ID B2ZTR1_ACIBA Unreviewed; 273 AA.
AC B2ZTR1;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE Flags: Fragment;
OS Acinetobacter baumannii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=470 {ECO:0000313|EMBL:ACD67727.1};
RN [1] {ECO:0000313|EMBL:ACD67727.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19631092; DOI=10.1016/j.diagmicrobio.2009.03.029;
RA Park Y.K., Choi J.Y., Jung S.I., Park K.H., Lee H., Jung D.S., Heo S.T.,
RA Kim S.W., Chang H.H., Cheong H.S., Chung D.R., Peck K.R., Song J.H.,
RA Ko K.S.;
RT "Two distinct clones of carbapenem-resistant Acinetobacter baumannii
RT isolates from Korean hospitals.";
RL Diagn. Microbiol. Infect. Dis. 64:389-395(2009).
RN [2] {ECO:0000313|EMBL:ADI16146.1}
RP NUCLEOTIDE SEQUENCE.
RA Ko K.S.;
RT "Two distinct clones of carbapenem-resistant Acinetobacter baumannii
RT isolates from Korean hospitals.";
RL Submitted (FEB-2009) 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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; EU687473; ACD67727.1; -; Genomic_DNA.
DR EMBL; FJ763636; ADI16146.1; -; Genomic_DNA.
DR AlphaFoldDB; B2ZTR1; -.
DR SMR; B2ZTR1; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam 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; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR023650; Beta-lactam_class-A_AS.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140}.
FT DOMAIN 33..257
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACD67727.1"
FT NON_TER 273
FT /evidence="ECO:0000313|EMBL:ACD67727.1"
SQ SEQUENCE 273 AA; 29769 MW; E5133A5693E220B8 CRC64;
VSFSSFETSA QSPLLKEQIE SIVIGKKATV GVAVWGPDDL EPLLINPFEK FPMQSVFKLH
LAMLVLHQVD QGKLDLNQTV IVNRAKVLQN TWAPIMKAYQ GDEFSVPVQQ LLQYSVSHSD
SVACDLLFEL VGGPAALHDY IQSMGIKETA VVANEAQMHA DDQVQYQNWT SMKGAAEILK
KFEQKTQLSE TSQALLWKWM VETTTGPERL KGLLPAGTVV AHKTGTSGIK AGKTAATNDL
GIILLPDGRP LLVAVFVKDS AESSRTNEAI IAQ
//
