ID   BLA24_ECOLX             Reviewed;         286 AA.
AC   Q9S169;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Beta-lactamase SHV-24;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=shv24;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=HKY453;
RX   PubMed=10817740; DOI=10.1128/aac.44.6.1725-1727.2000;
RA   Kurokawa H., Yagi T., Shibata N., Shibayama K., Kamachi K., Arakawa Y.;
RT   "A new SHV-derived extended-spectrum beta-lactamase (SHV-24) that
RT   hydrolyzes ceftazidime through a single-amino-acid substitution (D179G) in
RT   the omega-loop.";
RL   Antimicrob. Agents Chemother. 44:1725-1727(2000).
CC   -!- FUNCTION: Hydrolyzes ampicillin. Can also hydrolyze cephaloridine,
CC       aztreonam and ceftazidime with a low catalytic rate.
CC       {ECO:0000269|PubMed:10817740}.
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10101};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=32 uM for ampicillin {ECO:0000269|PubMed:10817740};
CC         KM=210 uM for cephaloridine {ECO:0000269|PubMed:10817740};
CC         KM=500 uM for aztreonam {ECO:0000269|PubMed:10817740};
CC         KM=30 uM for ceftazidime {ECO:0000269|PubMed:10817740};
CC         Vmax=0.366 umol/min/ug enzyme with ampicillin as substrate
CC         {ECO:0000269|PubMed:10817740};
CC         Vmax=0.434 umol/min/ug enzyme with cephaloridine as substrate
CC         {ECO:0000269|PubMed:10817740};
CC         Vmax=0.135 umol/min/ug enzyme with aztreonam as substrate
CC         {ECO:0000269|PubMed:10817740};
CC         Vmax=0.008 umol/min/ug enzyme with ceftazidime as substrate
CC         {ECO:0000269|PubMed:10817740};
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; AB023477; BAA84973.1; -; Genomic_DNA.
DR   RefSeq; WP_063864670.1; NG_050061.1.
DR   AlphaFoldDB; Q9S169; -.
DR   SMR; Q9S169; -.
DR   KEGG; ag:BAA84973; -.
DR   SABIO-RK; Q9S169; -.
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; -; 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; PTHR35333; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Disulfide bond; Hydrolase; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..286
FT                   /note="Beta-lactamase SHV-24"
FT                   /id="PRO_0000016988"
FT   ACT_SITE        66
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         230..232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..119
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  31166 MW;  5EA9990BC8B0AAFF CRC64;
     MRYIRLCIIS LLATLPLAVH ASPQPLEQIK LSESQLSGRV GMIEMDLASG RTLTAWRADE
     RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD YSPVSEKHLA DGMTVGELCA
     AAITMSDNSA ANLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARGTTTPA
     SMAATLRKLL TSQRLSARSQ RQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGAGERGARG
     IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR