AFP18_YERRA
ID AFP18_YERRA Reviewed; 2123 AA.
AC C4ULG3;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Toxin Afp18 {ECO:0000303|PubMed:26190758};
DE AltName: Full=Antifeeding prophage 18 {ECO:0000303|PubMed:26190758};
DE AltName: Full=Antifeeding protein 18 {ECO:0000303|PubMed:26190758};
DE Includes:
DE RecName: Full=Protein N-acetylglucosaminyltransferase {ECO:0000305|PubMed:26190758};
DE Short=Protein O-GlcNAc transferase {ECO:0000305|PubMed:26190758};
DE EC=2.4.1.- {ECO:0000269|PubMed:26190758};
DE AltName: Full=Tyrosine glycosyltransferase {ECO:0000303|PubMed:26190758};
GN Name=afp18 {ECO:0000303|PubMed:26190758};
GN ORFNames=DJ39_2720 {ECO:0000312|EMBL:KGA43845.1},
GN yruck0001_1570 {ECO:0000312|EMBL:EEP98478.1};
OS Yersinia ruckeri serotype O1 (strain ATCC 29473 / DSM 18506 / JCM 15110 /
OS NCIMB 2194 / NCTC 12986 / 2396-61).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=527005;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29473 / DSM 18506 / JCM 15110 / NCIMB 2194 / NCTC 12986 /
RC 2396-61;
RA Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P.,
RA Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M.,
RA Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., Willner K.,
RA Zwick M.E.;
RT "Annotation of the Yersinia ruckeri ATCC 29473 genome.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29473 / DSM 18506 / JCM 15110 / NCIMB 2194 / NCTC 12986 /
RC 2396-61;
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION,
RP DOMAIN, AND MUTAGENESIS OF 1957-ASP--ASP-1959.
RC STRAIN=ATCC 29473 / DSM 18506 / JCM 15110 / NCIMB 2194 / NCTC 12986 /
RC 2396-61;
RX PubMed=26190758; DOI=10.1038/ncomms8807;
RA Jank T., Eckerle S., Steinemann M., Trillhaase C., Schimpl M., Wiese S.,
RA van Aalten D.M., Driever W., Aktories K.;
RT "Tyrosine glycosylation of Rho by Yersinia toxin impairs blastomere cell
RT behaviour in zebrafish embryos.";
RL Nat. Commun. 6:7807-7807(2015).
CC -!- FUNCTION: Toxin component of the prophage tail-derived protein
CC translocation system Afp, which is the causative agent of enteric
CC redmouth disease in salmonid fish species. Mono-O-GlcNAcylates the
CC small GTPase RhoA in eukaryotic host cells at Tyr-34, using UDP-N-
CC acetylglucosamine (UDP-GlcNAc) as the sugar donor. Glycosylation of
CC RhoA results in impaired effector and regulator interaction and
CC inactivation of downstream RhoA signaling which leads to actin filament
CC depolymerization and blocks cytokinesis and gastrulation during
CC zebrafish embryo development. To a lesser extent, is also able to
CC glycosylate other Rho family GTPases (RhoB, RhoC, Rac1, Rac2, Rac3, and
CC Cdc42) in vitro at a switch I tyrosine residue, but not Ras proteins.
CC {ECO:0000269|PubMed:26190758}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+)
CC + O-(N-acetyl-alpha-D-glucosaminyl)-L-tyrosyl-[protein] + UDP;
CC Xref=Rhea:RHEA:51536, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13016,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:134208;
CC Evidence={ECO:0000269|PubMed:26190758};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:C7BKP9};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26190758}. Host cell
CC membrane {ECO:0000269|PubMed:26190758}. Note=Is likely secreted by the
CC antifeeding prophage tail (Afp) protein translocation system into
CC eukaryotic host cell. Targets the host cell membrane, and shows co-
CC localization with RhoA. {ECO:0000269|PubMed:26190758}.
CC -!- DOMAIN: The glycosyltransferase domain is the Afp18 protein domain
CC mediating toxicity. {ECO:0000269|PubMed:26190758}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACCC01000029; EEP98478.1; -; Genomic_DNA.
DR EMBL; JPPT01000015; KGA43845.1; -; Genomic_DNA.
DR RefSeq; WP_004721406.1; NZ_KN150747.1.
DR AlphaFoldDB; C4ULG3; -.
DR SMR; C4ULG3; -.
DR GeneID; 66880871; -.
DR PATRIC; fig|527005.28.peg.674; -.
DR HOGENOM; CLU_232095_0_0_6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IMP:UniProtKB.
DR GO; GO:0045992; P:negative regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0036210; P:protein modification process in another organism; IDA:UniProtKB.
DR InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF04488; Gly_transf_sug; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Host cell membrane; Host membrane; Membrane;
KW Metal-binding; Secreted; Toxin; Transferase; Virulence.
FT CHAIN 1..2123
FT /note="Toxin Afp18"
FT /id="PRO_0000434567"
FT REGION 864..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1771..2123
FT /note="Tyrosine glycosyltransferase"
FT /evidence="ECO:0000305|PubMed:26190758"
FT MOTIF 1957..1960
FT /note="DxDD motif"
FT /evidence="ECO:0000305|PubMed:26190758"
FT COMPBIAS 866..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1850..1852
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 1940..1941
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 1957
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 1959
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 1993
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT MUTAGEN 1957..1959
FT /note="DID->NIN: Loss of glycosyltransferase activity. Loss
FT of the ability to abrogate zebrafish embryo development.
