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Entry version 51 (25 May 2022)
Sequence version 1 (22 Sep 2009)
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Protein

Toxin PAU_02230

Gene

PAU_02230

Organism
Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77) (Xenorhabdus luminescens (strain 2))
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.

1 Publication

Miscellaneous

The active GTP-bound conformation of Rho is the preferred substrate for PaTox-induced glycosylation.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

a divalent metal cation1 PublicationNote: A Ca2+ ion is seen in the structure.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi2276Divalent metal cationCombined sources1 Publication1
Metal bindingi2278Divalent metal cationCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei2312UDP-GlcNAc1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei2509For deamidase activity1 Publication1
Active sitei2547For deamidase activity1 Publication1
Active sitei2562For deamidase activity1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosyltransferase, Hydrolase, Multifunctional enzyme, Toxin, Transferase
Biological processVirulence
LigandCalcium, Metal-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Toxin PAU_02230Curated
Alternative name(s):
Photorhabdus asymbiotica toxin1 Publication
Short name:
PaTox1 Publication
Including the following 2 domains:
Protein N-acetylglucosaminyltransferase1 Publication (EC:2.4.1.-1 Publication)
Short name:
Protein O-GlcNAc transferase1 Publication
Alternative name(s):
PaToxG1 Publication
Tyrosine glycosyltransferase1 Publication
Protein-glutamine amidohydrolase1 Publication (EC:3.5.1.441 Publication)
Alternative name(s):
Glutamine deamidase1 Publication
PaToxD1 Publication
Protein-glutamine glutaminaseCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Ordered Locus Names:PAU_02230Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPhotorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77) (Xenorhabdus luminescens (strain 2))Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri553480 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesMorganellaceaePhotorhabdus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002747 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2134 – 2135RK → 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. 1 Publication2
Mutagenesisi2139 – 2140RK → 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. 1 Publication2
Mutagenesisi2170W → A: 7-fold reduction in glycosyltransferase activity. 1 Publication1
Mutagenesisi2260D → A: 10000-fold reduction in glycosyltransferase activity. Reduced cell toxicity. 1 Publication1
Mutagenesisi2263R → A: 2000-fold reduction in glycosyltransferase activity. Reduced cell toxicity. 1 Publication1
Mutagenesisi2276 – 2278DID → 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. 1 Publication3
Mutagenesisi2276D → N: 16700-fold reduction in glycosyltransferase activity. 1 Publication1
Mutagenesisi2278D → N: 333-fold reduction in glycosyltransferase activity. 1 Publication1
Mutagenesisi2279D → N: 700-fold reduction in glycosyltransferase activity. 1 Publication1
Mutagenesisi2312N → A: 1.3-fold reduction in glycosyltransferase activity. 1 Publication1
Mutagenesisi2509C → S: Loss of deamidase activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004345681 – 2957Toxin PAU_02230Add BLAST2957

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
C7BKP9

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
291112.PAU_02230

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

12957
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
C7BKP9

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni949 – 968DisorderedSequence analysisAdd BLAST20
Regioni2115 – 2449Tyrosine glycosyltransferase PaToxG1 PublicationAdd BLAST335
Regioni2115 – 2144Membrane localization domain that interacts with the inner leaflet of the plasma membrane1 PublicationAdd BLAST30
Regioni2169 – 2171UDP-GlcNAc binding1 Publication3
Regioni2259 – 2260UDP-GlcNAc binding1 Publication2
Regioni2450 – 2672SseI-like deamidase PaToxD1 PublicationAdd BLAST223
Regioni2667 – 2705DisorderedSequence analysisAdd BLAST39

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi2276 – 2279DxDD motif1 Publication4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi2671 – 2702Pro residuesSequence analysisAdd BLAST32

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.1 Publication

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG3774, Bacteria
COG5539, Bacteria

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007577, GlycoTrfase_DXD_sugar-bd_CS
IPR029044, Nucleotide-diphossugar_trans
IPR028907, Tox-PLDMTX_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04488, Gly_transf_sug, 1 hit
PF15645, Tox-PLDMTX, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53448, SSF53448, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

