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Dieu"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Cytochrome c oxidase","Metal transport","P1b-type atpase","Copper","Caulobacter vibrioides","Oxygen limitation"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067252"],"sample_protocol":["C. vibrioides NA1000 was routinely grown at 30°C under moderate shaking in PYE rich medium (0.2% bacto peptone, 0.1% yeast extract, 1 mM MgSO4, 0.5 mM CaCl2) or mineral M2G medium (5.4 mM Na2PO4, 4 mM KH2PO4, 9.35 mM NH4Cl, 0.2 % w/v 278 glucose, 10 μM FeSO4-EDTA, 0.5 mM MgSO4, 0.5 mM CaCl2). Microaerobic conditions were created by filling the 50 ml Falcon tube with PYE-rich medium and placing it in the incubator at 30°C without shaking. When required, the media were supplemented with 5 μg/mL kanamycin, 2.5 μg/mL oxytetracycline, 15 μg/mL nalidixic acid, and/or CuSO4. Exponentially growing cultures were used for all experiments.Aerobically and microaerobically grown Cells from 15 mL cultures of C. vibrioides were isolated by centrifugation for 10 min at 8,000 rpm at 4°C and washed three times with ice-cold wash buffer (10 mM Tris–HCl pH 6.8, 100 μM EDTA). Normalized pellets were resuspended in 2 mL of complete EDTA-free protease inhibitor cocktail (Roche, Mannheim, Germany). Cells were lysed under 2.4 kbar by using a cell disrupter (Cell Disruption System, One-shot model, Constant). For proper dissolution of membrane proteins, lysates are incubated for 30 min with 0.01% SDS at room temperature. Cell debris was removed by centrifugation for 15 min at 19,000 x g. The samples were treated using the optimized filter-aided sample preparation protocol. Briefly, the samples were loaded onto Millipore Microcon 30 MRCFOR030 Ultracel PL-30 filtersfilters that have been rinsed and washed beforehand with 1% formic acid (FA) and 8 M urea buffer (8 M urea in 0.1 M Tris buffer at pH 8.5), respectively. The proteins on the filter were then exposed to a reducing agent (dithiothreitol) and alkylated with iodoacetamide. The proteins were then finally digested overnight with trypsin. The final step of digestion is to transfer proteins in 20 μL of 2% acetonitrile (ACN) and 0.1% FA in an injection vial for inverted phase chromatography. The digest was analyzed using nano-LC–ESI–MS/MS tims TOF Pro (Bruker, Billerica, MA, USA) coupled with UHPLC nanoElute (Bruker).   Peptides were separated by nanoUHPLC (nanoElute, Bruker) on a 75 μm ID, 25 cm C18 column with integrated CaptiveSpray insert (Aurora, IonOpticks, Melbourne) at a flowflow rate of 400 nL/min at 50°C. LC mobile phase A was water with 0.1% formic acid (v/v), and B was ACN with formic acid 0.1% (v/v). Samples were loaded directly on the analytical column at a constant pressure of 800 bars. The digest (1 μL) was injected, and the organic content of the mobile phase was increased linearly from 2% B to 15% in 22 min, 15% B to 35% in 38 min, and 35% B to 85% in 3 min. Data acquisition on the tims TOF Pro was performed using Hystar 5.1 and timsControl 2.0. tims TOF Pro data were acquired using 100 ms TIMS accumulation time and mobility (1/K0) range from 0.6 to 1.6 Vs/cm². Mass-spectrometric analysis was carried out using the parallel accumulation serial fragmentation (PASEF) acquisition method (31). One MS spectrum was followed by 10 PASEF MSMS spectra per total cycle of 1.1 s."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["All MS/MS samples were analyzed using Mascot (Matrix Science, London, UK; version 2.8.1). Mascot was set up to search the C. vibrioides NA1000_190306 database from UniRef 100 and Contaminants_20190304 database, assuming the digestion enzyme trypsin. Mascot was searched with a fragment ion mass tolerance of 0.050 Da and a parent ion tolerance of 15 PPM. Carbamidomethyl of cysteine was specified in Mascot as a fixed modification. Oxidation of methionine and acetyl of the n-terminus was specified in Mascot as variable modifications.   