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 08-MAY-2019, entry version 70. 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; Pseudomonadales; OC Moraxellaceae; 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 RT from 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X83586; CAA58569.1; -; Genomic_DNA. 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 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 {ECO:0000269|PubMed:9063463}. FT CHAIN 40 401 Beta-lactamase. FT /FTId=PRO_0000016964. FT REGION 353 355 Substrate binding. {ECO:0000250}. FT ACT_SITE 102 102 Acyl-ester intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU10102}. FT ACT_SITE 188 188 Proton acceptor. {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 //