ID A9FES6_SORC5 Unreviewed; 301 AA.
AC A9FES6;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=pp2c10 {ECO:0000313|EMBL:CAN94917.1};
GN OrderedLocusNames=sce4754 {ECO:0000313|EMBL:CAN94917.1};
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN94917.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN94917.1, ECO:0000313|Proteomes:UP000002139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
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};
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DR EMBL; AM746676; CAN94917.1; -; Genomic_DNA.
DR RefSeq; WP_012237386.1; NC_010162.1.
DR AlphaFoldDB; A9FES6; -.
DR STRING; 448385.sce4754; -.
DR KEGG; scl:sce4754; -.
DR eggNOG; COG0631; Bacteria.
DR HOGENOM; CLU_034545_4_1_7; -.
DR OrthoDB; 9801841at2; -.
DR BioCyc; SCEL448385:SCE_RS24410-MONOMER; -.
DR Proteomes; UP000002139; Chromosome.
DR GO; GO:0017018; F:myosin 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; PTHR47992:SF267; ALPHABET, ISOFORM E; 1.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00481; PP2C; 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:0000313|EMBL:CAN94917.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002139}.
FT DOMAIN 16..271
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 301 AA; 31691 MW; 713DFD1ABBF6D2F7 CRC64;
MPVYRTSAVE HAAAVAVAAR TDVGLSREHN EDTFLISDLA RGLAHGPAAA QASVEPPLAL
SLAVYDGSGG ASSPDAASRL AARIVHATLT RSAPRSSDAL ERSLLEAIGE AGRAVRDNAR
RSSQHRNSGT TATVAALCDE RLLLAQVGDS RAYLLRSGVL TQLTRDQTLL QSLLDSGKLR
PEEAATFEHR GVMLQALGLR EHLRIALSAV ELRREDTLLL CTDGLSDLID DQHIAAALDA
HPDPAAAASA LIDAALAAGG RDNVTALVTR FDGPWLAPPA SDRATEIVEI ARFSEGPTRR
S
//
