ID Q6LP74_PHOPR Unreviewed; 631 AA. AC Q6LP74; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 02-SEP-2026, entry version 116. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082}; DE EC=3.1.3.16 {ECO:0000256|PROSITE-ProRule:PRU01082}; DE AltName: Full=Serine/threonine-protein {ECO:0000256|PROSITE-ProRule:PRU10027}; DE EC=2.7.11.1 {ECO:0000256|PROSITE-ProRule:PRU10027}; GN Name=BLL2800 {ECO:0000313|EMBL:CAG20902.1}; GN OrderedLocusNames=PBPRA2520 {ECO:0000313|EMBL:CAG20902.1}; OS Photobacterium profundum (strain SS9). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG20902.1, ECO:0000313|Proteomes:UP000000593}; RN [1] {ECO:0000313|Proteomes:UP000000593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593}; RX PubMed=15746425; DOI=10.1126/science.1103341; RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., RA Bartlett D.H., Valle G.; RT "Life at depth: Photobacterium profundum genome sequence and expression RT analysis."; RL Science 307:1459-1461(2005). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00048679, ECO:0000256|PROSITE- CC ProRule:PRU10027}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00047899, ECO:0000256|PROSITE- CC ProRule:PRU10027}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-seryl-[protein] + H2O = 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; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU01082}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-threonyl-[protein] + H2O = 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; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU01082}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU01082}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU01082}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000256|PROSITE-ProRule:PRU01082}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000256|PROSITE-ProRule:PRU00159}. 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; CR378671; CAG20902.1; -; Genomic_DNA. DR AlphaFoldDB; Q6LP74; -. DR STRING; 298386.PBPRA2520; -. DR KEGG; ppr:PBPRA2520; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_034273_0_0_6; -. DR Proteomes; UP000000593; Chromosome 1. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. DR CDD; cd00143; PP2Cc; 1. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF13672; PP2C_2; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51746; PPM_2; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01082}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE- KW ProRule:PRU00159}; Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01082}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Protein phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082}; KW Reference proteome {ECO:0000313|Proteomes:UP000000593}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|PROSITE-ProRule:PRU00159}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00159}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 608..628 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 56..288 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" FT DOMAIN 321..585 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT ACT_SITE 447 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10027" SQ SEQUENCE 631 AA; 71260 MW; 4AC862AC45B58C06 CRC64; MGAYMTQTSS NTYSAKECVS SSDLNKIEVA LNTPSKQQKS SLFSSNKKVE NRLHVAMGGY SIAGVRPVNQ DAFSVKLPSN NNVVKYKGIV ACIADGVSCS ENAQQASQTS VTQFIDEYYS TPDSWNVKKS ASTVLTSLNQ WLYQHGQYSD LRHNGLVTTF SGVVLKSNTA HLIHVGDSRI YRYRQGKLIL LTRDHCRKQK GRNSFLTRAL GMDSHLEVDY QQKSIEKGDI FFLSTDGVHE WLSNNEITAL IYEGKKENRD REQQAKAIIA QAQANGSDDN LSCLLLEVLD VPSLNIEEAY NQLTEKVIPP ILKVGNTIDN LKVVDVIHSG TRSHVYLVKK IEDNAEAAHY ILKAPSPNFA EDLLYLEGFT REHWVGCQLN NASIMKIYDH NTSSPFLYHL CEYVEGQSLR QWMYDNPKPS FESVRIIAKG MIKAIRVFQR MEMVHRDLKP ENIMLAKDGR IVIIDFGTVQ VDGLDEIASP VSEDVPMGSV DYIAPEYLAG ERAQHQSDIF SIGVILFEML TGKLPYVTRP SRVVQSIPHQ DWHYISACQY REDIPFWLDI TLKKACQPSP KLRYQAMSEL QQDFTSPNPQ IVAEYDKSPL IKRYPISFWK VVSLVLLVIV LAEGYFLMTI S //