ID A0A520ELL1_SPHSX Unreviewed; 302 AA. AC A0A520ELL1; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 24-JAN-2024, entry version 10. DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865}; DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865}; GN ORFNames=EOP66_16090 {ECO:0000313|EMBL:RZL70613.1}; OS Sphingomonas sp. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=28214 {ECO:0000313|EMBL:RZL70613.1, ECO:0000313|Proteomes:UP000315532}; RN [1] {ECO:0000313|EMBL:RZL70613.1, ECO:0000313|Proteomes:UP000315532} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PMG_033 {ECO:0000313|EMBL:RZL70613.1}; RX PubMed=30498029; DOI=.1073/pnas.1812668115; RA Crombie A.T., Larke-Mejia N.L., Emery H., Dawson R., Pratscher J., RA Murphy G.P., McGenity T.J., Murrell J.C.; RT "Poplar phyllosphere harbors disparate isoprene-degrading bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 115:13081-13086(2018). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RZL70613.1}. 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; SEGD01001082; RZL70613.1; -; Genomic_DNA. DR AlphaFoldDB; A0A520ELL1; -. DR Proteomes; UP000315532; Unassembled WGS sequence. DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro. 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 SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1. PE 3: Inferred from homology; KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251}; KW Hydrolase {ECO:0000313|EMBL:RZL70613.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000315532}. FT DOMAIN 17..275 FT /note="Beta-lactamase class A catalytic" FT /evidence="ECO:0000259|Pfam:PF13354" SQ SEQUENCE 302 AA; 32425 MW; 4B025C02D269440E CRC64; MLNAVQALGA SFKGEAGISV RDIDEGWVVA WAGDSPRPQQ SVSKFWVAIA VMDAVDRGRL SLSDPVTVTR SDLTVFHQPI RTLVGKDGYK TTIGELLRGA MTRSDNTCND VLLWRVGGPA AINRMLAEKE IAGVRFGPGE RQLQARTAGL EWRSEWAGGW GFLQARAAMT YEARDKALRR YLADPLDGAS ANGVTLGLSL LAQGKLLSAR STASLLTLMR SSKTGPLRLK SGLRPGWTLA HKTGTGQDLG TLSTGYNDVG LLVAPDGHRY AVAVMIASTR QPIPVRMRLM GDVTRAVVAA TR //