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Toxin PAU_02230 (Photorhabdus asymbiotica toxin) (PaTox) [Includes: Protein N-acetylglucosaminyltransferase (Protein O-GlcNAc transferase) (EC 2.4.1.-) (PaToxG) (Tyrosine glycosyltransferase); Protein-glutamine amidohydrolase (EC 3.5.1.44) (Glutamine deamidase) (PaToxD) (Protein-glutamine glutaminase)]

 PATOX_PHOAA             Reviewed;        2957 AA.
C7BKP9;
11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 1.
23-MAY-2018, entry version 39.
RecName: Full=Toxin PAU_02230 {ECO:0000305};
AltName: Full=Photorhabdus asymbiotica toxin {ECO:0000303|PubMed:24141704};
Short=PaTox {ECO:0000303|PubMed:24141704};
Includes:
RecName: Full=Protein N-acetylglucosaminyltransferase {ECO:0000305|PubMed:24141704};
Short=Protein O-GlcNAc transferase {ECO:0000305|PubMed:24141704};
EC=2.4.1.- {ECO:0000269|PubMed:24141704};
AltName: Full=PaToxG {ECO:0000303|PubMed:24141704};
AltName: Full=Tyrosine glycosyltransferase {ECO:0000303|PubMed:24141704};
Includes:
RecName: Full=Protein-glutamine amidohydrolase {ECO:0000305|PubMed:24141704};
EC=3.5.1.44 {ECO:0000269|PubMed:24141704};
AltName: Full=Glutamine deamidase {ECO:0000303|PubMed:24141704};
AltName: Full=PaToxD {ECO:0000303|PubMed:24141704};
AltName: Full=Protein-glutamine glutaminase {ECO:0000305};
OrderedLocusNames=PAU_02230 {ECO:0000312|EMBL:CAQ84322.1};
Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 /
3105-77) (Xenorhabdus luminescens (strain 2)).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Morganellaceae; Photorhabdus.
NCBI_TaxID=553480 {ECO:0000312|Proteomes:UP000002747};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43949 / 3105-77;
PubMed=19583835; DOI=10.1186/1471-2164-10-302;
Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
Harris D., Thompson N.R., Quail M., Parkhill J.,
ffrench-Constant R.H.;
"Comparative genomics of the emerging human pathogen Photorhabdus
asymbiotica with the insect pathogen Photorhabdus luminescens.";
BMC Genomics 10:302-302(2009).
[2]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 2134-ARG-LYS-2135 AND
2139-ARG-LYS-2140.
STRAIN=ATCC 43950;
PubMed=25782990; DOI=10.1096/fj.14-269381;
Jank T., Trillhaase C., Brozda N., Steinemann M., Schwan C., Suess R.,
Aktories K.;
"Intracellular plasma membrane guidance of Photorhabdus asymbiotica
toxin is crucial for cell toxicity.";
FASEB J. 29:2789-2802(2015).
[3]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2114-2449 IN COMPLEX WITH
CALCIUM AND UDP-GLCNAC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
SUBSTRATE SPECIFICITY, DOMAIN, AND MUTAGENESIS OF TRP-2170; ASP-2260;
ARG-2263; ASP-2276; ASP-2278; ASP-2279; 2276-ASP--ASP-2279; ASN-2312
AND CYS-2509.
STRAIN=ATCC 43950;
PubMed=24141704; DOI=10.1038/nsmb.2688;
Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
Aktories K.;
"A bacterial toxin catalyzing tyrosine glycosylation of Rho and
deamidation of Gq and Gi proteins.";
Nat. Struct. Mol. Biol. 20:1273-1280(2013).
-!- FUNCTION: Toxin that acts on host cells by modifying Rho proteins
by tyrosine GlcNAcylation and heterotrimeric G alpha proteins by
deamidation. Catalyzes the mono-O-GlcNAcylation of small GTPases
of the Rho family (RhoA, RhoB, RhoC, Rac1, Rac2, Rac3, Cdc42) in
eukaryotic host cells at the conserved tyrosine residue located in
the switch I region (Tyr-32/34), using UDP-N-acetylglucosamine
(UDP-GlcNAc) as the sugar donor; other GTPases of the Rho, Ras or
Rab families are not substrates. Tyrosine glycosylation inhibits
Rho activation and prevents interaction with downstream effectors,
resulting in actin disassembly, inhibition of phagocytosis, cell
rounding, and toxicity toward insects and mammalian cells. Also
catalyzes the deamidation of the catalytic glutamine in
heterotrimeric G alpha proteins (Gi, Gq/11), which blocks GTP
hydrolysis and arrests the G proteins in a permanent active state
leading to activation of Rho GTPases. Thus, PaTox hijacks host
GTPase signaling in a bidirectional manner by deamidation-induced
activation and glycosylation-induced inactivation of GTPases.
{ECO:0000269|PubMed:24141704}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + [protein]-
L-tyrosine = UDP + [protein]-O-(N-acetyl-alpha-D-glucosaminyl)-L-
tyrosine. {ECO:0000269|PubMed:24141704}.
-!- CATALYTIC ACTIVITY: Protein L-glutamine + H(2)O = protein L-
glutamate + NH(3). {ECO:0000269|PubMed:24141704}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000269|PubMed:24141704};
Note=A Ca(2+) ion is seen in the structure.
{ECO:0000269|PubMed:24141704};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Host cell membrane
{ECO:0000269|PubMed:25782990}; Peripheral membrane protein
{ECO:0000269|PubMed:25782990}; Cytoplasmic side
{ECO:0000269|PubMed:25782990}. Note=Associates with the negatively
charged inner leaflet of the plasma membrane via interaction with
phosphatidylserine and phosphatidylinositolphosphates. Plasma
membrane localization of PaTox is essential for cytotoxicity. The
glycosyltransferase domain alone is sufficient to localize at the
plasma membrane. {ECO:0000269|PubMed:25782990}.
-!- DOMAIN: In the C-terminal region, contains two catalytic domains:
a glycosyltransferase (PaToxG) and a deamidase domain (PaToxD).
The N-terminal region contains a receptor-translocation domain
necessary for toxin entry into the cytoplasm of host cell.
{ECO:0000269|PubMed:24141704}.
-!- MISCELLANEOUS: The active GTP-bound conformation of Rho is the
preferred substrate for PaTox-induced glycosylation.
{ECO:0000269|PubMed:24141704}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; FM162591; CAQ84322.1; -; Genomic_DNA.
PDB; 4MIX; X-ray; 1.80 A; A/B=2114-2449.
PDBsum; 4MIX; -.
SMR; C7BKP9; -.
STRING; 553480.PAU_02230; -.
PRIDE; C7BKP9; -.
EnsemblBacteria; CAQ84322; CAQ84322; PAU_02230.
KEGG; pay:PAU_02230; -.
eggNOG; ENOG4106EE1; Bacteria.
eggNOG; ENOG410Y12W; LUCA.
OrthoDB; POG091H070A; -.
Proteomes; UP000002747; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
GO; GO:0050568; F:protein-glutamine glutaminase activity; IDA:UniProtKB.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0036210; P:protein modification process in other organism; IDA:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR028907; Tox-PLDMTX_dom.
Pfam; PF04488; Gly_transf_sug; 1.
Pfam; PF15645; Tox-PLDMTX; 1.
SUPFAM; SSF53448; SSF53448; 2.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Glycosyltransferase;
Host cell membrane; Host membrane; Hydrolase; Membrane; Metal-binding;
Multifunctional enzyme; Reference proteome; Secreted; Toxin;
Transferase; Virulence.
CHAIN 1 2957 Toxin PAU_02230.
/FTId=PRO_0000434568.
REGION 2115 2449 Tyrosine glycosyltransferase PaToxG.
{ECO:0000305|PubMed:24141704}.
REGION 2115 2144 Membrane localization domain that
interacts with the inner leaflet of the
plasma membrane.
{ECO:0000269|PubMed:25782990}.
REGION 2169 2171 UDP-GlcNAc binding.
{ECO:0000269|PubMed:24141704}.
