{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079457/SI_Table9_Pulldown.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079457/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD079457/A01054.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["hpxiao@stanford.edu"],"submitter":["Junyi Chen"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["pulldown proteomics","stand ntpase","phage major capsid protein","ef-tu","Seavs7","tmtpro","affinity purification mass spectrometry","bacterial immunity","antiphage defense","Seavs7; stand ntpase; bacterial immunity; antiphage defense; phage major capsid protein; ef-tu; affinity purification mass spectrometry; pulldown proteomics; tmtpro"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD079457"],"tissue":["Prokaryotic Cell"],"sample_protocol":["Proteomics sample preparation. Pulldown eluates were digested with Lys-C and trypsin (10 ng/µL each) in 200 mM EPPS pH 8.5 at 37 °C overnight with shaking at 1,200 rpm. Neat acetonitrile was added to each digest to a final concentration of 30% (v/v), and peptides were labeled with 62.5 µg TMTpro-16 reagent for 1 h at 25 °C with shaking at 900 rpm. Twenty percent of each TMT-labeled sample was pooled, acidified, and diluted with 1% formic acid to pH <3 and a final acetonitrile concentration <5%. The combined sample was desalted with StageTips, dried in a SpeedVac, and reconstituted in 5% acetonitrile / 5% formic acid. LC-MS analysis. A total of 1.3 μg of peptides was analyzed by liquid chromatography–mass spectrometry (LC-MS). Peptides were separated on an Aurora Ultimate column 25cm × 75μm with 1.5 μm media and analyzed on an Orbitrap Ascend Tribrid mass spectrometer (ThermoFisher) coupled to a Vanquish Neo UHPLC (ThermoFisher) using a 55-min gradient (5–35.6% acetonitrile, 0.125% formic acid) at a 400 nL/min flow rate. Data-dependent acquisition was used with a mass range of m/z 400–1600. MS1 resolution was set at 120,000, with 50 ms maximum injection time and a 50% normalized automatic gain control (AGC) target. The top 10 most abundant species with charge states 2–6 were subjected to fragmentation. MS2 was performed with standard AGC, 35% normalized collisional energy (NCE), a 120 ms maximum ion injection time, and a 30 s dynamic exclusion window. Fragment ions were further analyzed using multi-notch synchronous precursor selection(SPS)-MS3 with 45% NCE to quantify TMT reporter ions."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Database searching. Database searching was conducted with the Comet algorithm on Masspike, an in-house search engine described previously. Searches used a concatenated target–decoy database comprising proteins from E. coli ATCC 25404, Escherichia phage T1, the SeAvs7 expression plasmid, common contaminants (e.g., keratins, trypsin), and their reversed sequences. Parameters were 25 ppm precursor mass tolerance, 1.0 Da fragment mass tolerance, fully tryptic specificity (K/R) with up to three missed cleavages, and variable Met oxidation (+15.9949 Da). For TMT experiments, TMTpro (+304.2071 Da) on Lys residues and peptide N termini was set as a static modification. Peptide-spectrum matches were filtered by a target–decoy strategy to achieve peptide-level false discovery rate (FDR) <1%, considering XCorr, ΔCn, missed cleavages, peptide length, charge state, and precursor mass accuracy. Short peptides (<7 amino acids) were discarded. Proteins were assembled from identified peptides and controlled to protein-level FDR <1%, and proteins supported by fewer than four unique peptides were discarded.  Proteomics quantification. For TMT-based quantification, peptide abundance was measured by TMT reporter ions. Reporter intensities were extracted using a 0.003 Th window centered on the theoretical m/z, selecting the most intense peak. Isotopic impurities were corrected based on the manufacturer’s specifications, and TMT signal-to-noise (S/N) values were used for quantification. Peptides were discarded if the summed S/N across 6 channels of each TMT plex was <60 or if isolation specificity was <50%. Protein abundances were computed by summing peptide S/N values. Protein quantification was normalized to ensure equal SeAvs7 protein loading across all TMT channels. SeAvs7 abundance was quantified using peptides mapping to the N-terminal 596 amino acids, including the TwinStrep tag."],"omics_type":["Proteomics"],"labhead":["Haopeng Xiao"],"instrument_platform":[""],"labhead_affiliation":["Department of Biochemistry Stanford Cancer Institute Stanford University Stanford, CA 94305, USA"],"submission_type":["PARTIAL"],"species":["Escherichia Coli","Escherichia Phage T1","Salmonella Enterica"],"submitter_mail":["jchen634@stanford.edu"],"publication":["Not available"],"submitter_affiliation":["Stanford University"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Diverse bacterial pattern recognition receptors sense the core phage proteome","description":"Recognition of foreign molecules inside cells is critical for immunity across all domains of life. Proteins of the STAND NTPase superfamily, including eukaryotic NOD-like receptors (NLRs), play a central role in this process. In bacteria and archaea, although several STAND families sense phage proteins, their functional diversity remains largely unexplored. We conducted a systematic phylogenetic analysis of prokaryotic STAND NTPases and identified at least 90 structurally distinct families associated with antiviral defense. We first show that the uncharacterized Avs7 family recognizes the major capsid protein (MCP) of tailed phages. Three cryo-EM structures of Salmonella enterica Avs7 reveal an asymmetric, butterfly-shaped tetramer that assembles stepwise via large, MCP-induced conformational changes, incorporating bacterial elongation factor Tu (EF-Tu) as a structural component that enhances defense. Using genetic screens with a library of 687 phage genes, we further show that 13 additional STAND families sense 13 conserved phage proteins, encompassing most of the core structural and replicative components of tailed phages. These include two distinct MCP-sensing families (Avs8 and Avs10) and 11 others (Avs11–21) recognizing the portal, portal adaptor, tail nozzle, head–tail connector, tail terminator, tail tube protein, tail assembly chaperone, tape measure protein, DNA polymerase, helicase/RecA-type ATPase, and single-stranded DNA annealing protein, respectively. Together, our findings highlight structure-based pattern recognition and host factor repurposing as fundamental strategies of bacterial immunity.  This dataset contains the raw mass spectrometry file from the SeAvs7 pulldown proteomics experiment used in Extended Data Figure 2 of the accepted manuscript “Diverse bacterial pattern recognition receptors sense the conserved phage proteome.” This is a partial PRIDE submission.","dates":{"publication":"2026-06-10","submission":"2026-06-09"},"accession":"PXD079457","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:1584","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:906914","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:595495","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:13037","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEW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