BLA1_KLEPN
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 03-AUG-2022, entry version 93.
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; Proteobacteria; 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; -; 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 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
