ID   BLAT_SALTI              Reviewed;         286 AA.
AC   P62594; P00810; Q47313;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Beta-lactamase TEM;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=bla; OrderedLocusNames=HCM1.216;
OS   Salmonella typhi.
OG   Plasmid pHCM1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
CC   -!- FUNCTION: TEM-type are the most prevalent beta-lactamases in
CC       enterobacteria; they hydrolyze the beta-lactam bond in susceptible
CC       beta-lactam antibiotics, thus conferring resistance to penicillins and
CC       cephalosporins. {ECO:0000250}.
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; AL513383; CAD09800.1; -; Genomic_DNA.
DR   RefSeq; NP_569411.1; NC_003384.1.
DR   RefSeq; WP_000027057.1; NZ_WSUR01000080.1.
DR   AlphaFoldDB; P62594; -.
DR   BMRB; P62594; -.
DR   SMR; P62594; -.
DR   DrugBank; DB02614; 1(R)-1-Acetamido-2-(3-Carboxyphenyl)Ethyl Boronic Acid.
DR   DrugBank; DB04430; 3-(4-Phenylamino-Phenylamino)-2-(1h-Tetrazol-5-Yl)-Acrylonitrile.
DR   DrugBank; DB02841; [(2-Ethoxy-1-Naphthoyl)Amino]Methylboronic Acid.
DR   DrugBank; DB02642; [[N-(Benzyloxycarbonyl)Amino]Methyl]Phosphate.
DR   DrugBank; DB03640; Beta-Hydroxyaspartic Acid.
DR   DrugBank; DB04037; N,N-Bis(4-Chlorobenzyl)-1h-1,2,3,4-Tetraazol-5-Amine.
DR   DrugBank; DB01606; Tazobactam.
DR   DrugCentral; P62594; -.
DR   GeneID; 84568456; -.
DR   KEGG; sty:HCM1.216; -.
DR   PATRIC; fig|220341.7.peg.5236; -.
DR   HOGENOM; CLU_031960_6_0_6; -.
DR   OMA; EWMKGNA; -.
DR   Proteomes; UP000000541; Plasmid pHCM1.
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   3: Inferred from homology;
KW   Antibiotic resistance; Disulfide bond; Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..286
FT                   /note="Beta-lactamase TEM"
FT                   /id="PRO_0000016979"
FT   ACT_SITE        68
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         232..234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..121
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  31515 MW;  BB678943BB18934B CRC64;
     MSIQHFRVAL IPFFAAFCLP VFAHPETLVK VKDAEDQLGA RVGYIELDLN SGKILESFRP
     EERFPMMSTF KVLLCGAVLS RVDAGQEQLG RRIHYSQNDL VEYSPVTEKH LTDGMTVREL
     CSAAITMSDN TAANLLLTTI GGPKELTAFL HNMGDHVTRL DRWEPELNEA IPNDERDTTM
     PAAMATTLRK LLTGELLTLA SRQQLIDWME ADKVAGPLLR SALPAGWFIA DKSGAGERGS
     RGIIAALGPD GKPSRIVVIY TTGSQATMDE RNRQIAEIGA SLIKHW
//