ID A1K3V8_AZOSB Unreviewed; 276 AA. AC A1K3V8; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 80. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN OrderedLocusNames=azo0896 {ECO:0000313|EMBL:CAL93513.1}; OS Azoarcus sp. (strain BH72). OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae; OC Azoarcus. OX NCBI_TaxID=418699 {ECO:0000313|EMBL:CAL93513.1, ECO:0000313|Proteomes:UP000002588}; RN [1] {ECO:0000313|EMBL:CAL93513.1, ECO:0000313|Proteomes:UP000002588} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BH72 {ECO:0000313|EMBL:CAL93513.1, RC ECO:0000313|Proteomes:UP000002588}; RX PubMed=17057704; DOI=10.1038/nbt1243; RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.; RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. RT strain BH72."; RL Nat. Biotechnol. 24:1385-1391(2006). CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC Evidence={ECO:0000256|ARBA:ARBA00001512}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC Evidence={ECO:0000256|ARBA:ARBA00001482}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AM406670; CAL93513.1; -; Genomic_DNA. DR RefSeq; WP_011764630.1; NZ_CP016210.1. DR AlphaFoldDB; A1K3V8; -. DR STRING; 62928.azo0896; -. DR KEGG; aoa:dqs_0967; -. DR KEGG; azo:azo0896; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_034545_5_0_4; -. DR OrthoDB; 9801841at2; -. DR Proteomes; UP000002588; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1. DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1. DR Pfam; PF13672; PP2C_2; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS51746; PPM_2; 1. PE 4: Predicted; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002588}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 256..275 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 7..244 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" SQ SEQUENCE 276 AA; 30056 MW; 8FAA318BAF7C7BBA CRC64; MVRPSRRAAF ACHIGGRAEQ QDRAACFTSR DGRNHLLVVA DGMGGHQGGE LASHVVMEVA ERAWSALDGL PHAPASFLER VCQQAHAEIR LAGQARGLRP CSTLAALLVS PHRAWWSYVG DSRIYVFRDG RPLWRTEDHT VVQQLVRSGR ISEAEVVDHP DRNKLLRGLG GDEPLRATHG QLRIDAATGF VLCTDGFWAT TSTEEMAPLL SASDLAAACT NAVAAAAQRG GPESDNVTIA VLQPERRTQA VNHRQLWPLY GALGLALLLL FSRFFN //