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Database: UniProt
Entry: A0A1D7QM24_9SPHI
LinkDB: A0A1D7QM24_9SPHI
Original site: A0A1D7QM24_9SPHI 
ID   A0A1D7QM24_9SPHI        Unreviewed;       470 AA.
AC   A0A1D7QM24;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   ORFNames=BFS30_22635 {ECO:0000313|EMBL:AOM79707.1};
OS   Pedobacter steynii.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=430522 {ECO:0000313|EMBL:AOM79707.1, ECO:0000313|Proteomes:UP000094313};
RN   [1] {ECO:0000313|EMBL:AOM79707.1, ECO:0000313|Proteomes:UP000094313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX4 {ECO:0000313|EMBL:AOM79707.1,
RC   ECO:0000313|Proteomes:UP000094313};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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; CP017141; AOM79707.1; -; Genomic_DNA.
DR   RefSeq; WP_069381369.1; NZ_CP017141.1.
DR   AlphaFoldDB; A0A1D7QM24; -.
DR   KEGG; psty:BFS30_22635; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000094313; 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; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   PANTHER; PTHR13832:SF827; PROTEIN PHOSPHATASE 2C-LIKE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF13672; PP2C_2; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094313};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..247
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   470 AA;  51955 MW;  09BD6F6ED4127BBF CRC64;
     MDNNYFGITD IGKIRDNNED AFIAERSSAN DFIIACVIDG VGGYSGGEIA AEITRKSILH
     YLANPEADLP LLMKEAILAA DAQIIVEKQR VKGHENMACV LTLAVIDLRQ NKLYYVHVGD
     TRLYLLRDNS LIKISKDQSF VGFMEDSGRL TEEQAMQHPK RNEINKALGF GMGMAGQEDY
     LETGESPFLP GDLLLLCSDG LSDMVNKKEI VSILTTDSSL REKGTQLINA ANTNGGLDNI
     TVVLVKNDNQ SRIHEATKPA SRPKNTITAP ATVNELDIPE MQAPPKNNKN IIILLSALCL
     ILLVACIYLF WQKYQLSYSK EPLPVKTGNG KNAQEIKLQE ALHQLKGNTL ILSDSIFKSP
     IILTESLQFE KDSLFLISKN QITIKSDSAF RGNAMIIQSA NNYVYLENIT FQDFNTAISS
     KNNALVLKNI QFKNSPNAIQ TIYDLPAKGY INGKISRSSF KADSIPNTSK
//
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