ID E1THC4_BURSG Unreviewed; 390 AA.
AC E1THC4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN OrderedLocusNames=BC1003_5870 {ECO:0000313|EMBL:ADN61781.1};
OS Burkholderia sp. (strain CCGE1003).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN61781.1};
RN [1] {ECO:0000313|EMBL:ADN61781.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN61781.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT "Complete sequence of chromosome2 of Burkholderia sp. CCGE1003.";
RL Submitted (SEP-2010) 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|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007840, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; CP002218; ADN61781.1; -; Genomic_DNA.
DR AlphaFoldDB; E1THC4; -.
DR STRING; 640512.BC1003_5870; -.
DR MEROPS; S12.006; -.
DR KEGG; bgf:BC1003_5870; -.
DR eggNOG; COG1680; Bacteria.
DR HOGENOM; CLU_020027_10_0_4; -.
DR OrthoDB; 5377431at2; -.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001586; Beta-lactam_class-C_AS.
DR PANTHER; PTHR46825:SF8; BETA-LACTAMASE-RELATED; 1.
DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00336; BETA_LACTAMASE_C; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140, ECO:0000313|EMBL:ADN61781.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..390
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003152221"
FT DOMAIN 37..385
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 390 AA; 41495 MW; C05A735DF2EE6FBF CRC64;
MKPGVISVMA SVVFALSTTT TTSRAANDAT GEMKAVVDAA VAPLMQKHHV PGMAIGVIAN
GNTYVFDYGV ASTETGEPVT QRTLFEVGSV SKTFTATLAA YAQLNGKMKL SDDTQRYLPS
LRGTAFGQVS LLNLGTHTPG GLPLQVPDGI HDNAQLLQYF SAWKPAYAPG TYRTYANPGI
GTLGLIAAKS MGGSYASLVE QRIFPALGMK DSYIDVPAAR MSDYAQGYTN AGAPIRMKGG
VLADEAYGVR TTAADMVRFV QANMSLIKVD DTLERAITAT HTGYFKAGPL TQDLIWEQYA
YPVTLDTLHE GNAPSMAITP TPATAIEPPL APQQDVWINK TGSTNGFGAY VAFVPRKRIG
VVLLANKNFP IEDRVGAAYR IMSALAPSRQ
//
