BLAB_PROVU
ID BLAB_PROVU Reviewed; 300 AA.
AC P52664;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Beta-lactamase;
DE EC=3.5.2.6;
DE AltName: Full=Cefuroximase;
DE Flags: Precursor;
GN Name=blaB; Synonyms=cumA;
OS Proteus vulgaris.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=585;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B317;
RX PubMed=7957242; DOI=10.1111/j.1432-1033.1994.tb20036.x;
RA Datz M., Joris B., Azab E.A., Galleni M., van Beeumen J., Frere J.-M.,
RA Martin H.H.;
RT "A common system controls the induction of very different genes. The class-
RT A beta-lactamase of Proteus vulgaris and the enterobacterial class-C beta-
RT lactamase.";
RL Eur. J. Biochem. 226:149-157(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=5E78-1;
RA Okuguchi M., Komai T., Makajima N., Eguchi H., Kuboki A., Ito T.,
RA Meguro M., Nakata T., Sugimoto K.;
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes broad-spectrum beta-lactam antibiotics. Active
CC against cephalosporins such as cefuroxime and cefotaxime.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; X80128; CAA56427.1; -; Genomic_DNA.
DR EMBL; D37831; BAA07084.1; -; Genomic_DNA.
DR PIR; S51044; S51044.
DR RefSeq; WP_063851288.1; NG_047908.1.
DR PDB; 1HZO; X-ray; 1.75 A; A/B=32-300.
DR PDBsum; 1HZO; -.
DR AlphaFoldDB; P52664; -.
DR SMR; P52664; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR EvolutionaryTrace; P52664; -.
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; Hydrolase; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..300
FT /note="Beta-lactamase"
FT /id="PRO_0000017008"
FT ACT_SITE 75
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT BINDING 239..241
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VARIANT 13
FT /note="T -> A (in strain: 5E78-1)"
FT VARIANT 23
FT /note="V -> A (in strain: 5E78-1)"
FT VARIANT 30..31
FT /note="NT -> DN (in strain: 5E78-1)"
FT VARIANT 40
FT /note="S -> N (in strain: 5E78-1)"
FT VARIANT 58
FT /note="E -> K (in strain: 5E78-1)"
FT VARIANT 88
FT /note="E -> A (in strain: 5E78-1)"
FT VARIANT 119
FT /note="V -> T (in strain: 5E78-1)"
FT VARIANT 123
FT /note="S -> T (in strain: 5E78-1)"
FT VARIANT 126
FT /note="Q -> E (in strain: 5E78-1)"
FT VARIANT 224
FT /note="H -> N (in strain: 5E78-1)"
FT VARIANT 235
FT /note="I -> V (in strain: 5E78-1)"
FT VARIANT 257
FT /note="K -> E (in strain: 5E78-1)"
FT VARIANT 283
FT /note="V -> A (in strain: 5E78-1)"
FT VARIANT 286
FT /note="T -> A (in strain: 5E78-1)"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:1HZO"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:1HZO"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:1HZO"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1HZO"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:1HZO"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:1HZO"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1HZO"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1HZO"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1HZO"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1HZO"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:1HZO"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:1HZO"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:1HZO"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1HZO"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:1HZO"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1HZO"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:1HZO"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1HZO"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:1HZO"
FT STRAND 234..243
FT /evidence="ECO:0007829|PDB:1HZO"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:1HZO"
FT STRAND 247..255
FT /evidence="ECO:0007829|PDB:1HZO"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:1HZO"
FT HELIX 279..294
FT /evidence="ECO:0007829|PDB:1HZO"
SQ SEQUENCE 300 AA; 32992 MW; 2719AF2464F1CD77 CRC64;
MTMFKTTFRQ TATIAVSLIS LLVSPMLWAN TNNTIEEQLS TLEKYSQGRL GVALINTEDN
SQITYRGEER FAMASTSKVM AVAAVLKESE KQAGLLDKNI TIKKSDLVAY SPITEKHLVT
GMSLAQLSAA TLQYSDNTAM NKILDYLGGP AKVTQFARSI NDVTYRLDRK EPELNTAIHG
DPRDTTSPIA MAKSLQALTL GDALGQSQRQ QLVTWLKGNT TGDHSIKAGL PKHWIVGDKT
GSGDYGTTND IAVIWPKNHA PLILVVYFTQ QEQDAKYRKD IIVKATEIVT KEISNSPQTK
