ID   AMPC_PSEAE              Reviewed;         397 AA.
AC   P24735;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   02-SEP-2026, entry version 152.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6 {ECO:0000269|PubMed:16251297};
DE   AltName: Full=Cephalosporinase;
DE   Flags: Precursor;
GN   Name=ampC; OrderedLocusNames=PA4110;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=2125210; DOI=10.1042/bj2720627;
RA   Lodge J.M., Minchin S.D., Piddock L.J.V., Busby S.J.W.;
RT   "Cloning, sequencing and analysis of the structural gene and regulatory
RT   region of the Pseudomonas aeruginosa chromosomal ampC beta-lactamase.";
RL   Biochem. J. 272:627-631(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [3]
RP   PROTEIN SEQUENCE OF 27-41.
RX   PubMed=8012497; DOI=10.1159/000468649;
RA   Michea-Hamzehpour M., Sanchez J.-C., Epp S.F., Paquet N., Hughes G.J.,
RA   Hochstrasser D.F., Pechere J.-C.;
RT   "Two-dimensional polyacrylamide gel electrophoresis isolation and
RT   microsequencing of Pseudomonas aeruginosa proteins.";
RL   Enzyme Protein 47:1-8(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=8405939; DOI=10.1111/j.1574-6968.1993.tb06404.x;
RA   Lodge J.M., Busby S.J.W., Piddock L.J.V.;
RT   "Investigation of the Pseudomonas aeruginosa ampR gene and its role at the
RT   chromosomal ampC beta-lactamase promoter.";
RL   FEMS Microbiol. Lett. 111:315-320(1993).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY BETA-LACTAM.
RX   PubMed=16251297; DOI=10.1128/aac.49.11.4567-4575.2005;
RA   Kong K.F., Jayawardena S.R., Indulkar S.D., Del Puerto A., Koh C.L.,
RA   Hoeiby N., Mathee K.;
RT   "Pseudomonas aeruginosa AmpR is a global transcriptional factor that
RT   regulates expression of AmpC and PoxB beta-lactamases, proteases, quorum
RT   sensing, and other virulence factors.";
RL   Antimicrob. Agents Chemother. 49:4567-4575(2005).
RN   [6]
RP   INDUCTION BY BETA-LACTAMS; RPON.
RX   PubMed=25182487; DOI=10.1128/jb.01997-14;
RA   Caille O., Zincke D., Merighi M., Balasubramanian D., Kumari H., Kong K.F.,
RA   Silva-Herzog E., Narasimhan G., Schneper L., Lory S., Mathee K.;
RT   "Structural and functional characterization of Pseudomonas aeruginosa
RT   global regulator AmpR.";
RL   J. Bacteriol. 196:3890-3902(2014).
RN   [7]
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: Class C beta-lactamase which confers resistance to
CC       penicillins and cephalosporins (By similarity). Has nitrocefin-
CC       hydrolyzing activity (PubMed:16251297). {ECO:0000250|UniProtKB:P00811,
CC       ECO:0000269|PubMed:16251297}.
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, ECO:0000269|PubMed:16251297};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P00811}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P85302}.
CC   -!- INDUCTION: Up-regulated by beta-lactam antibiotics, such as ampicillin
CC       or benzylpenicillin (PubMed:16251297, PubMed:25182487). Expression is
CC       negatively regulated by sigma factor RpoN, possibly through promoter
CC       blocking (PubMed:25182487). {ECO:0000269|PubMed:16251297,
CC       ECO:0000269|PubMed:25182487}.
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}.
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DR   EMBL; X54719; CAA38522.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG07497.1; -; Genomic_DNA.
DR   EMBL; X67095; CAA47469.1; -; Genomic_DNA.
DR   PIR; F83132; F83132.
DR   PIR; S13408; S13408.
DR   RefSeq; NP_252799.1; NC_002516.2.
DR   RefSeq; WP_003101289.1; NC_002516.2.
DR   PDB; 2WZX; X-ray; 1.40 A; A=27-397.
