PSP_BACSU
ID PSP_BACSU Reviewed; 260 AA.
AC P94512; Q795V9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Phosphoserine phosphatase {ECO:0000303|PubMed:28189581};
DE Short=PSP;
DE EC=3.1.3.3 {ECO:0000269|PubMed:28189581};
GN Name=serB {ECO:0000303|PubMed:28189581};
GN Synonyms=ysaA {ECO:0000312|EMBL:CAB14854.2}; OrderedLocusNames=BSU28940;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 94.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=28189581; DOI=10.1016/j.cels.2016.12.013;
RA Koo B.M., Kritikos G., Farelli J.D., Todor H., Tong K., Kimsey H.,
RA Wapinski I., Galardini M., Cabal A., Peters J.M., Hachmann A.B.,
RA Rudner D.Z., Allen K.N., Typas A., Gross C.A.;
RT "Construction and Analysis of Two Genome-Scale Deletion Libraries for
RT Bacillus subtilis.";
RL Cell Syst. 4:291-305(2017).
CC -!- FUNCTION: Catalyzes the last step of the phosphorylated serine
CC biosynthetic pathway, i.e. dephosphorylation of O-phospho-L-serine to
CC form L-serine. To a lesser extent, is also able to dephosphorylate
CC phosphothreonine, phosphoethanolamine, and histidinol phosphate in
CC vitro. {ECO:0000269|PubMed:28189581}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-serine = L-serine + phosphate;
CC Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3;
CC Evidence={ECO:0000269|PubMed:28189581};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21209;
CC Evidence={ECO:0000269|PubMed:28189581};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-D-serine = D-serine + phosphate;
CC Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
CC Evidence={ECO:0000305|PubMed:28189581};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24874;
CC Evidence={ECO:0000305|PubMed:28189581};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q72H00};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q72H00};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.116 mM for phosphoserine {ECO:0000269|PubMed:28189581};
CC KM=2.91 mM for phosphothreonine {ECO:0000269|PubMed:28189581};
CC KM=4.20 mM for phosphoethanolamine {ECO:0000269|PubMed:28189581};
CC KM=2.65 mM for histidinol phosphate {ECO:0000269|PubMed:28189581};
CC Note=The stereochemistry of phosphoserine and phosphothreonine is not
CC specified in the article. kcat is 6.9 sec(-1) with phosphoserine as
CC substrate. kcat is 9.5 sec(-1) with phosphothreonine as substrate.
CC kcat is 7.9 sec(-1) with phosphoethanolamine as substrate. kcat is
CC 7.1 sec(-1) with histidinol phosphate as substrate.
CC {ECO:0000269|PubMed:28189581};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3. {ECO:0000269|PubMed:28189581}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene cannot grow in minimal
CC medium, in contrast to wild type. ysaA, serA, and serC deletion mutants
CC have virtually identical profiles when observed across all the
CC conditions studied, likely placing YsaA in the serine biosynthesis
CC pathway. The defect is complemented by glycine, or a combination of
CC serine and other amino acids such as glutamine or glutamate. The
CC inability of serine alone to rescue the growth defect of the deletion
CC mutant is due to serine toxicity. {ECO:0000269|PubMed:28189581}.
CC -!- MISCELLANEOUS: ysaA complements E.coli serB and vice versa.
CC {ECO:0000269|PubMed:28189581}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02240, ECO:0000305}.
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DR EMBL; Z75208; CAA99609.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14854.2; -; Genomic_DNA.
DR PIR; B69983; B69983.
DR RefSeq; NP_390772.2; NC_000964.3.
DR RefSeq; WP_004398978.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P94512; -.
DR SMR; P94512; -.
DR STRING; 224308.BSU28940; -.
DR jPOST; P94512; -.
DR PaxDb; P94512; -.
DR PRIDE; P94512; -.
DR DNASU; 936546; -.
DR EnsemblBacteria; CAB14854; CAB14854; BSU_28940.
DR GeneID; 936546; -.
DR KEGG; bsu:BSU28940; -.
DR PATRIC; fig|224308.179.peg.3142; -.
DR eggNOG; COG1011; Bacteria.
DR InParanoid; P94512; -.
DR OMA; VMIGINP; -.
DR PhylomeDB; P94512; -.
DR BioCyc; BSUB:BSU28940-MON; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006564; P:L-serine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_02240; PSP; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR044266; PSP_YsaA.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cobalt; Hydrolase; Magnesium; Reference proteome;
KW Serine biosynthesis.
FT CHAIN 1..260
FT /note="Phosphoserine phosphatase"
FT /id="PRO_0000360636"
FT CONFLICT 94
FT /note="E -> G (in Ref. 1; CAA99609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 29581 MW; 2E0A0BB3B96134D3 CRC64;
MKAVFFDLDD TLLWDEKSVR TTFAETCLQA EKKYGLAPEE FEAAVREAAR ELYMSYETYP
YTVMIGINPF EGLWSNFSEP ISEGFQKLNK IVPEYRRNAW TNGLKALGID DPAYGEYLGE
FFAAERRKRP FVYDETFAVL DQLKGKYELL LLTNGDPSLQ KEKLAGVPEL APYFNEIVIS
GAFGKGKPDV SIFEHCLKLM NIEKDDAIMV GDNLNTDILG ASRAGIKTVW INRTDKKNET
DVKPDYIISS LHDLFPILEK
