ID   BLA1_MORCA              Reviewed;         313 AA.
AC   Q59514;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Beta-lactamase BRO-1;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=bla;
OS   Moraxella catarrhalis (Branhamella catarrhalis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 53879 / E22;
RA   Beaulieu D., Piche L., Parr T.R. Jr., Roeger-Lawry K., Rosteck P.,
RA   Roy P.H.;
RT   "The Moraxella (Branhamella) catarrhalis chromosomal beta-lactamase gene is
RT   flanked by an amidase gene and a conserved gene of unknown function.";
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
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;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; U49269; AAA92126.1; -; Genomic_DNA.
DR   RefSeq; WP_003657002.1; NZ_VLEN01000006.1.
DR   AlphaFoldDB; Q59514; -.
DR   SMR; Q59514; -.
DR   BindingDB; Q59514; -.
DR   ChEMBL; CHEMBL1744491; -.
DR   GeneID; 66584960; -.
DR   eggNOG; COG2367; Bacteria.
DR   SABIO-RK; Q59514; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   PANTHER; PTHR35333; PTHR35333; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell membrane; Hydrolase; Lipoprotein; Membrane;
KW   Palmitate; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           26..313
FT                   /note="Beta-lactamase BRO-1"
FT                   /id="PRO_0000017002"
FT   ACT_SITE        90
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         255..257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   LIPID           26
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           26
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   313 AA;  35383 MW;  A673AF8FBAB02840 CRC64;
     MQRRHFLQKT LLALPIIFSG NLLTGCKTNL SDDYLPDDKI TNNPNLLQNK LKEILPIWEN
     KFNAKIGMTI IADNGELSSH RGNEYFPVNS TIKAFIASHI LLLVDKEKLD LNEKIIIKES
     DLIEYSPVCK KYFDENKPIS ISELCEATIT LSDNGSANIL LDKIGGLTAF NQFLKEIGAD
     MVLANNEPLL NRSHYGETSD TAKPIPYTKS LKALIVGNIL SNQSKEQLIT WLINDKVADN
     LLRKYLPKNW RIGDKTGTGS ESKNIIAVIW NENNKPYFIS LFITQPHDGK SLDFKNQKDE
     IMAQIGKEIY PFL