAFGINSGCSVMSGGCNGGVSGSVDGNESFTTEKSVTHNNSLLRAKNLKIAAGKDLNLISSNIKADHLDLNIKGKTNIVSKQDSFDRLYRGFDFSASAGAALSSSTLVKGNGSFGAGYTHEVENRKLLNQQAGIVANRITGQIKDLDLVAAHFINKDENSGFRVSGNVTSQQLNDSHHKDGGSVGVSVGINERGASSFNVRGGRAEQKHYDAVQKSVISGINLKDNNVTGEIVDDLSKAKTVTRDDVYASTQFNFEVADLVELGEKAKSKLQSKFSKAVNNDAEQPTTTRISSEDVVEMVDNPLYGSNADVRKLRTLDEVGEGYSTLGDQNANKGRKLPNGSDDIYSLLGKVKVSGDEPVYDKVSAEGAYDLLGDSNANKGRTLRNNSDDLYSTVGDANSDISRIRSNVYDEIAAGPYSLLGRTKAAEEHIYEQIGEGPYSLLGNGSAVRNRTLGGESNSTYSTVGDANSDISRIRSNVYDEIVAGPYSLLGKPKAAEEHIYEQIGEGPYSLLGNGSAVRNRTLGGESDSPYSTVGDANSDISRIRSNVYDEIVAGPYSLLGRTKAAEEHIYEQIGEGPYSLLGNGSAVRNRTLGGESDSPYSLLGGEGTRNKVLADTIESIYSTLSRPQASSNLEMVDNPLYDSVRRSASDQLPELPTVRNLLNSDTEAGNGTYSEITSRTRNANDPLPPLPNEFRTRLSQGADLADHVYDTIGSIYSVLSKPKASSNLEMVDNPLYGSVRRAAGDQLPELPTVKTLLNKVEEVGNEIYSEITSKTRSANDPLPALPNFRLTQEVDTADHIYADINDVVNRANKAKRDLPATPEATPKVAVDGGDYATIGEVSPLQPRASRQQGSSDYEEIPLPQETAPQKTSPVKRTSAEGEDGYATIAEVLQPRAAKGQVSDYETIPLDEPSQAAVRTERSAVEGDYAEITSPSIQPRSARGQSGGEEFEPFPSEFSSEPQSPKRALPAENAVVNELGNELKARLKSKEDQANPAKAEVSEPIYATLDKSPEGLARAKAKGDEAAAANPIVKTRVEDDVAPELPARPSNLSDSISNETIAENGQSVALGTPKSAVAESNRNNNGNQKLQSEGAEGVSPKTKSEDKSWFAKVKDFFFAKSNKSQAKEAKSEQETVSKPNYDSLEDDLNLKNLLALEDKRGSSFEENVLKNPEFLAEAREIAKKYIPEATIKQMGNSPEFDEILTEGAKKVEKRINDALTFKPSVDEFNEIQGLVKNIQKGSAVDDLNAQTLAITEALADTSKTIQRNPKLKEEVQGAIEEFLKSSQGKELTVEMIEKLNHGLRPDEGSDRLLYKKENLTKENAVFSSPQASKIQLNETVDFINQAIKQNVEPSVLAGLVYQRLIAYHPFAEGNGRMARVVVNKILLDAGYPPFTKFSSEFETQIIPQTKATAKSATSAEVVKEFLTELGKKSSPQEGGANNQNGQATSPVTLKSKDVSEVENTQSADSLTIKQPEQGKAGGQLPSVPKVETSVNEVAPLSSVPAELKDAAGGNKKAAEKSEGATGVEKEKTTLFQRVKQFFTGSKSGAKPVAGDETANKVNYQDLEDNLNLKGLISLEDDRNANFESNVLKNEKFLDEAREISKKSIPEATVKQMSHLPEFDDILTEGAKKVESRINKAITFRPSVEEFSEIQDLVKTLPKTKVIEDLSTKTNEITEALAATSKTIQRTPELKEQLKTAIEDFLQNSQGKPLTVQMIENLNHGLRPDEGEGRLLYKKENLTKENAVFSSPEAAKIQLAETVDFINRAKNEGIEPSVVGALVYQRLIAYHPFAEGNGRMARVIVNKILLDAGYPAFTKFSDEFEPQIIPQTKASTKSATSSEVVVEFLKELAKKGSKEDNEQNLEKTDRTSTDLTESAVENSAALSSGTVRSATVSETVTETEQAKAKPVSDLVSSKDLVEQQRTVLQRIQDQFQPLKVKSKIDAVRSSVEEFGGEVSFKFAQSKGEVYKEIVKHIETQNGVCESTCAHWIAKNVNPTDENFFNTLYEGGKKGHLKKETIDSIKKLQTEFINSGSATQQFKLTDSWLQEQGVVPKEKKVADFVRRDEVSGTVSKNDVSSLVKAILDTGDDTAGVKKISINLEGGSHTVSAAVDGSKVTFFDPNFGEMTFPTHQQFENWLKNAFWQKSGYAGKQEGRRFFNVVNYKKNN |
| Enzyme Length | 4095 |
| Uniprot Accession Number | Q06277 |
| Absorption | |
| Active Site | ACT_SITE 3910; /note=For cysteine protease activity; /evidence=ECO:0000255; ACT_SITE 4033; /note=For cysteine protease activity; /evidence=ECO:0000255; ACT_SITE 4048; /note=For cysteine protease activity; /evidence=ECO:0000255 |
