ID   BLA1_KLEPN              Reviewed;         286 AA.
AC   P0AD64; O07941; P14557; P23982;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Beta-lactamase SHV-1;
DE            EC=3.5.2.6;
DE   AltName: Full=PIT-2;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=shv1;
OS   Klebsiella pneumoniae.
OG   Plasmid R974.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=R974;
RX   PubMed=2221867; DOI=10.1128/aac.34.8.1577;
RA   Mercier J., Levesque R.C.;
RT   "Cloning of SHV-2, OHIO-1, and OXA-6 beta-lactamases and cloning and
RT   sequencing of SHV-1 beta-lactamase.";
RL   Antimicrob. Agents Chemother. 34:1577-1583(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KPAA-1, KPZU-13, and KPZU-8;
RX   PubMed=9145849; DOI=10.1128/aac.41.5.943;
RA   Nuesch-Inderbinen M., Kayser F.H., Hachler H.;
RT   "Survey and molecular genetics of SHV beta-lactamases in Enterobacteriaceae
RT   in Switzerland: two novel enzymes, SHV-11 and SHV-12.";
RL   Antimicrob. Agents Chemother. 41:943-949(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=15571;
RX   PubMed=10639363; DOI=10.1128/aac.44.2.362-367.2000;
RA   Rice L.B., Carias L.L., Hujer A.M., Bonafede M., Hutton R., Hoyen C.,
RA   Bonomo R.A.;
RT   "High-level expression of chromosomally encoded SHV-1 beta-lactamase and an
RT   outer membrane protein change confer resistance to ceftazidime and
RT   piperacillin-tazobactam in a clinical isolate of Klebsiella pneumoniae.";
RL   Antimicrob. Agents Chemother. 44:362-367(2000).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS).
RC   STRAIN=15571;
RX   PubMed=10231522; DOI=10.1021/bi990136d;
RA   Kuzin A.P., Nukaga M., Nukaga Y., Hujer A.M., Bonomo R.A., Knox J.R.;
RT   "Structure of the SHV-1 beta-lactamase.";
RL   Biochemistry 38:5720-5727(1999).
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   EMBL; M59181; AAA26087.1; -; Genomic_DNA.
DR   EMBL; X98098; CAA66726.1; -; Genomic_DNA.
DR   EMBL; X98099; CAA66727.1; -; Genomic_DNA.
DR   EMBL; X98100; CAA66728.1; -; Genomic_DNA.
DR   EMBL; AF124984; AAD18054.1; -; Genomic_DNA.
DR   PIR; A44996; A44996.
DR   RefSeq; WP_001620095.1; NZ_WXZO01000019.1.
DR   PDB; 1ONG; X-ray; 1.10 A; A=22-286.
DR   PDB; 1Q2P; X-ray; 2.00 A; A=22-286.
DR   PDB; 1RCJ; X-ray; 1.63 A; A=22-286.
DR   PDB; 1SHV; X-ray; 1.98 A; A=22-286.
DR   PDB; 1TDG; X-ray; 1.80 A; A=22-286.
DR   PDB; 1TDL; X-ray; 1.80 A; A=22-286.
DR   PDB; 1VM1; X-ray; 2.02 A; A=22-286.
DR   PDB; 2A3U; X-ray; 1.34 A; A=22-286.
DR   PDB; 2A49; X-ray; 1.43 A; A=22-286.
DR   PDB; 2G2U; X-ray; 1.60 A; A=22-284.
DR   PDB; 2G2W; X-ray; 1.80 A; A=22-284.
DR   PDB; 2H0T; X-ray; 1.60 A; A=22-286.
DR   PDB; 2H0Y; X-ray; 1.70 A; A=22-284.
DR   PDB; 2H10; X-ray; 1.75 A; A=22-284.
DR   PDB; 2H5S; X-ray; 1.28 A; A=22-286.
DR   PDB; 2ZD8; X-ray; 1.05 A; A=22-286.
DR   PDB; 3C4O; X-ray; 1.70 A; A=22-286.
DR   PDB; 3C4P; X-ray; 1.75 A; A=22-286.
DR   PDB; 3D4F; X-ray; 1.55 A; A=1-286.
DR   PDB; 3MKE; X-ray; 1.75 A; A=22-286.
DR   PDB; 3MKF; X-ray; 1.33 A; A=22-286.
DR   PDB; 3MXR; X-ray; 1.30 A; A=22-286.
DR   PDB; 3MXS; X-ray; 1.24 A; A=22-286.
DR   PDB; 3N4I; X-ray; 1.56 A; A=22-286.
DR   PDB; 3OPH; X-ray; 1.34 A; A=1-286.
DR   PDB; 3OPL; X-ray; 1.80 A; A=1-286.
DR   PDB; 3OPP; X-ray; 1.80 A; A=1-286.
DR   PDB; 3OPR; X-ray; 1.65 A; A=1-286.
DR   PDB; 3V50; X-ray; 1.45 A; A=22-286.
DR   PDB; 3V5M; X-ray; 1.30 A; A=22-286.
DR   PDB; 4FCF; X-ray; 1.09 A; A=22-286.
DR   PDB; 4FD8; X-ray; 1.52 A; A=22-286.
DR   PDB; 4FH2; X-ray; 1.44 A; A=22-286.
DR   PDB; 4FH4; X-ray; 1.09 A; A=22-286.
DR   PDB; 4GD6; X-ray; 1.53 A; A=1-286.
DR   PDB; 4GD8; X-ray; 1.60 A; A=1-286.
