ID   Q5FJH7_LACAC            Unreviewed;       251 AA.
AC   Q5FJH7;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=LBA1318 {ECO:0000313|EMBL:AAV43147.1};
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621 {ECO:0000313|Proteomes:UP000006381};
RN   [1] {ECO:0000313|EMBL:AAV43147.1, ECO:0000313|Proteomes:UP000006381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM
RC   {ECO:0000313|Proteomes:UP000006381};
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV43147.1; -; Genomic_DNA.
DR   RefSeq; WP_011254417.1; NC_006814.3.
DR   RefSeq; YP_194178.1; NC_006814.3.
DR   AlphaFoldDB; Q5FJH7; -.
DR   STRING; 272621.LBA1318; -.
DR   GeneID; 56942904; -.
DR   KEGG; lac:LBA1318; -.
DR   PATRIC; fig|272621.13.peg.1248; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_4_1_9; -.
DR   OrthoDB; 9801841at2; -.
DR   BioCyc; LACI272621:G1G49-1297-MONOMER; -.
DR   Proteomes; UP000006381; 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   NCBIfam; NF033484; Stp1_PP2C_phos; 1.
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   Hydrolase {ECO:0000313|EMBL:AAV43147.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006381}.
FT   DOMAIN          3..243
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   251 AA;  27720 MW;  E26A3BE707EA2EFA CRC64;
     MIETAYASSI GKVRKSNQDF VQVFKNHADI TLAIVCDGMG GHQGGDVAST MAVTHLGHNF
     KMTDFTNADL AQKWLEVQLK SENETILKTA DKFPDLNGMG TTIVLAFAFA DTALIAHLGD
     SRAYNYSEGK FVQLTEDHSL VNELVKMRQI TREQAKHHPQ KNIITQALGV SSTIDPEFDE
     IKLGENDIIL LCTDGLTNSL NDPQIQQILA TKELSLKERC NKLISEANRL GGGDNITVCL
     IWNKEDKSSD R
//