YFKJ_BACSU
ID YFKJ_BACSU Reviewed; 156 AA.
AC O35016; Q79EX9;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Low molecular weight protein-tyrosine-phosphatase YfkJ;
DE Short=LMPTP;
DE EC=3.1.3.48;
GN Name=yfkJ; OrderedLocusNames=BSU07880;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RA Sekiguchi J., Yamamoto H., Uchiyama S., Fajar A.;
RT "Nucleotide sequence analysis of B. subtilis cromosome in 74 degree
RT region.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP MUTAGENESIS OF CYS-8; ARG-14 AND ASP-125, CHARACTERIZATION, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=168 / JH642;
RX PubMed=15995210; DOI=10.1128/jb.187.14.4945-4956.2005;
RA Musumeci L., Bongiorni C., Tautz L., Edwards R.A., Osterman A., Perego M.,
RA Mustelin T., Bottini N.;
RT "Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.";
RL J. Bacteriol. 187:4945-4956(2005).
CC -!- FUNCTION: Dephosphorylates the phosphotyrosine-containing proteins.
CC Involved in ethanol stress resistance.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- ACTIVITY REGULATION: Efficiently inhibited by Cu(2+) ion, Zn(2+) ion
CC and N-ethylmaleimide, while the addition of Mg(2+), Ca(2+) or Fe(3+)
CC ions has minimal effect. Inhibited in a competitive manner by vanadate.
CC {ECO:0000269|PubMed:15995210}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=244 uM for p-nitrophenyl-phosphate (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:15995210};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:15995210};
CC -!- INDUCTION: By ethanol stress. Expression is sigma B-dependent.
CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC phosphatase family. {ECO:0000305}.
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DR EMBL; AL009126; CAB12617.1; -; Genomic_DNA.
DR EMBL; D83967; BAA23400.1; -; Genomic_DNA.
DR PIR; E69808; E69808.
DR RefSeq; NP_388669.1; NC_000964.3.
DR RefSeq; WP_003243480.1; NZ_JNCM01000032.1.
DR PDB; 4ETM; X-ray; 1.60 A; A/B=1-156.
DR PDBsum; 4ETM; -.
DR AlphaFoldDB; O35016; -.
DR SMR; O35016; -.
DR STRING; 224308.BSU07880; -.
DR PaxDb; O35016; -.
DR EnsemblBacteria; CAB12617; CAB12617; BSU_07880.
DR GeneID; 939191; -.
DR KEGG; bsu:BSU07880; -.
DR PATRIC; fig|224308.179.peg.852; -.
DR eggNOG; COG0394; Bacteria.
DR InParanoid; O35016; -.
DR OMA; TGSWHVG; -.
DR PhylomeDB; O35016; -.
DR BioCyc; BSUB:BSU07880-MON; -.
DR SABIO-RK; O35016; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR InterPro; IPR023485; Ptyr_pPase.
DR InterPro; IPR036196; Ptyr_pPase_sf.
DR InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR Pfam; PF01451; LMWPc; 1.
DR PRINTS; PR00719; LMWPTPASE.
DR SMART; SM00226; LMWPc; 1.
DR SUPFAM; SSF52788; SSF52788; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..156
FT /note="Low molecular weight protein-tyrosine-phosphatase
FT YfkJ"
FT /id="PRO_0000234659"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:15995210"
FT ACT_SITE 14
FT /evidence="ECO:0000269|PubMed:15995210"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:15995210"
FT MUTAGEN 8
FT /note="C->S: Completely abolishes the tyrosine-phosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:15995210"
FT MUTAGEN 14
FT /note="R->K: Completely abolishes the tyrosine-phosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:15995210"
FT MUTAGEN 125
FT /note="D->A: Completely abolishes the tyrosine-phosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:15995210"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:4ETM"
FT HELIX 14..28
FT /evidence="ECO:0007829|PDB:4ETM"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:4ETM"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:4ETM"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:4ETM"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:4ETM"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:4ETM"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:4ETM"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:4ETM"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4ETM"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:4ETM"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:4ETM"
FT HELIX 132..153
FT /evidence="ECO:0007829|PDB:4ETM"
SQ SEQUENCE 156 AA; 17269 MW; 7CDC8C4D6D0FD528 CRC64;
MISVLFVCLG NICRSPMAEA IFRDLAAKKG LEGKIKADSA GIGGWHIGNP PHEGTQEILR
REGISFDGML ARQVSEQDLD DFDYIIAMDA ENIGSLRSMA GFKNTSHIKR LLDYVEDSDL
ADVPDPYYTG NFEEVCQLIK TGCEQLLASI QKEKQL
