BLA4_KLEPN
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 03-AUG-2022, entry version 79.
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; Proteobacteria; 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; -; 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; 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