ID   BLA3_KLEPN              Reviewed;         286 AA.
AC   P30896;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Beta-lactamase SHV-3;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=shv3;
OS   Klebsiella pneumoniae.
OG   Plasmid pUD18.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=86-4; PLASMID=pUD18;
RX   PubMed=2694951; DOI=10.1128/aac.33.12.2096;
RA   Nicolas M.H., Jarlier V., Honore N., Philippon A., Cole S.T.;
RT   "Molecular characterization of the gene encoding SHV-3 beta-lactamase
RT   responsible for transferable cefotaxime resistance in clinical isolates of
RT   Klebsiella pneumoniae.";
RL   Antimicrob. Agents Chemother. 33:2096-2100(1989).
CC   -!- FUNCTION: This enzyme hydrolyzes cefotaxime, ceftazidime and other
CC       broad spectrum cephalosporins.
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; A37200; A37200.
DR   RefSeq; WP_063864673.1; NG_050068.1.
DR   PDB; 1N9B; X-ray; 0.90 A; A=22-286.
DR   PDBsum; 1N9B; -.
DR   AlphaFoldDB; P30896; -.
DR   SMR; P30896; -.
DR   EvolutionaryTrace; P30896; -.
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   3D-structure; Antibiotic resistance; Disulfide bond; Hydrolase; Plasmid;
KW   Signal.
FT   SIGNAL          1..21
FT   CHAIN           22..286
FT                   /note="Beta-lactamase SHV-3"
FT                   /id="PRO_0000016982"
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"
FT   HELIX           25..36
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   STRAND          38..46
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   STRAND          52..57
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   HELIX           68..81
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   HELIX           105..108
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   TURN            109..111
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   HELIX           115..125
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   HELIX           128..137
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   HELIX           140..150
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   HELIX           164..166
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   HELIX           179..191
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   STRAND          192..195
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   HELIX           197..208
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   STRAND          211..213
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   HELIX           214..218
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   STRAND          226..234
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   TURN            235..237
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   STRAND          238..247
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   STRAND          253..261
FT                   /evidence="ECO:0007829|PDB:1N9B"
FT   HELIX           266..282
FT                   /evidence="ECO:0007829|PDB:1N9B"
SQ   SEQUENCE   286 AA;  31211 MW;  82715D986508F50D CRC64;
     MRYIRLCIIS LLATLPLAVH ASPQPLEQIK LSESQLSGRV GMIEMDLASG RTLTAWRADE
     RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD YSPVSEKHLA DGMTVGELCA
     AAITMSDNSA ANLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARDTTTPA
     SMAATLRKLL TSQRLSARSQ LQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGASERGARG
     IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR
//