ID Q2SEC1_HAHCH Unreviewed; 241 AA. AC Q2SEC1; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 04-NOV-2026, entry version 99. DE SubName: Full=Serine/threonine protein phosphatase {ECO:0000313|EMBL:ABC31003.1}; GN OrderedLocusNames=HCH_04296 {ECO:0000313|EMBL:ABC31003.1}; OS Hahella chejuensis (strain KCTC 2396). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Oceanospirillales; Hahellaceae; Hahella. OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC31003.1, ECO:0000313|Proteomes:UP000000238}; RN [1] {ECO:0000313|EMBL:ABC31003.1, ECO:0000313|Proteomes:UP000000238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC31003.1, RC ECO:0000313|Proteomes:UP000000238}; RX PubMed=16352867; DOI=10.1093/nar/gki1016; RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., RA Oh T.K., Kim J.F.; RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an RT algicidal agent."; RL Nucleic Acids Res. 33:7066-7073(2005). 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 --------------------------------------------------------------------------- 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; CP000155; ABC31003.1; -; Genomic_DNA. DR RefSeq; WP_011398070.1; NC_007645.1. DR AlphaFoldDB; Q2SEC1; -. DR STRING; 349521.HCH_04296; -. DR KEGG; hch:HCH_04296; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_034545_0_3_6; -. DR OMA; AADCYSG; -. DR OrthoDB; 9801841at2; -. DR Proteomes; UP000000238; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:UniProtKB-EC. 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; PTHR13832:SF827; PROTEIN PHOSPHATASE 1L; 1. DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 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 Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01082}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01082}; KW Protein phosphatase {ECO:0000256|PROSITE-ProRule:PRU01082}; KW Reference proteome {ECO:0000313|Proteomes:UP000000238}. FT DOMAIN 5..240 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" SQ SEQUENCE 241 AA; 26438 MW; 8CC1ADA50C86DACE CRC64; MANHLNWKSE LRTHVGNVRK HNEDAALARD AGGLWAVADG MGGHHAGEVA SQKIVEQLDH LLLRAYLVDV VEQIEDALIK TNEDLLAYAQ QELNGSKVGS TVACLFVRYG VAVAVWAGDS RVYLMRNHKL HRITHDHSKV QELVDKGDMT PAQAEQSSFR NMLTRAVGVH EHLCVDVNAI LVEPSDRFLI CTDGLYNEVG EAGLAKAMQI RSLSEAADTL LTETLNGDAK DNVTFIALQA H //