REGION 2259 2260 UDP-GlcNAc binding.
{ECO:0000269|PubMed:24141704}.
REGION 2450 2672 SseI-like deamidase PaToxD.
{ECO:0000305|PubMed:24141704}.
MOTIF 2276 2279 DxDD motif.
{ECO:0000305|PubMed:24141704}.
ACT_SITE 2509 2509 For deamidase activity.
{ECO:0000305|PubMed:24141704}.
ACT_SITE 2547 2547 For deamidase activity.
{ECO:0000305|PubMed:24141704}.
ACT_SITE 2562 2562 For deamidase activity.
{ECO:0000305|PubMed:24141704}.
METAL 2276 2276 Divalent metal cation.
{ECO:0000244|PDB:4MIX,
ECO:0000305|PubMed:24141704}.
METAL 2278 2278 Divalent metal cation.
{ECO:0000244|PDB:4MIX,
ECO:0000305|PubMed:24141704}.
BINDING 2312 2312 UDP-GlcNAc.
{ECO:0000269|PubMed:24141704}.
MUTAGEN 2134 2135 RK->EE: Abrogates plasma membrane
localization, resulting in a cytosolic
distribution of this mutant protein. Loss
of toxic activity on host cells during
the first hours of incubation. No effect
on glycosyltransferase activity and
interaction with RhoA.
{ECO:0000269|PubMed:25782990}.
MUTAGEN 2139 2140 RK->EE: Abrogates plasma membrane
localization, resulting in a cytosolic
distribution of this mutant protein. Loss
of toxic activity on host cells during
the first hours of incubation. No effect
on glycosyltransferase activity and
interaction with RhoA.
{ECO:0000269|PubMed:25782990}.
MUTAGEN 2170 2170 W->A: 7-fold reduction in
glycosyltransferase activity.
{ECO:0000269|PubMed:24141704}.
MUTAGEN 2260 2260 D->A: 10000-fold reduction in
glycosyltransferase activity. Reduced
cell toxicity.
{ECO:0000269|PubMed:24141704}.
MUTAGEN 2263 2263 R->A: 2000-fold reduction in
glycosyltransferase activity. Reduced
cell toxicity.
{ECO:0000269|PubMed:24141704}.
MUTAGEN 2276 2278 DID->NIN: Loss of glycosyltransferase
activity. Reduced toxicity in insect
larvae. Loss of the ability to block
phagocytosis in mammalian macrophages.
Loss of effect on actin skeleton.
{ECO:0000269|PubMed:24141704}.
MUTAGEN 2276 2276 D->N: 16700-fold reduction in
glycosyltransferase activity.
{ECO:0000269|PubMed:24141704}.
MUTAGEN 2278 2278 D->N: 333-fold reduction in
glycosyltransferase activity.
{ECO:0000269|PubMed:24141704}.
MUTAGEN 2279 2279 D->N: 700-fold reduction in
glycosyltransferase activity.
{ECO:0000269|PubMed:24141704}.
MUTAGEN 2312 2312 N->A: 1.3-fold reduction in
glycosyltransferase activity.
{ECO:0000269|PubMed:24141704}.
MUTAGEN 2509 2509 C->S: Loss of deamidase activity.
{ECO:0000269|PubMed:24141704}.
HELIX 2132 2153 {ECO:0000244|PDB:4MIX}.
STRAND 2164 2169 {ECO:0000244|PDB:4MIX}.
STRAND 2172 2174 {ECO:0000244|PDB:4MIX}.
HELIX 2178 2189 {ECO:0000244|PDB:4MIX}.
STRAND 2194 2200 {ECO:0000244|PDB:4MIX}.
HELIX 2208 2218 {ECO:0000244|PDB:4MIX}.
STRAND 2221 2227 {ECO:0000244|PDB:4MIX}.
HELIX 2228 2230 {ECO:0000244|PDB:4MIX}.
HELIX 2234 2239 {ECO:0000244|PDB:4MIX}.
HELIX 2241 2251 {ECO:0000244|PDB:4MIX}.
HELIX 2255 2270 {ECO:0000244|PDB:4MIX}.
