{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SngC-3-evidence.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-4-evidence.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-3-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-3-5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-4-7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-3-7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-4-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-3-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-4-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-3-8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-4-5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-3-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-3-6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-4-8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-4-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-4-4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-4-6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062346/SgnC-3-4.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["timo.glatter@mpi-marburg.mpg.de"],"submitter":["Timo Glatter"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Cell motility","Miniturbo","Myxococcus xanthus","Proximity labeling"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062346"],"tissue":["Permanent Cell Line Cell"],"sample_protocol":["Proximity-dependent biotinylation assays were performed as described in (65). For the assay, M. xanthus cultures expressing the bait and the control proteins were diluted in 40 mL 1% CTT medium to OD550nm = 0.05 and these cell suspensions were transferred to Petri dishes (Ø = 150 mm, three Petri dishes for each replicate). After incubation at 32°C in the dark for 8hrs without shaking, vanillate was added to induce the expression of the control protein, and the incubation was continued overnight. Then, for the labeling reaction, 50 μM biotin was added to each plate and the plates were incubated for 4hrs at 32°C in the dark without shaking. After labeling, cells from three plates for each replicate were harvested at 8000× g for 5 min at room temperature (RT). These cells were washed in 10 mL TPM (10 mM Tris-HCl, 1 mM potassium phosphate, 8 mM MgSO4, pH 7.6) buffer three times. Next, the cell pellets were lysed in 600 μL RIPA lysis buffer (50 mM Tris-HCl pH: 7.0, 150 mM NaCl, 1% (v/v) Triton X-100, 0.5% (w/v) sodium deoxycholate (SDC), 0.2% (w/v) SDS) supplemented with one cOmplete Protease Inhibitor Cocktail Tablette (Roche). For lysis, these cell suspensions were sonicated for 30 s and the cell debris was pelleted with a centrifugation. Then, 500 μL of the cleared lysate was added to an equilibrated G-25 desalting column and collected with centrifugation. Protein concentrations of the cleared lysate were measured using the Pierce 660nm Protein Assay Reagent (Thermo Scientific), which is supplemented with Ionic Detergent Compatibility Reagent (Thermo Scientific). When necessary the protein samples were diluted in ddH2O. Meanwhile, 40 μL of Pierce Streptavidin Magnetic Beads (Thermo Scientific) per sample were equilibrated and washed with 1 mL RIPA buffer. 500 μL desalted lysate containing 2 mg/mL total protein was mixed with 500 μL washed beads. This mixture was incubated for 1 h on a rotary shaker at 4°C. Samples were then washed 2 times with 1 ml RIPA buffer, 2 times with 1 mL 1 M KCl, and 3 times with 1 mL 50 mM Tris-HCl (pH: 7.6). Finally, the beads were washed with 1 mL 10 mM Ammonium bicarbonate (ABC) and resuspended in 100 μL ABC. After ABC was removed, the beads were shock-f 50 mM Tris-HCl (pH: 7.6) of which 20 μl were used for quality control. The remaining 80 μl were separated, and the supernatant was discarded while the beads were shock-frozen in liquid nitrogen and stored at -80°C.  Proteins were digested by an on-bead digest using 1 µg trypsin overnight at 30°C in the presence of 1 mM TCEP. Following digestion, the peptides were further alkylated with 2 mM iodoacetamide and peptides purified using solid-phase extraction on Chromabond spin columns (Macherey-Nagel). Peptides were then loaded on the LC-MS system described above. Peptide separation was carried out using a constant flow rate of 300 nL min−1 and a 45 min gradient from 6%‒35% LC buffer B (99.85% acetonitrile/0.15% formic acid). Eluting peptides were ionized at 2.3 kV. MS raw data was acquired in data-dependent mode (DDA) with a MS1 resolution of 60,000 full width at half maximum (at m/z 200) followed by MS/MS scans of the most intense ions within 1 s (cycle 1 s). The dynamic exclusion time was set to 14 s, and the ion accumulation time was set to 50 ms for MS1 and 50 ms at 17,500 resolution for MS/MS scans. The AGC was set to 3×106 for MS survey scans and 2×105 for MS/MS scans. The quadrupole isolation was 1.5 m/z, collision was induced with an HCD collision energy of 27 %."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["MS raw data was analyzed with MaxQuant (105), and an M. xanthus UniProt database. MaxQuant was executed using standard settings without the “match between runs” option. The MaxQuant “proteinGroups.txt” output file was further processed by the SafeQuant R package for statistical analysis (101, 102). The criteria for significant enrichment in samples over that of the control were: An abundance difference of ≥8 (log2-fold enrichment of ≥3) and a P-value of ≤0.0001 (−log10 P-value ≥ 4.0)."],"omics_type":["Proteomics"],"labhead":["Timo Glatter"],"instrument_platform":[""],"labhead_affiliation":["Max Planck Institute for Terrestrial Microbiology Karl-von-Frisch Str. 10  35043 Marburg Germany"],"submission_type":["PARTIAL"],"species":["Myxococcus Xanthus Dk 1622"],"submitter_mail":["timo.glatter@mpi-marburg.mpg.de"],"publication":["Not available"],"submitter_affiliation":["Max Planck Institute for Terrestrial Microbiology\nMarburg"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"SgnC, a PATAN-domain response regulator, regulates Myxococcus xanthus motility","description":"Rod-shaped Myxococcus xanthus cells move across surfaces with defined front-rear polarity using type IVa pili (T4aP)-dependent motility and gliding. The M. xanthus genome encodes 15 PATAN domain proteins, including SgnC, SgmC, and PglH, which have been implicated in motility. Notably, six of these proteins contain a MshEN_N c-di-GMP binding motif as an α-clip insertion within the PATAN domain. Given the role of c-di-GMP in motility of M. xanthus, we characterized these proteins and found that MXAN3211, MXAN5196, and SgnC are important for both motility systems of M. xanthus, while MXAN4739 is specifically required for only T4aP-dependent motility. Next, we further investigated the molecular role of SgnC in motility of M. xanthus and found that SgnC inhibits cellular reversals in a Frz chemosensory system-dependent manner. This inhibition is independent of c-di-GMP binding of SgnC and not related to changes in the accumulation of motility-associated proteins. Surprisingly, SgnC was found to be close to the proteins that regulate T4aP formation, such as SgmX, FrzS, and SopA as revealed by our proximity labeling experiments. Consistently, our data support a direct interaction between SgnC and SgmX in vivo. Localization studies confirmed the previous findings regarding MglA, SgmX, and FrzS polar localization and demonstrated that SgnC affects the polar localization of SgmX directly, as well as MglA and PilB through its potential interaction with SgmX. In turn, proper SgmX localization is essential for SgnC polar localization.  Importantly, our data suggest that SgnC and SgmX reduce sensitivity to Frz chemosensory signaling by two distinct mechanisms. First, SgnC and SgmX stimulate MglA localization at the leading cell pole, which potentially shields MglA-GTP from the Frz signaling. Second, SgnC appears to inhibit the polar binding of the Frz effector FrzZ at the leading cell pole via an unknown mechanism. Together, our findings highlight SgnC as a novel regulator of M. xanthus motility, linking chemosensory signaling to T4aP 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