ID   BLH_XYLFT               Reviewed;         431 AA.
AC   Q87AD6;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Beta-lactamase hydrolase-like protein {ECO:0000250|UniProtKB:Q9PFB0};
DE            Short=BLH {ECO:0000250|UniProtKB:Q9PFB0};
DE            EC=3.-.-.-;
GN   Name=blh {ECO:0000250|UniProtKB:Q9PFB0}; OrderedLocusNames=PD_1890;
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=183190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Temecula1 / ATCC 700964;
RX   PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA   Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA   Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA   Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA   Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA   Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA   Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA   Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA   Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA   Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA   Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA   Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's disease
RT   and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(2003).
CC   -!- FUNCTION: Could play a role in cell adherence or biofilm development.
CC       {ECO:0000250|UniProtKB:Q9PFB0}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P25910};
CC   -!- INDUCTION: Repressed by BigR. {ECO:0000250|UniProtKB:Q9PFB0}.
CC   -!- MISCELLANEOUS: Probably part of an operon that comprises bigR, PD_1892,
CC       PD_1893 and PD_1894. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE009442; AAO29721.1; -; Genomic_DNA.
DR   RefSeq; WP_004090446.1; NC_004556.1.
DR   AlphaFoldDB; Q87AD6; -.
DR   SMR; Q87AD6; -.
DR   EnsemblBacteria; AAO29721; AAO29721; PD_1890.
DR   GeneID; 58017410; -.
DR   KEGG; xft:PD_1890; -.
DR   HOGENOM; CLU_030571_9_1_6; -.
DR   OMA; LYLCHDY; -.
DR   Proteomes; UP000002516; 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   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..431
FT                   /note="Beta-lactamase hydrolase-like protein"
FT                   /id="PRO_0000305340"
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;  47371 MW;  36FEE329B6F6B3C5 CRC64;
     MKIVDINERL AISGQPNTDE FINFARRGYR SIINLRPDGE EPNQPGNDAE QAAARRAGLA
     YNFVPVIGTS ITEADIQAFQ RAIATTEGSV LVHCKSGTRA LMLYALSEVI DGRMKRDEVE
     ALGHAHGFDL GRAVTWLKRQ AIQTPRVSGF FDPRTGSIQY VVTDQTTKRC AIIDPVLDFD
     EKSGATATTN ADAILAHVEQ QGLTVEWILD THPHADHFSA AQYLKQRTGA PTAIGTHVTK
     VQRLWREIYN LPTLSTNGSQ WDHLFADGDV FNVGSIKGRV MFSPGHTLAS VTYVIGDTAF
     VHDTIFMPDS GTARADFPGG SARALWSSIQ AILSLPDETR LFTGHDYQPS GRHPRWESTV
     GEQKKANLHL AGVDETTFVA LREARDKTLP MPKLILHALQ VNVLGGQLPE PEANGRRYLK
     FPLNALEGAA W