STRAND 2272 2274 {ECO:0000244|PDB:4MIX}.
HELIX 2291 2293 {ECO:0000244|PDB:4MIX}.
STRAND 2312 2317 {ECO:0000244|PDB:4MIX}.
HELIX 2322 2337 {ECO:0000244|PDB:4MIX}.
HELIX 2343 2346 {ECO:0000244|PDB:4MIX}.
HELIX 2348 2358 {ECO:0000244|PDB:4MIX}.
HELIX 2360 2362 {ECO:0000244|PDB:4MIX}.
HELIX 2364 2382 {ECO:0000244|PDB:4MIX}.
HELIX 2399 2412 {ECO:0000244|PDB:4MIX}.
TURN 2413 2417 {ECO:0000244|PDB:4MIX}.
STRAND 2418 2420 {ECO:0000244|PDB:4MIX}.
SEQUENCE 2957 AA; 334884 MW; AE0C52A8C11E4C6B CRC64;
MKGIEGVIML SHDILPEKLL VSEKKHENVG SYFSDDIGEQ SEQTEVSHFN LSLDDAFDIY
ADISIENQQE LKNKDNNTNI WSSLGRGDDD HNLKKIINDA FKEKLPQLME YRRKGYNVIG
LDKEGIKKLE GMLKAVPPEI QQPTMKNLYS AAQELLNTLK QHPLLPENQD MIQQSNLVIR
NLSDALEAIN AVSKVNQVEW WEEVHKTNKA QSDRLIAATL EELFFKVKDK RLPGSNDDYC
QQEREETERK IKDLLLYDGY QLTAEHFKFG RLRKSLLAES RVTRLKLAEY LEKKSVGILT
AARDAKMYAM KILLAQTRNN GFNAKDLINA GQVNDRLLSF QQYARHIRAV DGEIDGIILS
NPLVVACIKE TNDEPAHIKI ARAILPVSEE LGTVSKVLRE TKEKVQPSKP KEELNHPHQD
WWNRGDELWK YIKKTSWNIK ETSVHVTQMV GYEASKTASR AKHKLKESSY SESINGAVKG
TALLLLDEIQ QAENRIRQIP QFAWDVQEAV EQHSSVIQRT AYPDELPELS ELLNEQLKHE
EARWQAVKKQ SRDKLQELIA PITRLAQEKW AQDLYFQLGE ELRKERQDRW KDIQQFDEIM
AEAVGQFAEM ARELDSEAVR LAEHGHSGGK ELQEKVAKWL RDLSKLKGKV KAGVAKITGT
SLDNFSRSGM LARGMSEWAE DLKQSYLQET LQEGSAVAAE LFERTLMEVV EENRTHFAKE
SDPEAERFLK RLALALKHAA ENTTVYPPTP EEILAGSRSL PEDIRHWAEK KVVSGAISAA
FRGGFKLVTG TFSLPVRVVI RGAKTGGTLY RGVRAINRSV RLGQGPATQV KSKFINQELS
KTAFRLTLSL SPLVAWGMAA SITAGRLYNE KDYPEKIIKN IVIDLPEELL WIGGYAGINA
AIRAHAEKAI QQAIQHALDE QADKLALRIN KEIAGKSADV NVEIIPQETS VSPAETAQST
PEPLSDFAST SQLTMPELID IQDNNSAQQP KVRRKRDVSV ESEISIDNLN IINANTREDK
VNSEIKSELR SELKRFENSD ANSPMSDVER AIFIDLFLYK NKYEVSESQQ DYKNTWLKFR
RELESQENKE IKEYLRFRSI IEAYEIYDKK RLDDDTIPEA GTIIKEVIDF FQKLKKENPI
TFMKLAEAMV KFQYYYEEED ENEDRYFKMA EIYYFLNKTE NEKKSKTFHL DIIDKYPNEN
NRLLDEFFLN KNNNNPDLDE IIYKLQSMQE KYRESYEMLS KVENIHQVLS DDSKNEENIF
