ID   BLA4_KLEPN              Reviewed;         265 AA.
AC   P37323;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Beta-lactamase SHV-4;
DE            EC=3.5.2.6;
DE   AltName: Full=Ceftazidimase 5;
DE            Short=CAZ-5;
GN   Name=bla; Synonyms=shv4;
OS   Klebsiella pneumoniae.
OG   Plasmid pUD21.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=210-2;
RX   PubMed=2694955; DOI=10.1128/aac.33.12.2160;
RA   Peduzzi J., Barthelemy M., Tiwari K., Mattioni D., Labia R.;
RT   "Structural features related to hydrolytic activity against ceftazidime of
RT   plasmid-mediated SHV-type CAZ-5 beta-lactamase.";
RL   Antimicrob. Agents Chemother. 33:2160-2163(1989).
CC   -!- FUNCTION: SHV enzymes hydrolyze broad spectrum cephalosporins notably
CC       cefotaxime and ceftazidime. SHV-4 causes particularly high levels of
CC       resistance to aztreonam and ceftazidime.
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   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   PIR; A60448; A60448.
DR   AlphaFoldDB; P37323; -.
DR   SMR; P37323; -.
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   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   1: Evidence at protein level;
KW   Antibiotic resistance; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Plasmid.
FT   CHAIN           1..265
FT                   /note="Beta-lactamase SHV-4"
FT                   /id="PRO_0000195440"
FT   ACT_SITE        45
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   ACT_SITE        143
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         209..211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..98
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   265 AA;  28860 MW;  E575CF38B1ADE304 CRC64;
     SPQPLEQIKL SESQLSGRVG MIEMDLASGR TLTAWRADER FPMMSTFKVV LCGAVLARVD
     AGDEQLERKI HYRQQDLVDY SPVSEKHLAD GMTVGELCAA AITMSDNSAA NLLLATVGGP
     AGLTAFLRQI GDNVTRLDRW ETELNEALPG DARDTTTPAS MAATLRKLLT SQRLSARSQL
     QLLQWMVDDR VAGPLIRSVL PAGWFIADKT GASKRGARGI VALLGPNNKA ERIVVIYLRD
     TPASMAERNQ QIAGIGAALI EHWQR
//