DR   PDB; 2WZZ; X-ray; 1.57 A; A=27-397.
DR   PDB; 3S1Y; X-ray; 1.40 A; A=27-397.
DR   PDB; 3S22; X-ray; 1.65 A; A=27-397.
DR   PDB; 4GZB; X-ray; 1.79 A; A=27-397.
DR   PDB; 4HEF; X-ray; 1.86 A; A=29-388.
DR   PDB; 4NK3; X-ray; 1.90 A; A=27-397.
DR   PDB; 4OOY; X-ray; 1.10 A; A=29-387.
DR   PDB; 4WYY; X-ray; 1.28 A; A=29-388.
DR   PDB; 4WZ4; X-ray; 1.05 A; A=29-388.
DR   PDB; 4X68; X-ray; 1.68 A; A/B=32-387.
DR   PDB; 6UQS; X-ray; 1.37 A; A=27-397.
DR   PDB; 6UQT; X-ray; 1.25 A; A=27-397.
DR   PDB; 6UQU; X-ray; 1.09 A; A=27-397.
DR   PDB; 6UR3; X-ray; 1.42 A; A=27-397.
DR   PDB; 8SDL; X-ray; 1.75 A; A=1-397.
DR   PDB; 8SDN; X-ray; 2.10 A; A=1-397.
DR   PDB; 8SDR; X-ray; 1.35 A; A=1-397.
DR   PDB; 8SDS; X-ray; 1.63 A; A=1-397.
DR   PDB; 8SDT; X-ray; 1.38 A; A=1-397.
DR   PDB; 8SDV; X-ray; 1.42 A; A=1-397.
DR   PDB; 9AZU; X-ray; 1.73 A; A=1-397.
DR   PDB; 9AZW; X-ray; 1.55 A; A=28-397.
DR   PDB; 9AZY; X-ray; 1.50 A; A=28-397.
DR   AlphaFoldDB; P24735; -.
DR   MDposit; P24735; -.
DR   MDRepo; P24735; -.
DR   SMR; P24735; -.
DR   FunCoup; P24735; 170.
DR   STRING; 208964.PA4110; -.
DR   BindingDB; P24735; -.
DR   ChEMBL; CHEMBL5031; -.
DR   DrugCentral; P24735; -.
DR   CARD; ARO:3002497; PDC-1; ARO:0001004; antibiotic inactivation.
DR   PaxDb; 208964-PA4110; -.
DR   GeneID; 878149; -.
DR   KEGG; pae:PA4110; -.
DR   PseudoCAP; PA4110; -.
DR   HOGENOM; CLU_020027_10_0_6; -.
DR   InParanoid; P24735; -.
DR   OrthoDB; 5377431at2; -.
DR   PhylomeDB; P24735; -.
DR   SABIO-RK; P24735; -.
DR   EvolutionaryTrace; P24735; -.
DR   Proteomes; UP000002438; Chromosome.
DR   AbasyAtlas; P24735; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; ISS:UniProtKB.
DR   GO; GO:0008800; F:beta-lactamase activity; EXP:UniProtKB.
DR   GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0033252; P:regulation of beta-lactamase activity; IDA:PseudoCAP.
DR   FunFam; 3.40.710.10:FF:000012; Beta-lactamase; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR058136; AmpC.
DR   InterPro; IPR050491; AmpC-like.
DR   InterPro; IPR058164; AmpC_pseudomonas.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001586; Beta-lactam_class-C_AS.
DR   NCBIfam; NF033085; bla_class_C; 1.
DR   NCBIfam; NF000422; blaPDC; 1.
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.
DR   PDBsum; 2WZX; -.
DR   PDBsum; 2WZZ; -.
DR   PDBsum; 3S1Y; -.
DR   PDBsum; 3S22; -.
DR   PDBsum; 4GZB; -.
DR   PDBsum; 4HEF; -.
DR   PDBsum; 4NK3; -.
DR   PDBsum; 4OOY; -.
DR   PDBsum; 4WYY; -.
