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Database: UniProt
Entry: P96717
LinkDB: P96717
Original site: P96717 
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   02-JUN-2021, entry version 113.
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   SMR; P96717; -.
DR   IntAct; P96717; 8.
DR   STRING; 224308.BSU36240; -.
DR   PaxDb; 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-MONOMER; -.
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   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
//
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