C7BKP9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKGIEGVIML SHDILPEKLL VSEKKHENVG SYFSDDIGEQ SEQTEVSHFN
60 70 80 90 100
LSLDDAFDIY ADISIENQQE LKNKDNNTNI WSSLGRGDDD HNLKKIINDA
110 120 130 140 150
FKEKLPQLME YRRKGYNVIG LDKEGIKKLE GMLKAVPPEI QQPTMKNLYS
160 170 180 190 200
AAQELLNTLK QHPLLPENQD MIQQSNLVIR NLSDALEAIN AVSKVNQVEW
210 220 230 240 250
WEEVHKTNKA QSDRLIAATL EELFFKVKDK RLPGSNDDYC QQEREETERK
260 270 280 290 300
IKDLLLYDGY QLTAEHFKFG RLRKSLLAES RVTRLKLAEY LEKKSVGILT
310 320 330 340 350
AARDAKMYAM KILLAQTRNN GFNAKDLINA GQVNDRLLSF QQYARHIRAV
360 370 380 390 400
DGEIDGIILS NPLVVACIKE TNDEPAHIKI ARAILPVSEE LGTVSKVLRE
410 420 430 440 450
TKEKVQPSKP KEELNHPHQD WWNRGDELWK YIKKTSWNIK ETSVHVTQMV
460 470 480 490 500
GYEASKTASR AKHKLKESSY SESINGAVKG TALLLLDEIQ QAENRIRQIP
510 520 530 540 550
QFAWDVQEAV EQHSSVIQRT AYPDELPELS ELLNEQLKHE EARWQAVKKQ
560 570 580 590 600
SRDKLQELIA PITRLAQEKW AQDLYFQLGE ELRKERQDRW KDIQQFDEIM
610 620 630 640 650
AEAVGQFAEM ARELDSEAVR LAEHGHSGGK ELQEKVAKWL RDLSKLKGKV
660 670 680 690 700
KAGVAKITGT SLDNFSRSGM LARGMSEWAE DLKQSYLQET LQEGSAVAAE
710 720 730 740 750
LFERTLMEVV EENRTHFAKE SDPEAERFLK RLALALKHAA ENTTVYPPTP
760 770 780 790 800
EEILAGSRSL PEDIRHWAEK KVVSGAISAA FRGGFKLVTG TFSLPVRVVI
810 820 830 840 850
RGAKTGGTLY RGVRAINRSV RLGQGPATQV KSKFINQELS KTAFRLTLSL
860 870 880 890 900
SPLVAWGMAA SITAGRLYNE KDYPEKIIKN IVIDLPEELL WIGGYAGINA
910 920 930 940 950
AIRAHAEKAI QQAIQHALDE QADKLALRIN KEIAGKSADV NVEIIPQETS
960 970 980 990 1000
VSPAETAQST PEPLSDFAST SQLTMPELID IQDNNSAQQP KVRRKRDVSV
1010 1020 1030 1040 1050
ESEISIDNLN IINANTREDK VNSEIKSELR SELKRFENSD ANSPMSDVER
1060 1070 1080 1090 1100
AIFIDLFLYK NKYEVSESQQ DYKNTWLKFR RELESQENKE IKEYLRFRSI
1110 1120 1130 1140 1150
IEAYEIYDKK RLDDDTIPEA GTIIKEVIDF FQKLKKENPI TFMKLAEAMV
1160 1170 1180 1190 1200
KFQYYYEEED ENEDRYFKMA EIYYFLNKTE NEKKSKTFHL DIIDKYPNEN
1210 1220 1230 1240 1250
NRLLDEFFLN KNNNNPDLDE IIYKLQSMQE KYRESYEMLS KVENIHQVLS
1260 1270 1280 1290 1300
DDSKNEENIF LDNRIIAAQV FDGSINISLQ DKKKWLNRYD QIRNEEGSDG
1310 1320 1330 1340 1350
WKLMHIESIL INLRRINTAI NLTAMKSESA LLLIDKLLNF QKKARENILH
1360 1370 1380 1390 1400
ISETPHEDFT SYSQFKTRKE LGNDDSKYYA QFDNYKDNHD AEKEAKEILS
1410 1420 1430 1440 1450
QVVARASLSF SELFDKVESI KLFSFVYKNR DGGAPLAAPG RTVVIKFPGK
1460 1470 1480 1490 1500
DTGGLVISNL FLRNHVKRIS TKEMEDLKPL TEGMYTRATQ HRSLGSYYHI
1510 1520 1530 1540 1550
GSQSEHTNAL EILSGMNKEE LKTHLKKQGI WFGEPALFSN EYPKQENTGH
1560 1570 1580 1590 1600
LENTTLKNAI IGVSTIQNNA AANYLRSTMY ESTGWEKLGD RFIPFYEIGR
1610 1620 1630 1640 1650
RKHYDREYEI NSEQLTLDII TSIAIAYPAA RGIVATIRSS AIPSILKSGL
1660 1670 1680 1690 1700
RGSALFKSLS LELGKMGFNA SKVFGGAVYE LIEPYPINSH LNRHNVFNKV
1710 1720 1730 1740 1750
KDTAWEFHTD VGLKGGGLKD FIDRFTKEPK EITISGYKFK RIKYNQENFD
1760 1770 1780 1790 1800
TMQRMALDYA YNPDSKGKIA QAQQAYKTGK EDYNAPQYDN FNGLSLDKKI
1810 1820 1830 1840 1850
ERYISPDTDA TTKGVLAGKM NESIKDINAF QTAKDAQSWK KSANKANKVV
1860 1870 1880 1890 1900
LTPQNLYLKG KPSECLPESV LMGWALQSSQ DAKLSKMLMG IYSSNDITSN
1910 1920 1930 1940 1950
PLYKSLKELH ANGNASKFNA SATSISNINV SNLATSETKL FPTEISSVRV
1960 1970 1980 1990 2000
DAPKHTMLIS KIKNRENKIK YVFYDPNYGM AYFDKHSDMA AFFQKKMQQY
2010 2020 2030 2040 2050
DFPDDSVSFH PLDYSNVSDI KISGRNLNEI IDGEIPLLYK QEGVQLEGIT
2060 2070 2080 2090 2100
PRDGIYRVPP KNTLGVQETK HYIIVNNDIY QVEWDQTNNT WRVFDPSNTN
2110 2120 2130 2140 2150
RSRPTVPVKQ DTNGEWFKHS ETGLKGGGPI DDIRKYIARK SAIKIFNQSI
2160 2170 2180 2190 2200
NYSATKWPPE PIDKNIHMIW IGTKNISEKN IKLSIDTAKK NPDYNTSIIY
2210 2220 2230 2240 2250
DSGISGHEGA KKFMLEKFQD SNVNIIDFRK KSYFSQLKQE PSFAYYEQVI
2260 2270 2280 2290 2300
AENKYAQASD ILRLLVLKYE GGIYKDIDDI QVKGFGSLTF PKGIGVMREY
2310 2320 2330 2340 2350
APEAGKATAF PNTPIAVTKN NPIINKTLDL AVSNYQRGEK NVLKLAGPDV
2360 2370 2380 2390 2400
FTQALYQEIP GLDSKVLNAQ LYQLELAKRQ ALGVPLEKPK NFADEQLTSA
2410 2420 2430 2440 2450
EKEKINRPYQ SIRGLSGYVE NGADHSWAVD TNIPSTSTQT STIVTPLAPK
2460 2470 2480 2490 2500
TEMLPPVPSS STKSSTSAPV LQEKISYNLA TDIDATDYLN QLKQKTNINN
2510 2520 2530 2540 2550
KISSPAGQCE SLMKPVSDFM RENGFTDIRY RGMFIWNNAT EQIPMNHFVV
2560 2570 2580 2590 2600
VGKKVGKDYV FDVSAHQFEN KGMPDLNGPL ILAAEDWAKK YRGATTRKLI
2610 2620 2630 2640 2650
YYSDFKNAST ATNTYNALPR ELVLESMEGK TFITSPNWYQ TFKRTHNIHP
2660 2670 2680 2690 2700
EVTVSDPATF SLNYSVNPTA ENLSPPPPPP IPSHGQVPKT VTPPPPPMRS
2710 2720 2730 2740 2750
PLSLSQPLER LPANKTKPIG FNPGENKASF SKLEEAGKHY YKDDKSRQAA
2760 2770 2780 2790 2800
PVNTMSDFDN RYLSHTTEAP APSNVAHLAP GNIYNTKVTA KGAEKPAYDI
2810 2820 2830 2840 2850
YISKDGESLI TSSSYKVDDI TTDSKFGKPL PYSEIMFNSL KKSGVDPKNL
2860 2870 2880 2890 2900
KRSVQASIEN KVTQDVISAI GTRIQRGQVI RVSPTENPDA FYTLLGTDNC
2910 2920 2930 2940 2950
KATLHMLNQH AEEFGHKVVT SIEFKGTGYL VMNIGTSTQT STIVTPPPMP

