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UniProtKB - C7BKP9 (PATOX_PHOAA)

Entry version 51 (25 May 2022)
Sequence version 1 (22 Sep 2009)
Previous versions | rss
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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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Morganellaceae › Photorhabdus ›
<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

More...MobiDBi		Search...

<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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