ID AMPC_CITFR Reviewed; 381 AA. AC P05193; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 03-MAY-2023, entry version 111. DE RecName: Full=Beta-lactamase; DE EC=3.5.2.6; DE AltName: Full=Cephalosporinase; DE Flags: Precursor; GN Name=ampC; Synonyms=blaC; OS Citrobacter freundii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex. OX NCBI_TaxID=546; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=OS60; RX PubMed=3486121; DOI=10.1111/j.1432-1033.1986.tb09601.x; RA Lindberg F., Normark S.; RT "Sequence of the Citrobacter freundii OS60 chromosomal ampC beta-lactamase RT gene."; RL Eur. J. Biochem. 156:441-445(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=GN346; RX PubMed=1969344; DOI=10.1111/j.1432-1033.1990.tb15365.x; RA Tsukamoto K., Tachibana K., Yamazaki N., Ishii Y., Ujiie K., Nishida N., RA Sawai T.; RT "Role of lysine-67 in the active site of class C beta-lactamase from RT Citrobacter freundii GN346."; RL Eur. J. Biochem. 188:15-22(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-381, AND INHIBITION BY SULBACTAM. RC STRAIN=GN346; RX PubMed=3263684; DOI=10.1093/clinids/10.4.721; RA Sawai T., Yamaguchi A., Tsukamoto K.; RT "Amino acid sequence, active-site residue, and effect of suicide inhibitors RT on cephalosporinase of Citrobacter freundii GN346."; RL Rev. Infect. Dis. 10:721-725(1988). RN [4] RP PROTEIN SEQUENCE OF 66-87. RX PubMed=3496243; DOI=10.1016/0014-5793(87)81031-1; RA Yamaguchi A., Adachi H., Sawai T.; RT "Identification of the active site of Citrobacter freundii beta-lactamase RT using dansyl-penicillin."; RL FEBS Lett. 218:126-130(1987). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=2300174; DOI=10.1038/343284a0; RA Oefner C., D'Arcy A.A., Daly J.J., Gubernator K., Charnas R.L., Heinze I., RA Hubschwerlen C., Winkler F.K.; RT "Refined crystal structure of beta-lactamase from Citrobacter freundii RT indicates a mechanism for beta-lactam hydrolysis."; RL Nature 343:284-288(1990). 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 -!- ACTIVITY REGULATION: Sulbactam is an effective progressive inhibitor CC but a poor competitive inhibitor. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. 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; X03866; CAA27494.1; -; Genomic_DNA. DR EMBL; X51632; CAA35959.1; -; Genomic_DNA. DR PIR; S08296; S08296. DR PDB; 1RGY; X-ray; 1.52 A; A=22-381. DR PDBsum; 1RGY; -. DR AlphaFoldDB; P05193; -. DR SMR; P05193; -. DR STRING; 1333848.CFNIH1_08415; -. DR BindingDB; P05193; -. DR ChEMBL; CHEMBL1255130; -. DR DrugBank; DB00355; Aztreonam. DR DrugCentral; P05193; -. DR MEROPS; S12.006; -. DR SABIO-RK; P05193; -. DR EvolutionaryTrace; P05193; -. 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; IMP:CACAO. DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1. 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 3D-structure; Antibiotic resistance; Direct protein sequencing; Hydrolase; KW Periplasm; Signal. FT SIGNAL 1..20 FT CHAIN 21..381 FT /note="Beta-lactamase" FT /id="PRO_0000016957" FT ACT_SITE 84 FT /note="Acyl-ester intermediate" FT ACT_SITE 170 FT /note="Proton acceptor" FT BINDING 335..337 FT /ligand="substrate" FT /evidence="ECO:0000250" FT VARIANT 97 FT /note="R -> A (in strain: GN346)" FT VARIANT 143 FT /note="G -> D (in strain: GN346)" FT VARIANT 145 FT /note="V -> I (in strain: GN346)" FT VARIANT 150 FT /note="E -> A (in strain: GN346)" FT VARIANT 185 FT /note="S -> P (in strain: GN346)" FT VARIANT 224 FT /note="L -> R (in strain: GN346)" FT VARIANT 243 FT /note="V -> L (in strain: GN346)" FT VARIANT 325 FT /note="A -> V (in strain: GN346)" FT VARIANT 368 FT /note="A -> V (in strain: GN346)" FT CONFLICT 98 FT /note="I -> T (in Ref. 3)" FT /evidence="ECO:0000305" FT HELIX 25..43 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 46..54 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 57..67 FT /evidence="ECO:0007829|PDB:1RGY" FT TURN 68..71 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 86..99 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 109..112 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 126..130 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 148..157 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 172..182 FT /evidence="ECO:0007829|PDB:1RGY" FT TURN 183..187 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 190..197 FT /evidence="ECO:0007829|PDB:1RGY" FT TURN 198..203 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 207..210 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 213..218 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 237..240 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 247..258 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 260..262 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 266..275 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 277..282 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 285..287 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 292..297 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 300..306 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 309..312 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 319..325 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 329..338 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 343..349 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:1RGY" FT STRAND 354..362 FT /evidence="ECO:0007829|PDB:1RGY" FT HELIX 366..378 FT /evidence="ECO:0007829|PDB:1RGY" SQ SEQUENCE 381 AA; 41975 MW; 3F955F6933F0D76B CRC64; MMKKSICCAL LLTASFSTFA AAKTEQQIAD IVNRTITPLM QEQAIPGMAV AIIYEGKPYY FTWGKADIAN NHPVTQQTLF ELGSVSKTFN GVLGGDRIAR GEIKLSDPVT KYWPELTGKQ WRGISLLHLA TYTAGGLPLQ IPGDVTDKAE LLRFYQNWQP QWTPGAKRLY ANSSIGLFGA LAVKSSGMSY EEAMTRRVLQ PLKLAHTWIT VPQSEQKNYA WGYLEGKPVH VSPGQLDAEA YGVKSSVIDM ARWVQANMDA SHVQEKTLQQ GIELAQSRYW RIGDMYQGLG WEMLNWPLKA DSIINGSDSK VALAALPAVE VNPPAPAVKA SWVHKTGSTG GFGSYVAFVP EKNLGIVMLA NKSYPNPARV EAAWRILEKL Q //