BL133_ACIRA
ID BL133_ACIRA Reviewed; 273 AA.
AC B3U538;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Beta-lactamase OXA-133 {ECO:0000305};
DE EC=3.5.2.6 {ECO:0000250|UniProtKB:Q51574};
DE AltName: Full=BlaOXA-23-like protein {ECO:0000303|PubMed:19015330};
DE Flags: Precursor;
GN Name=blaOXA-133 {ECO:0000303|PubMed:19015330};
OS Acinetobacter radioresistens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=40216;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND FUNCTION.
RC STRAIN=251-39C;
RX PubMed=19015330; DOI=10.1128/aac.00999-08;
RA Mendes R.E., Bell J.M., Turnidge J.D., Castanheira M., Deshpande L.M.,
RA Jones R.N.;
RT "Codetection of blaOXA-23-like gene (blaOXA-133) and blaOXA-58 in
RT Acinetobacter radioresistens: report from the SENTRY antimicrobial
RT surveillance program.";
RL Antimicrob. Agents Chemother. 53:843-844(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of beta-lactam antibiotics.
CC {ECO:0000250|UniProtKB:Q51574, ECO:0000303|PubMed:19015330}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000250|UniProtKB:Q51574};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: Is transcribed at very low levels, about 1,500-fold lower
CC than those for blaOXA-58. {ECO:0000269|PubMed:19015330}.
CC -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; EU571228; ACE63186.1; -; Genomic_DNA.
DR RefSeq; WP_063861038.1; NG_049433.1.
DR AlphaFoldDB; B3U538; -.
DR SMR; B3U538; -.
DR STRING; 575589.HMPREF0018_00443; -.
DR KEGG; ag:ACE63186; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 2: Evidence at transcript level;
KW Antibiotic resistance; Cell membrane; Hydrolase; Lipoprotein; Membrane;
KW Palmitate; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..273
FT /note="Beta-lactamase OXA-133"
FT /id="PRO_0000430517"
FT ACT_SITE 79
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P14559"
FT BINDING 216..218
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 82
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:P14489"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 273 AA; 31174 MW; F4A8F619AE6486A7 CRC64;
MNKYFTCYVV ASLFFSGCTV QHNLINETQS QIVQGHNQVI HQYFDEKNTS GVLVIQTDKK
INLYGNALSR ANTEYVPAST FKMLNALIGL ENQKTDINEI FKWKGEKRSF TTWEKDMTLG
EAMKLSAVPV YQELARRIGL DLMQKEVERI DFGNAEIGQQ VDNFWLIGPL KVTPIQEVEF
VSQLAHTQLP FSEKVQANVK NMLLLEENNG YKIFGKTGWA MDIKPQVGWL TGWVEQPDGK
IVAFALNMEM RSEMPASIRN ELLMKSLKQL NII
