ID S6ACH9_SULDS Unreviewed; 274 AA.
AC S6ACH9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=SCD_n01781 {ECO:0000313|EMBL:BAN35593.1};
OS Sulfuricella denitrificans (strain DSM 22764 / NBRC 105220 / skB26).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sulfuricellaceae; Sulfuricella.
OX NCBI_TaxID=1163617 {ECO:0000313|EMBL:BAN35593.1, ECO:0000313|Proteomes:UP000015559};
RN [1] {ECO:0000313|EMBL:BAN35593.1, ECO:0000313|Proteomes:UP000015559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=skB26 {ECO:0000313|Proteomes:UP000015559};
RX PubMed=22773644; DOI=10.1128/AEM.01349-12;
RA Watanabe T., Kojima H., Fukui M.;
RT "Draft genome sequence of a psychrotolerant sulfur-oxidizing bacterium,
RT Sulfuricella denitrificans skB26, and proteomic insights into cold
RT adaptation.";
RL Appl. Environ. Microbiol. 78:6545-6549(2012).
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; AP013066; BAN35593.1; -; Genomic_DNA.
DR RefSeq; WP_009204785.1; NC_022357.1.
DR AlphaFoldDB; S6ACH9; -.
DR STRING; 1163617.SCD_n01781; -.
DR KEGG; sdr:SCD_n01781; -.
DR eggNOG; COG0631; Bacteria.
DR HOGENOM; CLU_034545_4_1_4; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000015559; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000015559}.
FT DOMAIN 8..255
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 274 AA; 30053 MW; 620294FA7A3B698F CRC64;
MTVQSRVEFA SATDTGVVRK FNEDSIATDS EIGLMMLADG MGGYMAGDVA SALAISVVKE
ELAAALGNLE SVENDAAKRY LPQTLAVKRA AEKANQMILR VARKNSQCQD MGTTLTLAVF
HDDRISIAHV GDSRLYRLRY DRLEQLTMDH SLLQGQVEAG LIDSGDAKLS HNRNLVTRAL
GKEEKVEVDV REEGMLPGDL YLLCSDGLND MVEDTDIELA LCELKANLPL AANLLVQMAN
DNGGHDNVSV VLARVRAQSA RRGLFERLFG WFRR
//
