AMPC_PSEAE
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 03-AUG-2022, entry version 138.
DE RecName: Full=Beta-lactamase;
DE EC=3.5.2.6;
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; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC 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 / 1C /
RC 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 / 1C /
RC 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 / 1C /
RC 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).
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: Periplasm {ECO:0000250}.
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; NZ_QZGE01000013.1.
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 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 AlphaFoldDB; P24735; -.
DR SMR; P24735; -.
DR STRING; 287.DR97_3761; -.
DR BindingDB; P24735; -.
DR ChEMBL; CHEMBL5031; -.
DR DrugCentral; P24735; -.
DR PaxDb; P24735; -.
DR PRIDE; P24735; -.
DR EnsemblBacteria; AAG07497; AAG07497; PA4110.
DR GeneID; 878149; -.
DR KEGG; pae:PA4110; -.
DR PseudoCAP; PA4110; -.
DR HOGENOM; CLU_020027_10_0_6; -.
DR InParanoid; P24735; -.
DR OMA; ANRNYPN; -.
DR PhylomeDB; P24735; -.
DR SABIO-RK; P24735; -.
DR EvolutionaryTrace; P24735; -.
DR Proteomes; UP000002438; Chromosome.
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:0033252; P:regulation of beta-lactamase activity; IDA:PseudoCAP.
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 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 342..344
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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..203
FT /evidence="ECO:0007829|PDB:4WZ4"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:4WZ4"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:4WZ4"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:4WZ4"
FT HELIX 232..234
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