LDNRIIAAQV FDGSINISLQ DKKKWLNRYD QIRNEEGSDG WKLMHIESIL INLRRINTAI
NLTAMKSESA LLLIDKLLNF QKKARENILH ISETPHEDFT SYSQFKTRKE LGNDDSKYYA
QFDNYKDNHD AEKEAKEILS QVVARASLSF SELFDKVESI KLFSFVYKNR DGGAPLAAPG
RTVVIKFPGK DTGGLVISNL FLRNHVKRIS TKEMEDLKPL TEGMYTRATQ HRSLGSYYHI
GSQSEHTNAL EILSGMNKEE LKTHLKKQGI WFGEPALFSN EYPKQENTGH LENTTLKNAI
IGVSTIQNNA AANYLRSTMY ESTGWEKLGD RFIPFYEIGR RKHYDREYEI NSEQLTLDII
TSIAIAYPAA RGIVATIRSS AIPSILKSGL RGSALFKSLS LELGKMGFNA SKVFGGAVYE
LIEPYPINSH LNRHNVFNKV KDTAWEFHTD VGLKGGGLKD FIDRFTKEPK EITISGYKFK
RIKYNQENFD TMQRMALDYA YNPDSKGKIA QAQQAYKTGK EDYNAPQYDN FNGLSLDKKI
ERYISPDTDA TTKGVLAGKM NESIKDINAF QTAKDAQSWK KSANKANKVV LTPQNLYLKG
KPSECLPESV LMGWALQSSQ DAKLSKMLMG IYSSNDITSN PLYKSLKELH ANGNASKFNA
SATSISNINV SNLATSETKL FPTEISSVRV DAPKHTMLIS KIKNRENKIK YVFYDPNYGM
AYFDKHSDMA AFFQKKMQQY DFPDDSVSFH PLDYSNVSDI KISGRNLNEI IDGEIPLLYK
QEGVQLEGIT PRDGIYRVPP KNTLGVQETK HYIIVNNDIY QVEWDQTNNT WRVFDPSNTN
RSRPTVPVKQ DTNGEWFKHS ETGLKGGGPI DDIRKYIARK SAIKIFNQSI NYSATKWPPE
PIDKNIHMIW IGTKNISEKN IKLSIDTAKK NPDYNTSIIY DSGISGHEGA KKFMLEKFQD
SNVNIIDFRK KSYFSQLKQE PSFAYYEQVI AENKYAQASD ILRLLVLKYE GGIYKDIDDI
QVKGFGSLTF PKGIGVMREY APEAGKATAF PNTPIAVTKN NPIINKTLDL AVSNYQRGEK
NVLKLAGPDV FTQALYQEIP GLDSKVLNAQ LYQLELAKRQ ALGVPLEKPK NFADEQLTSA
EKEKINRPYQ SIRGLSGYVE NGADHSWAVD TNIPSTSTQT STIVTPLAPK TEMLPPVPSS
STKSSTSAPV LQEKISYNLA TDIDATDYLN QLKQKTNINN KISSPAGQCE SLMKPVSDFM
RENGFTDIRY RGMFIWNNAT EQIPMNHFVV VGKKVGKDYV FDVSAHQFEN KGMPDLNGPL
ILAAEDWAKK YRGATTRKLI YYSDFKNAST ATNTYNALPR ELVLESMEGK TFITSPNWYQ
TFKRTHNIHP EVTVSDPATF SLNYSVNPTA ENLSPPPPPP IPSHGQVPKT VTPPPPPMRS
PLSLSQPLER LPANKTKPIG FNPGENKASF SKLEEAGKHY YKDDKSRQAA PVNTMSDFDN
RYLSHTTEAP APSNVAHLAP GNIYNTKVTA KGAEKPAYDI YISKDGESLI TSSSYKVDDI
TTDSKFGKPL PYSEIMFNSL KKSGVDPKNL KRSVQASIEN KVTQDVISAI GTRIQRGQVI
RVSPTENPDA FYTLLGTDNC KATLHMLNQH AEEFGHKVVT SIEFKGTGYL VMNIGTSTQT
STIVTPPPMP GTSQLVQ


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