ID A0A0D5CAH8_ECOLX Unreviewed; 169 AA. AC A0A0D5CAH8; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 22-FEB-2023, entry version 19. DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865}; DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865}; DE Flags: Fragment; GN Name=blaCTX-M-27 {ECO:0000313|EMBL:AJW75145.1}; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562 {ECO:0000313|EMBL:AJW75145.1}; RN [1] {ECO:0000313|EMBL:AJW75145.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=18 {ECO:0000313|EMBL:AJW75145.1}; RA Altayb H.N., El Amin N.M., Mukhtar M.M., Hassan M.A., Siddig M.A.; RT "Molecular Characterization of CTX-M Beta-Lactamases Genes among Pathogenic RT Enterobacteriaceae isolated from different regions in Sudan."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00001526}; CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family. CC {ECO:0000256|ARBA:ARBA00009009}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KP317202; AJW75145.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0D5CAH8; -. DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC. DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro. DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro. DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR045155; Beta-lactam_cat. DR InterPro; IPR000871; Beta-lactam_class-A. DR PANTHER; PTHR35333; BETA-LACTAMASE; 1. DR PANTHER; PTHR35333:SF3; D-ALANYL-D-ALANINE ENDOPEPTIDASE; 1. DR Pfam; PF13354; Beta-lactamase2; 1. DR PRINTS; PR00118; BLACTAMASEA. DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1. PE 3: Inferred from homology; FT DOMAIN 3..164 FT /note="Beta-lactamase class A catalytic" FT /evidence="ECO:0000259|Pfam:PF13354" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AJW75145.1" FT NON_TER 169 FT /evidence="ECO:0000313|EMBL:AJW75145.1" SQ SEQUENCE 169 AA; 17760 MW; FB53554CE8969CAE CRC64; MAAAAVLKQS ETQKQLLNQP VEIKPADLVN YNPIAEKHVN GTMTLAELSA AALQYSDNTA MNKLIAQLGG PGGVTAFARA IGDETFRLDR TEPTLNTAIP GDPRDTTTPR AMAQTLRQLT LGHALGETQR AQLVTWLKGN TTGAASIRAG LPTSWTVGDK TGSGGYGTT //