| Activity Regulation | |
| Binding Site | BINDING 3728; /note=ATP; BINDING 3757; /note=ATP |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.n1; Evidence={ECO:0000269|PubMed:19362538, ECO:0000269|PubMed:20622875}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.n1; Evidence={ECO:0000269|PubMed:19362538, ECO:0000269|PubMed:20622875}; |
| DNA Binding | |
| EC Number | 2.7.7.n1; 3.4.22.- |
| Enzyme Function | FUNCTION: Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific tyrosine residue of host Rho GTPases RhoA, Rac and Cdc42. The resulting AMPylation inactivates Rho GTPases, thereby inhibiting actin assembly in infected cells. Probably also acts as a cysteine protease, which may play a central role after invasion of host cell and in virulence. Possible member (with IbpB) of a 2 partner secretion. Probably able to bind bovine epithelial cells (host cells). May participate in the formation of fibrils at the surface of the bacteria. {ECO:0000269|PubMed:12631474, ECO:0000269|PubMed:19362538, ECO:0000269|PubMed:20622875, ECO:0000269|PubMed:9317034}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 3670..3671; /note=ATP; NP_BIND 3722..3724; /note=ATP |
| Features | Active site (3); Beta strand (3); Binding site (2); Chain (2); Coiled coil (1); Compositional bias (11); Domain (2); Erroneous initiation (1); Helix (16); Mutagenesis (8); Nucleotide binding (2); Region (20); Repeat (12); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;ATP-binding;Cell outer membrane;Coiled coil;Hydrolase;Membrane;Multifunctional enzyme;Nucleotide-binding;Nucleotidyltransferase;Protease;Reference proteome;Repeat;Secreted;Signal;Thiol protease;Transferase;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16169703, ECO:0000269|PubMed:9317034}. Note=High molecular weight-immunoglobulin binding protein IbpA, and probably other shorter forms.; SUBCELLULAR LOCATION: [Protein p76 IgBP]: Cell outer membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: The long form of the protein is probably processed, and/or the transcript may be subject to differential translational initiation. |
| Signal Peptide | SIGNAL 1..97; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3N3U; 4ITR; 6SIU; |
| Mapped Pubmed ID | 32632184; |
| Motif | |
| Gene Encoded By | |
| Mass | 450,060 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:54288; RHEA:54292 |
| Cross Reference Brenda |