PHOE_BACSU
ID PHOE_BACSU Reviewed; 193 AA.
AC O07617; Q796T5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Uncharacterized phosphatase PhoE;
DE EC=3.1.3.-;
GN Name=phoE; Synonyms=yhfR; OrderedLocusNames=BSU10340;
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;
RA Noback M.A., Terpstra P., Holsappel S., Venema G., Bron S.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=10869096; DOI=10.1128/jb.182.14.4121-4123.2000;
RA Pearson C.L., Loshon C.A., Pedersen L.B., Setlow B., Setlow P.;
RT "Analysis of the function of a putative 2,3-diphosphoglyceric acid-
RT dependent phosphoglycerate mutase from Bacillus subtilis.";
RL J. Bacteriol. 182:4121-4123(2000).
RN [4]
RP FUNCTION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17693564; DOI=10.1128/aem.00861-07;
RA Withers S.T., Gottlieb S.S., Lieu B., Newman J.D., Keasling J.D.;
RT "Identification of isopentenol biosynthetic genes from Bacillus subtilis by
RT a screening method based on isoprenoid precursor toxicity.";
RL Appl. Environ. Microbiol. 73:6277-6283(2007).
CC -!- FUNCTION: Phosphatase with broad substrate specificity. Does not have
CC phosphoglycerate mutase activity. {ECO:0000269|PubMed:10869096,
CC ECO:0000269|PubMed:17693564}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:10869096}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. GpmB
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, has no
CC phosphoglycerate mutase activity. {ECO:0000305}.
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DR EMBL; Y14084; CAA74541.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12874.1; -; Genomic_DNA.
DR PIR; G69831; G69831.
DR RefSeq; NP_388915.1; NC_000964.3.
DR RefSeq; WP_003233157.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O07617; -.
DR SMR; O07617; -.
DR STRING; 224308.BSU10340; -.
DR PaxDb; O07617; -.
DR PRIDE; O07617; -.
DR EnsemblBacteria; CAB12874; CAB12874; BSU_10340.
DR GeneID; 939773; -.
DR KEGG; bsu:BSU10340; -.
DR PATRIC; fig|224308.179.peg.1112; -.
DR eggNOG; COG0406; Bacteria.
DR InParanoid; O07617; -.
DR OMA; TEWNVAR; -.
DR PhylomeDB; O07617; -.
DR BioCyc; BSUB:BSU10340-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..193
FT /note="Uncharacterized phosphatase PhoE"
FT /id="PRO_0000360623"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT ACT_SITE 82
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 193 AA; 21994 MW; 30B66B1AE2B18D5F CRC64;
MTAVCLVRHG ETDWNLQQKC QGKTDIPLNA TGERQARETG EYVKDFSWDI IVTSPLKRAK
RTAEIINEYL HLPIVEMDDF KERDYGDAEG MPLEERTKRY PDNIYPNMET LEELTDRLMG
GLAKVNQAYP NKKVLIVAHG AAIHALLTEI SGGDPELQST RLVNACLSNI EFAEEKWRIK
DYNINSHLSG FIK