DR   PDB; 4GDB; X-ray; 1.84 A; A=1-286.
DR   PDB; 4JPM; X-ray; 1.14 A; A=1-286.
DR   PDB; 4MBF; X-ray; 1.54 A; A=22-286.
DR   PDB; 4MBH; X-ray; 1.22 A; A=22-286.
DR   PDB; 4MBK; X-ray; 1.46 A; A=22-286.
DR   PDB; 4R3B; X-ray; 1.37 A; A=22-286.
DR   PDB; 4ZAM; X-ray; 1.42 A; A=22-286.
DR   PDB; 5EE8; X-ray; 1.54 A; A=22-286.
DR   PDBsum; 1ONG; -.
DR   PDBsum; 1Q2P; -.
DR   PDBsum; 1RCJ; -.
DR   PDBsum; 1SHV; -.
DR   PDBsum; 1TDG; -.
DR   PDBsum; 1TDL; -.
DR   PDBsum; 1VM1; -.
DR   PDBsum; 2A3U; -.
DR   PDBsum; 2A49; -.
DR   PDBsum; 2G2U; -.
DR   PDBsum; 2G2W; -.
DR   PDBsum; 2H0T; -.
DR   PDBsum; 2H0Y; -.
DR   PDBsum; 2H10; -.
DR   PDBsum; 2H5S; -.
DR   PDBsum; 2ZD8; -.
DR   PDBsum; 3C4O; -.
DR   PDBsum; 3C4P; -.
DR   PDBsum; 3D4F; -.
DR   PDBsum; 3MKE; -.
DR   PDBsum; 3MKF; -.
DR   PDBsum; 3MXR; -.
DR   PDBsum; 3MXS; -.
DR   PDBsum; 3N4I; -.
DR   PDBsum; 3OPH; -.
DR   PDBsum; 3OPL; -.
DR   PDBsum; 3OPP; -.
DR   PDBsum; 3OPR; -.
DR   PDBsum; 3V50; -.
DR   PDBsum; 3V5M; -.
DR   PDBsum; 4FCF; -.
DR   PDBsum; 4FD8; -.
DR   PDBsum; 4FH2; -.
DR   PDBsum; 4FH4; -.
DR   PDBsum; 4GD6; -.
DR   PDBsum; 4GD8; -.
DR   PDBsum; 4GDB; -.
DR   PDBsum; 4JPM; -.
DR   PDBsum; 4MBF; -.
DR   PDBsum; 4MBH; -.
DR   PDBsum; 4MBK; -.
DR   PDBsum; 4R3B; -.
DR   PDBsum; 4ZAM; -.
DR   PDBsum; 5EE8; -.
DR   AlphaFoldDB; P0AD64; -.
DR   SMR; P0AD64; -.
DR   BindingDB; P0AD64; -.
DR   ChEMBL; CHEMBL5094; -.
DR   DrugBank; DB08116; (3R)-4-{[(3,4-dihydroxyphenyl)acetyl]oxy}-N-(2-formylindolizin-3-yl)-3-sulfino-D-valine.
DR   DrugBank; DB03970; (7R)-7-(6,7-Dihydro-5H-cyclopenta[d]imidazo[2,1-b][1,3]thiazol-2-yl)-2,7-dihydro-1,4-thiazepine-3,6-dicarboxylic acid.
DR   DrugBank; DB09060; Avibactam.
DR   DrugBank; DB12107; Vaborbactam.
DR   DrugCentral; P0AD64; -.
DR   BRENDA; 3.5.2.6; 2814.
DR   SABIO-RK; P0AD64; -.
DR   EvolutionaryTrace; P0AD64; -.
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-1"
FT                   /id="PRO_0000043362"
FT   ACT_SITE        66
FT                   /note="Acyl-ester intermediate"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT   BINDING         230..232
FT                   /ligand="substrate"
FT   DISULFID        73..119
FT   CONFLICT        112
FT                   /note="G -> A (in Ref. 1; AAA26087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188..189
FT                   /note="KL -> NVG (in Ref. 1; AAA26087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278
FT                   /note="A -> K (in Ref. 1; AAA26087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        281
FT                   /note="I -> Y (in Ref. 1; AAA26087)"
FT                   /evidence="ECO:0000305"
FT   HELIX           25..36
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   STRAND          38..46
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   STRAND          52..57
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   HELIX           68..81
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   HELIX           105..108
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   TURN            109..111
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   HELIX           115..125
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   HELIX           128..137
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   HELIX           140..150
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   HELIX           164..166
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   HELIX           179..191
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   STRAND          192..195
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   HELIX           197..208
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   STRAND          211..213
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   HELIX           214..220
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   STRAND          226..233
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   HELIX           235..237
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   STRAND          239..247
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   STRAND          253..261
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   HELIX           266..282
FT                   /evidence="ECO:0007829|PDB:2ZD8"
FT   TURN            283..285
FT                   /evidence="ECO:0007829|PDB:3N4I"
SQ   SEQUENCE   286 AA;  31224 MW;  C78F42667E698E6C CRC64;
     MRYIRLCIIS LLATLPLAVH ASPQPLEQIK LSESQLSGRV GMIEMDLASG RTLTAWRADE
     RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD YSPVSEKHLA DGMTVGELCA
     AAITMSDNSA ANLLLATVGG PAGLTAFLRQ IGDNVTRLDR WETELNEALP GDARDTTTPA
     SMAATLRKLL TSQRLSARSQ RQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGAGERGARG
     IVALLGPNNK AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR
//