Scaffold (version Scaffold_5.1.1,Scaffold_5.1.1, Proteome Software, Inc., Portland, OR) was used to validate MS/MS-based peptide and protein identifications. Peptide identifications were accepted if they could be established at a probability greater than 97.0% to achieve an FDR of less than 1.0% by the Percolator posterior error probability calculation (32). Protein identifications were accepted if they could be established at a probability greater than 50.0% to achieve an FDR of less than 1.0% and contained at least two identified peptides. Protein probabilities were assigned by the Protein Prophet algorithm (33). Proteins that contained similar peptides and could not be differentiated based on MS/MS analysis alone were grouped to satisfy the principles of parsimony. Proteins sharing significant peptide evidence were grouped into clusters."],"omics_type":["Proteomics"],"labhead":["Jean-Yves Matroule"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Research Unit in Microorganisms Biology (URBM), Department of Biology, Namur Research Institute for Life Sciences (NARILIS), University of Namur, Namur, Belgium"],"species":["Caulobacter Crescentus (strain Na1000 / Cb15n)"],"publication":["10.1016/J.JBC.2025.110786"],"submitter_mail":["marc.dieu@unamur.be"],"submitter_affiliation":["University of Namur - MaSUN"],"submitter_country":["Belgium"],"doi":["10.6019/PXD067252"],"additional_accession":[]},"is_claimable":false,"name":"Unraveling the pathway of Copper Delivery to Cytochrome c oxidases in the Free-Living Bacterium Caulobacter vibrioides","description":"Copper (Cu) is an essential micronutrient that serves as a cofactor for many enzymes but becomes toxic when present in excess. In most bacteria, CopA-like P1B-type ATPases mediate Cu detoxification by exporting cytoplasmic Cu to the periplasm or extracellular environment.    In this study, we show that Caulobacter vibrioides lacks a canonical CopA-like ATPase but encodes a single FixI/CcoI-type Cu-transporting ATPase, previously implicated in Cu delivery to the cbb₃-type cytochrome c oxidase (Cox) in species such as Rhodobacter capsulatus. C. vibrioides harbors two terminal cytochrome c oxidases in its cytoplasmic membrane: an aa₃-type and a cbb₃-type Cox. We also demonstrate that the activity of cbb₃-Cox requires the FixI-type Cu transporter and the periplasmic Cu chaperone PccA. In contrast, aa₃-Cox activity depends on PccA and the inner membrane-bound protein CtaG. Since the mechanism of Cu acquisition for aa₃-Cox remains largely unknown, we conducted a genetic screen and identified a novel outer membrane TonB-dependent receptor (TccA) that is specifically required for aa₃-Cox function.    We also showed that cbb₃-Cox is upregulated under microaerobic conditions, possibly such as those encountered on solid media where O2 diffusion is limited. Under normoxic conditions, the expression and the activity of cbb₃-Cox decrease, and aa₃-Cox becomes the predominant terminal oxidase. These findings demonstrate that C. vibrioides differentially utilizes its Cox enzymes in response to O2 availability and relies on a distinct Cu trafficking pathway for their maturation, including an outer membrane component that has not been previously described in bacterial Cu homeostasis.","dates":{"publication":"2026-04-22","submission":"2025-08-12"},"accession":"PXD067252","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","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:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","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:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","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:44685","NEWT:161934","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:1182590","NEWT:3712","NEWT:3711","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","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:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","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:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","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:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:226900","NEWT:1266738","NEWT:231490","NEWT:244704","NEWT:7725","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:72664","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:452467","NEWT:198822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