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BLH_XYLFA
ID   BLH_XYLFA               Reviewed;         431 AA.
AC   Q9PFB0;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Beta-lactamase hydrolase-like protein {ECO:0000303|PubMed:17586627};
DE            Short=BLH {ECO:0000303|PubMed:17586627};
DE            EC=3.-.-.-;
GN   Name=blh {ECO:0000303|PubMed:17586627}; OrderedLocusNames=XF_0768;
OS   Xylella fastidiosa (strain 9a5c).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=160492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9a5c;
RX   PubMed=10910347; DOI=10.1038/35018003;
RA   Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA   Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA   Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA   Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA   Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA   Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA   Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA   Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA   Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA   Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA   Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA   Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA   Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA   Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA   Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA   Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA   de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA   Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA   Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA   Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA   da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA   Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA   Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA   Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT   "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL   Nature 406:151-159(2000).
RN   [2]
RP   INDUCTION BY BIGR.
RC   STRAIN=9a5c;
RX   PubMed=17586627; DOI=10.1128/jb.00331-07;
RA   Barbosa R.L., Benedetti C.E.;
RT   "BigR, a transcriptional repressor from plant-associated bacteria,
RT   regulates an operon implicated in biofilm growth.";
RL   J. Bacteriol. 189:6185-6194(2007).
CC   -!- FUNCTION: Could play a role in cell adherence or biofilm development.
CC       {ECO:0000305|PubMed:17586627}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P25910};
CC   -!- INDUCTION: Repressed by BigR. {ECO:0000269|PubMed:17586627}.
CC   -!- MISCELLANEOUS: Part of an operon that comprises bigR, XF_0764, XF_0765
CC       and XF_0766. {ECO:0000269|PubMed:17586627}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE003849; AAF83578.1; -; Genomic_DNA.
DR   PIR; E82766; E82766.
DR   RefSeq; WP_010893291.1; NC_002488.3.
DR   AlphaFoldDB; Q9PFB0; -.
DR   SMR; Q9PFB0; -.
DR   STRING; 160492.XF_0768; -.
DR   EnsemblBacteria; AAF83578; AAF83578; XF_0768.
DR   KEGG; xfa:XF_0768; -.
DR   eggNOG; COG0491; Bacteria.
DR   eggNOG; COG3453; Bacteria.
DR   HOGENOM; CLU_030571_9_1_6; -.
DR   OMA; LYLCHDY; -.
DR   Proteomes; UP000000812; Chromosome.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050313; F:sulfur dioxygenase activity; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   CDD; cd07724; POD-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR005939; BLH_phosphatase-like.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR044528; POD-like_MBL-fold.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   Pfam; PF04273; DUF442; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR01244; TIGR01244; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..431
FT                   /note="Beta-lactamase hydrolase-like protein"
FT                   /id="PRO_0000305339"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P25910"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P25910"
FT   BINDING         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P25910"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P25910"
SQ   SEQUENCE   431 AA;  47530 MW;  C027E5A72E80FD47 CRC64;
     MRIVDINERL AISGQPNTDE FINFARRGYR SIINLRPDGE EPNQPGNDAE QAAARRAGLA
     YNFVPVIGTS ITEADIQAFQ RAIATTEGSV LVHCKSGTRA LMLYALSEVI DGRMKRDEVE
     ALGHAHGFDL GRAVTWLERQ AIQTPRVSGF FDPRTSSIQY VVTDQTTKRC AIIDPVLDFD
     EKSGATATTN ADAILAHVEQ QGLTVEWILD THPHADHFSA AQYLKQRTGA PTAIGTHVTE
     VQRLWREIYN WPTLSANGSQ WDHLFADGDV FNVGSIKGRV MFSPGHTLAS VTYVIGDTAF
     VHDTIFMPDA GTARADFPGG SARALWSSIQ TILSLPDETR LFTGHDYQPS GRHPRWESTV
     GEQKKANPHL AGVDETTFVA LREARDKTLP MPKLILHALQ VNVLGGRLPE PETNGRRYLK
     FPLNALEGAA W
 
 
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