PA2200 is a 531-aa inner-membrane protein with two predicted transmembrane helices flanking a periplasmic region and a C-terminal cytoplasmic EAL domain with an intact catalytic motif. It is a c-di-GMP-specific phosphodiesterase: lysates of cells overexpressing PA2200 degrade added c-di-GMP. Its EAL domain groups phylogenetically with those of PA2818 (Arr) and PA3285, which likewise lack a GGDEF domain. Overexpressing PA2200 reduces type III secretion-dependent killing of CHO cells, consistent with lower c-di-GMP. An insertion mutant has no biofilm phenotype under standard conditions. The signal sensed by its periplasmic region and its physiological role are unknown.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: PM IBD at PTN002105365. PA2200 has two predicted TM helices, like the membrane-anchored E. coli seeds, so the claim holds for this gene. Reason: Consistent with PA2200's topology. The node-level concern (soluble clade members such as RocR and PA2133) is recorded once in the rocR review and does not affect PA2200. Supporting Evidence: file:PSEAE/PA2200/PA2200-uniprot.txt FT TRANSMEM 248..273 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" |
| GO:0071111 cyclic-guanylate-specific phosphodiesterase activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from the 18-seed PTN002105365 IBD; PA2200 appears among its own sources because of its own IDA row, which is expected. Reason: Correct for PA2200, which keeps an intact EAL motif and has lysate PDE activity. Node-level defects are recorded in the rocR review. Supporting Evidence: file:PSEAE/PA2200/PA2200-notes.md PA2133 ETL — +(71) PA2200 EAL +(61) |
| GO:1900190 regulation of single-species biofilm formation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: IBA from the 4-seed PTN009140332 IBD (seeds bifA, PA2133, E. coli PdeF, arr). PA2200 is not a seed and has no gene-specific biofilm data; its insertion mutant had no biofilm phenotype. Reason: The IBD is sound on bifA's evidence, and a membrane c-di-GMP PDE plausibly contributes to biofilm regulation. With no gene-specific support and no mutant phenotype, the row is kept as non-core. Supporting Evidence: file:PSEAE/PA2200/PA2200-notes.md insertion in genes encoding only PDE domains, with the exception of pvrR , did not cause a biofilm-related phenotype in our assay. |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: SubCell mapping (Cell membrane; multi-pass). The UniProt statement itself is ARBA-derived, but the two Phobius TM helices independently support it. Reason: Consistent with the predicted topology; same claim as the IBA row. Supporting Evidence: file:PSEAE/PA2200/PA2200-uniprot.txt FT TRANSMEM 20..39 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" |
| GO:0071111 cyclic-guanylate-specific phosphodiesterase activity | IEA GO_REF:0000003 | ACCEPT | Summary: EC mapping; consistent with lysate PDE activity. Reason: Correct core activity. Supporting Evidence: file:PSEAE/PA2200/PA2200-notes.md PA2133 ETL — +(71) PA2200 EAL +(61) |
| GO:0071111 cyclic-guanylate-specific phosphodiesterase activity | IDA PMID:16477007 Analysis of Pseudomonas aeruginosa diguanylate cyclases and ... | ACCEPT | Summary: PseudoCAP IDA and PA2200's seeding of PTN002105365. Lysates of a PA2200-overexpressing strain degraded 61% of added c-di-GMP (Table 1, full text read on PMC). Reason: Seed verdict SOUND. A lysate assay on an overexpressing strain is crude but direct, and the EAL motif is intact. No purified-enzyme data exist. Supporting Evidence: file:PSEAE/PA2200/PA2200-notes.md PA2133 ETL — +(71) PA2200 EAL +(61) |
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Download this section (compressed HTML)Experiment: Purify the cytoplasmic EAL domain of PA2200 for c-di-GMP hydrolysis kinetics, and screen a clean deletion for motility, dispersal and virulence phenotypes across conditions.
What is not known — curated, literature-grounded statements of the open unknowns (the inverse of core functions).
Gap: The signal sensed by the periplasmic region of PA2200 and the cellular process that its c-di-GMP hydrolysis regulates are unknown; its insertion mutant has no biofilm phenotype under standard conditions.
BIOLOGY
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