YWQE_BACSU
ID YWQE_BACSU Reviewed; 254 AA.
AC P96717;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Tyrosine-protein phosphatase YwqE;
DE EC=3.1.3.48;
GN Name=ywqE; OrderedLocusNames=BSU36240;
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=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
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 CHARACTERIZATION, AND MUTAGENESIS OF ASP-3; HIS-5; HIS-42; HIS-136; ASP-194
RP AND HIS-196.
RX PubMed=15866923; DOI=10.1128/jb.187.10.3384-3390.2005;
RA Mijakovic I., Musumeci L., Tautz L., Petranovic D., Edwards R.A.,
RA Jensen P.R., Mustelin T., Deutscher J., Bottini N.;
RT "In vitro characterization of the Bacillus subtilis protein tyrosine
RT phosphatase YwqE.";
RL J. Bacteriol. 187:3384-3390(2005).
RN [4]
RP FUNCTION.
RX PubMed=16549871; DOI=10.1093/nar/gkj514;
RA Mijakovic I., Petranovic D., Macek B., Cepo T., Mann M., Davies J.,
RA Jensen P.R., Vujaklija D.;
RT "Bacterial single-stranded DNA-binding proteins are phosphorylated on
RT tyrosine.";
RL Nucleic Acids Res. 34:1588-1596(2006).
CC -!- FUNCTION: Dephosphorylates the phosphotyrosine-containing proteins
CC YwqD, YwqF and Ssb. {ECO:0000269|PubMed:16549871}.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- ACTIVITY REGULATION: Inhibited by vanadate and sodium pyrophosphate.
CC Not inhibited by sodium fluoride.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimally active at alkaline pHs. Activity increases with increasing
CC pHs.;
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC CpsB/CapC family. {ECO:0000305}.
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DR EMBL; Z92952; CAB07456.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15641.1; -; Genomic_DNA.
DR PIR; H70066; H70066.
DR RefSeq; NP_391505.1; NC_000964.3.
DR RefSeq; WP_003227815.1; NZ_JNCM01000034.1.
DR PDB; 3QY6; X-ray; 1.80 A; A=1-254.
DR PDB; 3QY7; X-ray; 1.62 A; A=1-254.
DR PDBsum; 3QY6; -.
DR PDBsum; 3QY7; -.
DR AlphaFoldDB; P96717; -.
DR SMR; P96717; -.
DR IntAct; P96717; 8.
DR STRING; 224308.BSU36240; -.
DR PaxDb; P96717; -.
DR PRIDE; P96717; -.
DR EnsemblBacteria; CAB15641; CAB15641; BSU_36240.
DR GeneID; 936893; -.
DR KEGG; bsu:BSU36240; -.
DR PATRIC; fig|224308.179.peg.3922; -.
DR eggNOG; COG4464; Bacteria.
DR InParanoid; P96717; -.
DR OMA; VHPERNS; -.
DR PhylomeDB; P96717; -.
DR BioCyc; BSUB:BSU36240-MON; -.
DR SABIO-RK; P96717; -.
DR EvolutionaryTrace; P96717; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR InterPro; IPR016667; Caps_polysacc_synth_CpsB/CapC.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR PANTHER; PTHR39181; PTHR39181; 1.
DR Pfam; PF19567; CpsB_CapC; 1.
DR PIRSF; PIRSF016557; Caps_synth_CpsB; 1.
DR SUPFAM; SSF89550; SSF89550; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Manganese; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..254
FT /note="Tyrosine-protein phosphatase YwqE"
FT /id="PRO_0000057893"
FT MUTAGEN 3
FT /note="D->A: Large decrease in activity."
FT /evidence="ECO:0000269|PubMed:15866923"
FT MUTAGEN 5
FT /note="H->A: Large decrease in activity."
FT /evidence="ECO:0000269|PubMed:15866923"
FT MUTAGEN 7
FT /note="H->A: Large decrease in activity."
FT MUTAGEN 42
FT /note="H->A: Large decrease in activity."
FT /evidence="ECO:0000269|PubMed:15866923"
FT MUTAGEN 136
FT /note="H->A: Large decrease in activity."
FT /evidence="ECO:0000269|PubMed:15866923"
FT MUTAGEN 194
FT /note="D->A: Large decrease in activity."
FT /evidence="ECO:0000269|PubMed:15866923"
FT MUTAGEN 196
FT /note="H->A: Large decrease in activity."
FT /evidence="ECO:0000269|PubMed:15866923"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3QY7"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:3QY7"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:3QY7"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3QY7"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:3QY7"
FT HELIX 52..68
FT /evidence="ECO:0007829|PDB:3QY7"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:3QY7"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3QY7"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:3QY7"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3QY7"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:3QY7"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:3QY7"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:3QY7"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3QY7"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:3QY7"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:3QY7"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:3QY7"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:3QY7"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:3QY7"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:3QY7"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:3QY7"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:3QY7"
FT HELIX 205..216
FT /evidence="ECO:0007829|PDB:3QY7"
FT HELIX 219..232
FT /evidence="ECO:0007829|PDB:3QY7"
SQ SEQUENCE 254 AA; 28958 MW; E2625AE51E0E9A94 CRC64;
MIDIHCHILP AMDDGAGDSA DSIEMARAAV RQGIRTIIAT PHHNNGVYKN EPAAVREAAD
QLNKRLIKED IPLHVLPGQE IRIYGEVEQD LAKRQLLSLN DTKYILIEFP FDHVPRYAEQ
LFYDLQLKGY IPVIAHPERN REIRENPSLL YHLVEKGAAS QITSGSLAGI FGKQLKAFSL
RLVEANLIHF VASDAHNVKT RNFHTQEALY VLEKEFGSEL PYMLTENAEL LLRNQTIFRQ
PPQPVKRRKL FGFF