GTSQLVQ
Length:2,957
Mass (Da):334,884
Last modified:September 22, 2009 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iAE0C52A8C11E4C6B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
FM162591 Genomic DNA Translation: CAQ84322.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAQ84322; CAQ84322; PAU_02230

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pay:PAU_02230

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM162591 Genomic DNA Translation: CAQ84322.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MIXX-ray1.80A/B2114-2449[»]
6HV6X-ray2.00A1701-2114[»]
SMRiC7BKP9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi291112.PAU_02230

Proteomic databases

PRIDEiC7BKP9

Genome annotation databases

EnsemblBacteriaiCAQ84322; CAQ84322; PAU_02230
KEGGipay:PAU_02230

Phylogenomic databases

eggNOGiCOG3774, Bacteria
COG5539, Bacteria

Family and domain databases

InterProiView protein in InterPro
IPR007577, GlycoTrfase_DXD_sugar-bd_CS
IPR029044, Nucleotide-diphossugar_trans
IPR028907, Tox-PLDMTX_dom
PfamiView protein in Pfam
PF04488, Gly_transf_sug, 1 hit
PF15645, Tox-PLDMTX, 1 hit
SUPFAMiSSF53448, SSF53448, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPATOX_PHOAA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: C7BKP9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 11, 2015
Last sequence update: September 22, 2009
Last modified: May 25, 2022
This is version 51 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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