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NAP_BACSU
ID   NAP_BACSU               Reviewed;         300 AA.
AC   P96688; Q797G3;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Uncharacterized carboxylesterase nap;
DE            EC=3.1.1.1;
GN   Name=nap; OrderedLocusNames=BSU05440;
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   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-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   X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 1-294 IN COMPLEX WITH TRIETHYLENE
RP   GLYCOL, AND SUBUNIT.
RG   Joint center for structural genomics (JCSG);
RT   "Crystal structure of putative hydrolase (2632844) from Bacillus subtilis
RT   at 1.96 A resolution.";
RL   Submitted (SEP-2007) to the PDB data bank.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC         Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.3}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; AB001488; BAA19378.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12351.1; -; Genomic_DNA.
DR   PIR; C69664; C69664.
DR   RefSeq; NP_388425.1; NC_000964.3.
DR   RefSeq; WP_003242638.1; NZ_JNCM01000031.1.
DR   PDB; 2R11; X-ray; 1.96 A; A/B/C/D=1-294.
DR   PDBsum; 2R11; -.
DR   AlphaFoldDB; P96688; -.
DR   SMR; P96688; -.
DR   STRING; 224308.BSU05440; -.
DR   ESTHER; bacsu-cbxnp; 6_AlphaBeta_hydrolase.
DR   PaxDb; P96688; -.
DR   PRIDE; P96688; -.
DR   DNASU; 938069; -.
DR   EnsemblBacteria; CAB12351; CAB12351; BSU_05440.
DR   GeneID; 938069; -.
DR   KEGG; bsu:BSU05440; -.
DR   PATRIC; fig|224308.179.peg.583; -.
DR   eggNOG; COG0596; Bacteria.
DR   InParanoid; P96688; -.
DR   OMA; SSTMWYP; -.
DR   PhylomeDB; P96688; -.
DR   BioCyc; BSUB:BSU05440-MON; -.
DR   EvolutionaryTrace; P96688; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Reference proteome.
FT   CHAIN           1..300
FT                   /note="Uncharacterized carboxylesterase nap"
FT                   /id="PRO_0000360816"
FT   ACT_SITE        274
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   SITE            130
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   HELIX           13..26
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   STRAND          34..38
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   STRAND          43..51
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   STRAND          57..61
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   HELIX           68..71
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   HELIX           75..81
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   STRAND          82..87
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   HELIX           105..118
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   STRAND          122..129
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   HELIX           131..142
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   STRAND          147..154
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   HELIX           164..171
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   TURN            172..174
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   HELIX           178..186
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   TURN            187..189
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   HELIX           195..206
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   STRAND          209..211
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   HELIX           227..231
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   STRAND          237..242
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   HELIX           250..260
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   STRAND          265..269
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   HELIX           276..279
FT                   /evidence="ECO:0007829|PDB:2R11"
FT   HELIX           281..292
FT                   /evidence="ECO:0007829|PDB:2R11"
SQ   SEQUENCE   300 AA;  33953 MW;  FA818689172007AC CRC64;
     MSNHSSSIPE LSDNGIRYYQ TYNESLSLWP VRCKSFYIST RFGQTHVIAS GPEDAPPLVL
     LHGALFSSTM WYPNIADWSS KYRTYAVDII GDKNKSIPEN VSGTRTDYAN WLLDVFDNLG
     IEKSHMIGLS LGGLHTMNFL LRMPERVKSA AILSPAETFL PFHHDFYKYA LGLTASNGVE
     TFLNWMMNDQ NVLHPIFVKQ FKAGVMWQDG SRNPNPNADG FPYVFTDEEL RSARVPILLL
     LGEHEVIYDP HSALHRASSF VPDIEAEVIK NAGHVLSMEQ PTYVNERVMR FFNAETGISR
 
 
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