ID F6ET74_SPHCR Unreviewed; 382 AA.
AC F6ET74;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=Sphch_2813 {ECO:0000313|EMBL:AEG50448.1};
OS Sphingobium chlorophenolicum L-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG50448.1, ECO:0000313|Proteomes:UP000007150};
RN [1] {ECO:0000313|EMBL:AEG50448.1, ECO:0000313|Proteomes:UP000007150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-1 {ECO:0000313|EMBL:AEG50448.1,
RC ECO:0000313|Proteomes:UP000007150};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT "Complete sequence of chromosome 1 of Sphingobium chlorophenolicum L-1.";
RL Submitted (MAY-2011) 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}.
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DR EMBL; CP002798; AEG50448.1; -; Genomic_DNA.
DR RefSeq; WP_013848683.1; NC_015593.1.
DR AlphaFoldDB; F6ET74; -.
DR STRING; 690566.Sphch_2813; -.
DR KEGG; sch:Sphch_2813; -.
DR HOGENOM; CLU_031960_0_1_5; -.
DR Proteomes; UP000007150; Chromosome 1.
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:UniProtKB-KW.
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; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Hydrolase {ECO:0000313|EMBL:AEG50448.1}.
FT DOMAIN 95..353
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 382 AA; 41198 MW; 617A1D9FC8D23C49 CRC64;
MIMTKGGRGR RPNGGGWGRP VLLMAALSAC VSAPQQPYAA VQQRPQPSTA TFPIKPVANP
PKPFEALKVD QRETPPPGLV SVVRSLGQSF NGKVGIAVRR VGSDWTVAWN GNLLFPQQSV
SKLWVSMTFL DAVDRGKIRL SDSTTITKKD LTLFHQPTAA LVGNSGWTTT YSDLMRRAMT
QSDNTANDTL LRAVGGPEAV RGYLARRYIK DIRFGPGERL LQSTTAGLEW RQDYSIGRNF
YAARAKLPMA VRQKALDNYL ASPPDGAAPS SIVQALAKLK QNDMLSPASS QLLMSIMSEA
KTGPQRIKGG VPAGWHYLHK TGTGQELGAR STGFNDIGIM TAPDGTSYAV AVMIGSTTEP
IPTRWQLMQA VAKAVAANHE AR
//
