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 24-JUL-2024, entry version 79. 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; Pseudomonadota; 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). RN [2] RP AMINO ACID NUMBERING SCHEME. RX PubMed=31712217; DOI=10.1128/aac.01841-19; RA Mack A.R., Barnes M.D., Taracila M.A., Hujer A.M., Hujer K.M., Cabot G., RA Feldgarden M., Haft D.H., Klimke W., van den Akker F., Vila A.J., RA Smania A., Haider S., Papp-Wallace K.M., Bradford P.A., Rossolini G.M., RA Docquier J.D., Frere J.M., Galleni M., Hanson N.D., Oliver A., Plesiat P., RA Poirel L., Nordmann P., Palzkill T.G., Jacoby G.A., Bush K., Bonomo R.A.; RT "A Standard Numbering Scheme for Class C beta-Lactamases."; RL Antimicrob. Agents Chemother. 64:0-0(2020). 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 -!- MISCELLANEOUS: The class C beta-lactamase family has a specific amino- CC acid numbering system known as SANC, for structural alignment-based CC numbering of class C beta-lactamases, or else the simpler name CC structural position. A multiple sequence alignment was used to derive a CC consensus sequence and then the consensus was numbered taking into CC account insertions and deletions. This allows use of identical numbers, CC e.g. for active site residues, despite differences in protein length. CC UniProt always uses natural numbering of residues, hence there appear CC to be differences in numbering between this entry and some papers. CC {ECO:0000305|PubMed:31712217}. 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 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; DD-peptidase/beta-lactamase superfamily; 1. DR InterPro; IPR050491; Bact_CellWall_Synth/Modif. DR InterPro; IPR001466; Beta-lactam-related. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR001586; Beta-lactam_class-C_AS. DR PANTHER; PTHR46825:SF8; BETA-LACTAMASE-RELATED; 1. DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1. DR Pfam; PF00144; Beta-lactamase; 1. DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 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 //