ID A5CLV1_CLAM3 Unreviewed; 420 AA. AC A5CLV1; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN OrderedLocusNames=CMM_0019 {ECO:0000313|EMBL:CAN00025.1}; OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae; OC Clavibacter. OX NCBI_TaxID=443906 {ECO:0000313|EMBL:CAN00025.1, ECO:0000313|Proteomes:UP000001564}; RN [1] {ECO:0000313|EMBL:CAN00025.1, ECO:0000313|Proteomes:UP000001564} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 382 {ECO:0000313|EMBL:CAN00025.1, RC ECO:0000313|Proteomes:UP000001564}; RX PubMed=18192381; DOI=10.1128/JB.01595-07; RA Gartemann K.H., Abt B., Bekel T., Burger A., Engemann J., Flugel M., RA Gaigalat L., Goesmann A., Grafen I., Kalinowski J., Kaup O., Kirchner O., RA Krause L., Linke B., McHardy A., Meyer F., Pohle S., Ruckert C., RA Schneiker S., Zellermann E.M., Puhler A., Eichenlaub R., Kaiser O., RA Bartels D.; RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter RT michiganensis subsp. michiganensis NCPPB382 reveals a large island involved RT in pathogenicity."; RL J. Bacteriol. 190:2138-2149(2008). 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; AM711867; CAN00025.1; -; Genomic_DNA. DR RefSeq; WP_011931238.1; NC_009480.1. DR AlphaFoldDB; A5CLV1; -. DR GeneID; 56884274; -. DR KEGG; cmi:CMM_0019; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_025431_1_1_11; -. DR OrthoDB; 9801841at2; -. DR Proteomes; UP000001564; 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 Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 321..344 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 4..239 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" SQ SEQUENCE 420 AA; 45030 MW; F121B9025A5A8B66 CRC64; MATVTQAAAV SHVGKVRSNN QDSGYAGRDL FVVADGMGGH AGGDVASAVA LTRIIEADKP YASAHDAEFA LQAGLVAANQ LLAETVFEHS ELTGMGTTVS ALARVGRHVA IAHIGDSRIY LFRRGELSQI SADHTFVQRL VDSGRITPEE ALVHPRRSVL MRVLGDVDAA PEVDTQVLDT HTGDRWLLCS DGLSSYVSEE RITEILATAG TPDTVADALV KESLDHGAPD NVTVVVVDVL DEDDETAASR PAPEPVVVGS ASQPLAFGDE PAKRAVRIPS LLLHPLRATT AARDAQFEPE SDQYLEALIA EDKRRALRRR VTWLVGVTLI VAGLVLACVL GYRWTQSRYY VGESDGVVAV YNGVQQTIGP IELSHVYART EVQVDDLQPF YRQQVEQTIN ADSLAGAEEI VNRLQEAAGG //