{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Peptide_Data_COLUMN_Abundance.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Protein_Data_COLUMN_Abundance.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Protein_Data_COLUMN_Abundance_F2_126-131_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Protein_Data_COLUMN_Abundance_F1_126-131_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Protein_Data_COLUMN_Abundance_F2_126-131_F5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Protein_Data_COLUMN_Abundance_F1_126-131_F4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Peptide_Data_COLUMN_Abundance_F3_126-131.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Peptide_Data_COLUMN_Abundance_F2_126-131.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Peptide_Data_COLUMN_Abundance_F1_126-131.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Protein_Data_COLUMN_Abundance_F1_126-131_F6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Protein_Data_COLUMN_Abundance_F2_126-131_F2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Protein_Data_COLUMN_Abundance_F1_126-131_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Protein_Data_COLUMN_Abundance_F2_126-131_F1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Protein_Data_COLUMN_Abundance_F2_126-131_F6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Protein_Data_COLUMN_Abundance_F1_126-131_F5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Protein_Data_COLUMN_Abundance_F1_126-131_F3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067881/TABLE_Supplemental_Dataset_2_TAB_Full_Protein_Data_COLUMN_Abundance_F2_126-131_F4.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["eranthie@bc.edu"],"submitter":["Daniel Bak"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Chemoproteomics","Acinetobacter baumannii","Ziga","Calprotectin","Iron-sulfur cluster","Zinc"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067881"],"sample_protocol":["A. baumannii cell lysates were labeled with desthiobiotin-iodoacetmaide (DBIA), before SP3-based protein enrichment and on-bead reduction, alkylation, and trypsin digestion. Tryptic peptides were eluted and subject to 6-plex TMT labeling. The 6 TMT sample channels were combined and either directly analyzed for protein abundance or enriched on streptavidin-agarose beads for subsequent cysteine reactivity analysis. Both samples were analyzed on a Orbitrap Exploris 240 mass spectrometer coupled to a Dionex Ultimate 3000 RSLCnano system."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["MS data from all samples were searched using the SEQUEST algorithm against a UniProt Protein Knowledgebase (UniProtKB) database of the A. baumannii ATCC 17978 proteome. Trypsin was specified as the protease with a maximum of 2 missed cleavages. A static modification of +57.021 on cysteine was included to account for alkylation by iodoacetamide. The precursor ion mass tolerance was set at 50 ppm, while the fragment ion mass tolerance was set to 0 (default setting). Peptide precursor mass tolerance was set to 10 ppm with a fragment mass tolerance of 0.02 Da. The false discovery rate (FDR) for peptide identification was set to 1%. Oxidation of methionine (+15.995) as well as acetylation (+42.011) and/or methionine-loss (+131.040) of the protein N-terminus were set as dynamic modifications and cysteine alkylation (+57.021) as well as TMT-tag labeling (+229.163) of lysine residues and peptide N-termini were set as static modifications. For TMT-based quantification, a centroid tolerance of 20 ppm was applied for integration, with a co-isolation threshold of 50% and an average reporter signal-to-noise threshold of 10. Normalization of each channel was applied based on the total peptide signal of all peptides. Peptide ratio quantification was based on S/N values and protein ratios were calculated from grouped abundances. P-values were calculated by ANOVA of individual protein abundances."],"omics_type":["Proteomics"],"labhead":["Eranthie Weerapana"],"instrument_platform":[""],"labhead_affiliation":["Boston College, Chemistry"],"submission_type":["PARTIAL"],"species":["Acinetobacter Baumannii (strain Atcc 17978 / Cip 53.77 / Lmg 1025 / Ncdc Kc755 / 5377)"],"submitter_mail":["bakd@bc.edu"],"publication":["10.1021/ACSCHEMBIO.5C00753"],"submitter_affiliation":["Boston College"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Metalloproteome remodeling in calprotectin-stressed Acinetobacter baumannii using chemoproteomics","description":"The growth of bacterial pathogens is limited by nutritional immunity, where the infected host deploys metal scavenging proteins to starve the pathogen of essential transition metals. An important transition metal-sequestering protein is the Ca2+-activated S100A8-S100A9 heterotetramer, calprotectin (CP). Prior work reveals that CP induces a significant Fe- and Zn-starvation response in the Gram-negative opportunistic pathogen, Acinetobacter baumannii, in liquid culture. Here, we employ a quantitative thiol-specific chemoproteomics platform to pinpoint changes in abundance-corrected cysteine reactivity, and by extension cellular metal occupancy in metalloenzymes, that occur when A. baumannii is challenged with physiological CP in liquid culture relative to an untreated WT control. Changes in protein abundance with CP stress reveals a pronounced Zn-limitation and Fe-starvation response and reciprocal regulation of three enzymes of central carbon metabolism, including aconitase. A majority of 2645 quantifiable Cys-containing peptides that show an increase in abundance-corrected Cys reactivity (150) are derived from known Zn- and Fe-S-cluster proteins, revealing a significant decrease in metal occupancy in the proteome. Myriad cell processes are compromised by undermetalation of the metalloproteome, including enzymes that function in the TCA cycle and respiration, GTP metabolism, ribosome remodeling, tRNA charging, and proteostasis. A direct comparison of a strain lacking the candidate metallochaperone ZigA (∆zigA) with the wild-type strain reveals that the loss of ZigA is effectively silent in this assay. We conclude that CP induces a widespread, negative impact on the metalation status of the metalloproteome that results in a significant nutrient limitation 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