FT Loss of effect on actin skeleton and on cytokinesis."
FT /evidence="ECO:0000269|PubMed:26190758"
SQ SEQUENCE 2123 AA; 237975 MW; D20C013FF6D4BA6E CRC64;
MPYFNKSKKN EIRPEKSKEE VGGVLFDDSA IHENIDHNME PQTGDSVATF PDNSDEVVGG
DLAALRARLQ ATIGDYLPEF YEFQQTGRNI LYPKPVDIKA LQARLNSMPI TAWIQPLQQQ
LEQAGNAFLD RFRLFRKEKD WHNNALEFVK FRLAVKETGW DEQQTRDYNE ALKHANRLSG
YLSGTLDLIQ HLNDNPERQT SWEAVRKTSY DMLLNELLPV DAENNGNQYT AKIRGNLTKN
HPDNIKFNTI VNSVTRDERM ASEALSAETK GLSARLLSGI ALTRNSAEKI DKKSETSGIT
RDIVALCQVL QGVIKTIKRR GEYIQPLTDW QPSEHKLPGQ KEELTKAETV KRELVKSRKV
MMQKVQGAKT ILGVLSDKTN KNRHRITQTL PYSANPDTNT VSRKTNEAVF RAGIMLLDKI
QQTTSGIHKA SLASRPLQHA VTQYSALEQM SSGMPSNRIL DAKLRSESGR WQEKAEKSKK
QLQHILREIT ALAEEHLKHK FMSALRDELK RAPETLASNN IISNFDTRAK IVVEGLASIE
IGMNQSVVRL AGHGEAGRKD LDEQVVAWLQ RLERIKGELK TDITQATGQS INNFSRQGML
ARRMGEWNEA EKQRYLAALS TEDRAVAEMQ YNTLFFEVIQ HYLPLLSKET DPQGERLLQR
LRLEVSNAAE GTTVYPATMA EILAGMKSTE QAIRDWSGRK LLRVVFLAAC LEGVKLMPKL
AALPLRVAIK FVITGAKVAW ATHKGQQGIR GGEGDVDDEI GEYAKRSFKT ASVKVVLSLP
PGLATMLGVA SIALDVYEGG LKGAGGKIAK NIVGDAPWRA LNQGSKIAAE AYTTASMNAA
LKEGGANPVS HSSTLQQQMD AKPFFDNSDQ DADQPRVRRK REMTDEIMLS DGSSRSEAKA
LPDENELDTD QSKSRPESAL AVETLQSEHF DFDRGIRYQD FSDEQKKQTY LHGIKFVLLQ
IENDGHFAQN IRNNAYLARI GAKLAVPVDI YRYKLNNTFL LPDEIDSKSG VLIRLDSEIP
YYYVSEGKDL LENIAWAMPY NAANRGPLKF SLDPGEVTSS HSGVDILNNI RSERFKFETY
FNYNAPEAMS IESLSAQLAN TIEADYKFKN TSPTNKILIS RAIVGAHIPD PGVRATQGEY
HIEFDSDELA PAKYLRSFAR PFSTLSGEMQ LISSSIKGET IQETELHVHQ AEYIGSWVDA
TAGAIISFTP EGWFLNTAQS AAEITADLTE GKDPDPLAVA GLLVGIIPGG KIAAKVGKFT
RIGGKTVKYG LILGNKSVDL AIVGKSIKTA VDTGEPLAIY QAFLASGMSV KNSYDIAKNM
SSELKISKKI EESARLRKLK ALQKNTYKYS MNSKMPVRKF RVGQTDLLGK IHKGEIKISR
NNGTTWEKGN QLHLLAYRLQ NAGGGRLLPD VFRDKIVIGE YSFKRVKYNQ KKLNEMMRIA
KMYTPTSNST ERIAKLQQNY KTGKEMSHAP QYDTYNDLSL GEKLDLFINS NTDATTRGVL
AGKINESITN INLYETAKGV DAWKTSANKA TDVVLAPQNI FLKGRAGECL PESILMGWAL
QSGQDTKLAK KLMNIHSSSN IAANPLYKSL VELHSDGNAS RFGESVISDI NMKMLSGAES
KLFPTENSSV RVDIPEHTML ISKVNKDGKI KYVFYDPNYG MAYFNKYKEM ISFFKKKIKG
YDTPKRSTSF RQLDYSHLSD IKIKGKNLNE IIDGEIPQIF RQEDVNLEGI TPQDGIYRML
GTHQQENNTY IKSQNNIYQV EWDQTTNTWR VFDSANTNRS RITVPIKRDT DGEWFKYTET
GLKGGGLFDE IKNNWLQRKR FKNLQDFNDI VDFEENKWPS EPINKDIHMI WVGTRNISEK
NIGLSLETAR KNSDYNTTII YDSGIAGYES AKDFMTEKFK DSKVTLVDFR KKSYFHQLQQ
EPSFPYYEQA IRDKKYAQAS DILRLLVLKY EGGIYKDIDD VQVKAFGSLA FPKGIGVMRE
YAPEAGKTTA FPNTPIAATK NNPVVNKTLE LAVENYHRGE TNVLKLAGPD VFTESLYQEI
PGMRPQVLGA QLDQFELAKR QALGMRLEKP KGFADEKLTL QEKAKIRQPY EAIRGLSGYV
DNGADHSWVT DMPGNSTQSS GLS
