VOPS_VIBPA
ID VOPS_VIBPA Reviewed; 387 AA.
AC Q87P32;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein adenylyltransferase VopS;
DE EC=2.7.7.n1 {ECO:0000269|PubMed:19039103, ECO:0000269|PubMed:20410310};
DE AltName: Full=AMPylator VopS;
DE AltName: Full=Vibrio outer protein S;
GN Name=vopS; OrderedLocusNames=VP1686;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
RN [2]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18347050; DOI=10.1128/iai.01704-07;
RA Casselli T., Lynch T., Southward C.M., Jones B.W., DeVinney R.;
RT "Vibrio parahaemolyticus inhibition of Rho family GTPase activation
RT requires a functional chromosome I type III secretion system.";
RL Infect. Immun. 76:2202-2211(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP HIS-348.
RX PubMed=19039103; DOI=10.1126/science.1166382;
RA Yarbrough M.L., Li Y., Kinch L.N., Grishin N.V., Ball H.L., Orth K.;
RT "AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and
RT downstream signaling.";
RL Science 323:269-272(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 75-387, FUNCTION, CATALYTIC
RP ACTIVITY, AND MUTAGENESIS OF ARG-299; LEU-308; HIS-348; PHE-350; ASP-352;
RP ASN-354 AND ARG-356.
RX PubMed=20410310; DOI=10.1074/jbc.m110.114884;
RA Luong P., Kinch L.N., Brautigam C.A., Grishin N.V., Tomchick D.R., Orth K.;
RT "Kinetic and structural insights into the mechanism of AMPylation by VopS
RT Fic domain.";
RL J. Biol. Chem. 285:20155-20163(2010).
CC -!- FUNCTION: Adenylyltransferase involved in virulence by mediating the
CC addition of adenosine 5'-monophosphate (AMP) to specific threonine
CC residue of host Rho GTPases RhoA, Rac and Cdc42. The resulting
CC AMPylation prevents the interaction of Rho GTPases with downstream
CC effectors, thereby inhibiting actin assembly in infected cells.
CC {ECO:0000269|PubMed:19039103, ECO:0000269|PubMed:20410310}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.n1;
CC Evidence={ECO:0000269|PubMed:19039103, ECO:0000269|PubMed:20410310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-
CC [protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.n1;
CC Evidence={ECO:0000269|PubMed:19039103, ECO:0000269|PubMed:20410310};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=160 uM for ATP;
CC KM=180 uM for Cdc42;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18347050,
CC ECO:0000269|PubMed:19039103}. Note=Translocated into the host cell via
CC the type III secretion system (TTSS).
CC -!- DOMAIN: The fido domain mediates the adenylyltransferase activity.
CC -!- DISRUPTION PHENOTYPE: Abolishes the ability to inhibit host Rho family
CC GTPases and cause cytoskeletal disruption.
CC {ECO:0000269|PubMed:18347050}.
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DR EMBL; BA000031; BAC59949.1; -; Genomic_DNA.
DR RefSeq; NP_798065.1; NC_004603.1.
DR RefSeq; WP_005464511.1; NC_004603.1.
DR PDB; 3LET; X-ray; 1.80 A; A/B=75-387.
DR PDBsum; 3LET; -.
DR AlphaFoldDB; Q87P32; -.
DR SMR; Q87P32; -.
DR STRING; 223926.28806677; -.
DR EnsemblBacteria; BAC59949; BAC59949; BAC59949.
DR GeneID; 1189193; -.
DR KEGG; vpa:VP1686; -.
DR PATRIC; fig|223926.6.peg.1608; -.
DR eggNOG; COG3177; Bacteria.
DR HOGENOM; CLU_739533_0_0_6; -.
DR OMA; AAAWIIN; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070733; F:protein adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:BHF-UCL.
DR GO; GO:0052039; P:disruption by symbiont of host cytoskeleton; IMP:BHF-UCL.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:BHF-UCL.
DR GO; GO:0018178; P:peptidyl-threonine adenylylation; IDA:BHF-UCL.
DR GO; GO:0018117; P:protein adenylylation; IDA:UniProtKB.
DR GO; GO:0036211; P:protein modification process; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:BHF-UCL.
DR Gene3D; 1.10.3290.10; -; 1.
DR InterPro; IPR003812; Fido.
DR InterPro; IPR036597; Fido-like_dom_sf.
DR Pfam; PF02661; Fic; 1.
DR SUPFAM; SSF140931; SSF140931; 1.
DR PROSITE; PS51459; FIDO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Secreted; Transferase; Virulence.
FT CHAIN 1..387
FT /note="Protein adenylyltransferase VopS"
FT /id="PRO_0000381775"
FT DOMAIN 278..387
FT /note="Fido"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT BINDING 76..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 122..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 353..355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 299
FT /note="R->A: Abolishes adenylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20410310"
FT MUTAGEN 308
FT /note="L->A: Slight reduction in adenylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:20410310"
FT MUTAGEN 348
FT /note="H->A: Abolishes adenylyltransferase activity and its
FT ability to induce cell rounding in host cells."
FT /evidence="ECO:0000269|PubMed:19039103,
FT ECO:0000269|PubMed:20410310"
FT MUTAGEN 350
FT /note="F->A: Abolishes adenylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20410310"
FT MUTAGEN 352
FT /note="D->A: Abolishes adenylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20410310"
FT MUTAGEN 354
FT /note="N->A: Abolishes adenylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20410310"
FT MUTAGEN 356
FT /note="R->A: Abolishes adenylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20410310"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:3LET"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 131..148
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 186..212
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:3LET"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 241..252
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 257..272
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 311..323
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 333..347
FT /evidence="ECO:0007829|PDB:3LET"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 354..368
FT /evidence="ECO:0007829|PDB:3LET"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:3LET"
SQ SEQUENCE 387 AA; 41737 MW; A947E8E2F5A867AE CRC64;
MISFGNVSAL QAAMPQARNE ILNEGKLSIG GKEYTINAAT QEFTRANPTS GAVARFFEAT
GKLFREGSTQ SVAKAITKAV FDNEQGQAQR LQTSSSVEHG QMLFKDANLK TPSDVLNAFA
KLDSKMVKSH AAELSQLAER AMTEVMLETD SGKNLKALIG DDAVKSLAVR VVKDYGGGVA
AAQKNPEVRI NQMQAVFDME VMHLKAAQRH IEGLASTDLN QGVYAEGLPE DAFNKAGVTN
NVERAAAWII NASNSKGNDA ENITSLLKEY ATNGKDLLNM DNLKELHARL VPNVERDYRG
PNISGGTLPS SIGGEGMLKQ HIEGFLKENP VADKDLGKHL FAGVIGYHGF TDGNGRMGRM
LYAIAELRND SFNPLAMNAE NSLHGIK