DR   PDBsum; 4WZ4; -.
DR   PDBsum; 4X68; -.
DR   PDBsum; 6UQS; -.
DR   PDBsum; 6UQT; -.
DR   PDBsum; 6UQU; -.
DR   PDBsum; 6UR3; -.
DR   PDBsum; 8SDL; -.
DR   PDBsum; 8SDN; -.
DR   PDBsum; 8SDR; -.
DR   PDBsum; 8SDS; -.
DR   PDBsum; 8SDT; -.
DR   PDBsum; 8SDV; -.
DR   PDBsum; 9AZU; -.
DR   PDBsum; 9AZW; -.
DR   PDBsum; 9AZY; -.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; Direct protein sequencing; Hydrolase;
KW   Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:8012497"
FT   CHAIN           27..397
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000016963"
FT   ACT_SITE        90
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10102"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="a beta-lactam"
FT                   /ligand_id="ChEBI:CHEBI:35627"
FT                   /evidence="ECO:0000250|UniProtKB:P00811"
FT   BINDING         146
FT                   /ligand="a beta-lactam"
FT                   /ligand_id="ChEBI:CHEBI:35627"
FT                   /evidence="ECO:0000250|UniProtKB:P00811"
FT   BINDING         177
FT                   /ligand="a beta-lactam"
FT                   /ligand_id="ChEBI:CHEBI:35627"
FT                   /evidence="ECO:0000250|UniProtKB:P00811"
FT   BINDING         179
FT                   /ligand="a beta-lactam"
FT                   /ligand_id="ChEBI:CHEBI:35627"
FT                   /evidence="ECO:0000250|UniProtKB:P00811"
FT   BINDING         370
FT                   /ligand="a beta-lactam"
FT                   /ligand_id="ChEBI:CHEBI:35627"
FT                   /evidence="ECO:0000250|UniProtKB:P00811"
FT   CONFLICT        397
FT                   /note="R -> A (in Ref. 1; CAA38522)"
FT                   /evidence="ECO:0000305"
FT   HELIX           30..48
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   STRAND          52..60
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   STRAND          63..73
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   TURN            74..77
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           92..105
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           115..118
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           126..129
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           132..136
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           155..164
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   STRAND          173..175
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           179..192
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           197..200
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           201..205
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           206..209
FT                   /evidence="ECO:0007829|PDB:8SDS"
FT   STRAND          212..217
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           220..225
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           227..229
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           232..234
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           239..241
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           245..249
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   STRAND          252..254
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           255..266
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           268..270
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           273..280
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   STRAND          283..289
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   STRAND          292..294
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   STRAND          299..304
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           307..313
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           316..320
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   STRAND          326..333
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   STRAND          336..346
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   STRAND          349..356
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           357..359
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   STRAND          361..369
FT                   /evidence="ECO:0007829|PDB:4WZ4"
FT   HELIX           373..387
FT                   /evidence="ECO:0007829|PDB:4WZ4"
SQ   SEQUENCE   397 AA;  43401 MW;  C6341A53594BC261 CRC64;
     MRDTRFPCLC GIAASTLLFA TTPAIAGEAP ADRLKALVDA AVQPVMKAND IPGLAVAISL
     KGEPHYFSYG LASKEDGRRV TPETLFEIGS VSKTFTATLA GYALTQDKMR LDDRASQHWP
     ALQGSRFDGI SLLDLATYTA GGLPLQFPDS VQKDQAQIRD YYRQWQPTYA PGSQRLYSNP
     SIGLFGYLAA RSLGQPFERL MEQQVFPALG LEQTHLDVPE AALAQYAQGY GKDDRPLRVG
     PGPLDAEGYG VKTSAADLLR FVDANLHPER LDRPWAQALD ATHRGYYKVG DMTQGLGWEA
     YDWPISLKRL QAGNSTPMAL QPHRIARLPA PQALEGQRLL NKTGSTNGFG AYVAFVPGRD
     LGLVILANRN YPNAERVKIA YAILSGLEQQ GKVPLKR
//