ID   AMPC_PSYIM              Reviewed;         401 AA.
AC   O05465;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Cephalosporinase;
DE   Flags: Precursor;
GN   Name=ampC; Synonyms=bla;
OS   Psychrobacter immobilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=498;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-47, AND
RP   CHARACTERIZATION.
RC   STRAIN=A5;
RX   PubMed=9063463; DOI=10.1111/j.1432-1033.1997.00186.x;
RA   Feller G., Zekhnini Z., Lamotte-Brasseur J., Gerday C.;
RT   "Enzymes from cold-adapted microorganisms. The class C beta-lactamase from
RT   the antarctic psychrophile Psychrobacter immobilis A5.";
RL   Eur. J. Biochem. 244:186-191(1997).
CC   -!- FUNCTION: This protein is a serine beta-lactamase with a substrate
CC       specificity for cephalosporins.
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:PRU10102};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; X83586; CAA58569.1; -; Genomic_DNA.
DR   AlphaFoldDB; O05465; -.
DR   SMR; O05465; -.
DR   MEROPS; S12.006; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017001; P: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; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001586; Beta-lactam_class-C_AS.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS00336; BETA_LACTAMASE_C; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Direct protein sequencing; Hydrolase; Secreted;
KW   Signal.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000269|PubMed:9063463"
FT   CHAIN           40..401
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000016964"
FT   ACT_SITE        102
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10102"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         353..355
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   401 AA;  44451 MW;  93F0DB278EA8E043 CRC64;
     MKLFTSTLTA KKSSTHKPLI SLALSVLIST LLISETAQAA DANDRLEQEV DKQAKQLMAQ
     YQIPGMAFGI IVDGKSHFYN YGLADKQRNQ PVSEDTIFEL GSVSKTFAAT LASYSELNGT
     LSLDDTADKY IPYLKNSAIG NTKLISLVTY SAGGYHYRCL KTLENNKELL QYYKSWHPDF
     PVNSKRLYSN ASIGLFGYIS ALSMHSDYTK LIENTVLPSL KMTNTFVDVP ANKMEDYAFG
     YNAAGEPIRV NPGMLDAEAY GIKSTSADMT RFMAANMGLV TVDSQMQQAL DNNRKGYYRT
     KSFTQGLAWE MYPLPTTLQQ LVEGNSTETI LQPQPIQLNE PPTPVLNDVW VNKTGATNGF
     GAYIAYMPAK KTGMFILANK NYPNTERVKA AYTILDSVMN N