ID   AMPC_PSEFL              Reviewed;         358 AA.
AC   P85302;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-MAY-2023, entry version 44.
DE   RecName: Full=Beta-lactamase {ECO:0000250|UniProtKB:P05364, ECO:0000303|PubMed:18312599, ECO:0000303|Ref.2};
DE            EC=3.5.2.6;
DE   AltName: Full=Cephalosporinase {ECO:0000250|UniProtKB:P05364, ECO:0000303|PubMed:18312599, ECO:0000303|Ref.2};
GN   Name=ampC {ECO:0000250|UniProtKB:P05364};
OS   Pseudomonas fluorescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND MASS SPECTROMETRY.
RC   STRAIN=TAE 4 {ECO:0000269|PubMed:18312599};
RX   PubMed=18312599; DOI=10.1111/j.1742-4658.2008.06324.x;
RA   Michaux C., Massant J., Kerff F., Frere J.-M., Docquier J.-D.,
RA   Vandenberghe I., Samyn B., Pierrard A., Feller G., Charlier P.,
RA   Van Beeumen J., Wouters J.;
RT   "Crystal structure of a cold-adapted class C beta-lactamase.";
RL   FEBS J. 275:1687-1697(2008).
RN   [2] {ECO:0000305}
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR
RP   LOCATION.
RX   DOI=10.1111/j.1574-6968.1998.tb12962.x;
RA   Pierrard A., Ledent P., Docquier J.-D., Feller G., Gerday C., Frere J.-M.;
RT   "Inducible class C beta-lactamases produced by psychrophilic bacteria.";
RL   FEMS Microbiol. Lett. 161:311-315(1998).
CC   -!- FUNCTION: This protein is a serine beta-lactamase with a substrate
CC       specificity for cephalosporins. {ECO:0000305}.
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|Ref.2};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=120 uM for nitrocefin {ECO:0000269|PubMed:18312599,
CC         ECO:0000269|Ref.2};
CC         KM=116 uM for nitrocefin (at 30 degrees Celsius in 50 mM sodium
CC         phosphate, pH 7.0) {ECO:0000269|PubMed:18312599, ECO:0000269|Ref.2};
CC         KM=50 uM for cephalexin (at 30 degrees Celsius in 50 mM sodium
CC         phosphate, pH 7.0) {ECO:0000269|PubMed:18312599, ECO:0000269|Ref.2};
CC         KM=2.3 uM for benzylpenicillin (at 30 degrees Celsius in 50 mM sodium
CC         phosphate, pH 7.0) {ECO:0000269|PubMed:18312599, ECO:0000269|Ref.2};
CC         KM=5.1 uM for ampicillin (at 30 degrees Celsius in 50 mM sodium
CC         phosphate, pH 7.0) {ECO:0000269|PubMed:18312599, ECO:0000269|Ref.2};
CC         KM=3.7 uM for carbenicillin (at 30 degrees Celsius in 50 mM sodium
CC         phosphate, pH 7.0) {ECO:0000269|PubMed:18312599, ECO:0000269|Ref.2};
CC         KM=0.118 uM for oxacillin (at 30 degrees Celsius in 50 mM sodium
CC         phosphate, pH 7.0) {ECO:0000269|PubMed:18312599, ECO:0000269|Ref.2};
CC         KM=0.016 uM for cloxacillin (at 30 degrees Celsius in 50 mM sodium
CC         phosphate, pH 7.0) {ECO:0000269|PubMed:18312599, ECO:0000269|Ref.2};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|Ref.2}.
CC   -!- MASS SPECTROMETRY: Mass=38723.1; Mass_error=4.9; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18312599};
CC   -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC       {ECO:0000255}.
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DR   PDB; 2QZ6; X-ray; 2.26 A; A=1-358.
DR   PDBsum; 2QZ6; -.
DR   AlphaFoldDB; P85302; -.
DR   SMR; P85302; -.
DR   BRENDA; 3.5.2.6; 5121.
DR   EvolutionaryTrace; P85302; -.
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; 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.
FT   CHAIN           1..358
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000308487"
FT   ACT_SITE        60
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P05364,
FT                   ECO:0000255|PROSITE-ProRule:PRU10102"
FT   ACT_SITE        146
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P05364"
FT   BINDING         311..313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P05364"
FT   HELIX           4..18
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   STRAND          22..30
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   STRAND          33..42
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           62..75
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           85..88
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           102..106
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           125..133
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   TURN            140..142
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           148..160
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   TURN            161..163
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           166..172
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   TURN            173..175
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           176..178
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   STRAND          181..186
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           189..194
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           214..217
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           224..235
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           237..239
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           242..251
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   STRAND          253..258
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   STRAND          261..263
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   STRAND          268..273
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           276..282
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           286..289
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   STRAND          295..301
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   STRAND          305..314
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   STRAND          319..325
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   TURN            326..329
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   STRAND          330..338
FT                   /evidence="ECO:0007829|PDB:2QZ6"
FT   HELIX           342..355
FT                   /evidence="ECO:0007829|PDB:2QZ6"
SQ   SEQUENCE   358 AA;  38728 MW;  C2C35CB71DF9E501 CRC64;
     ATDIRQVVDS TVEPLMQQQD IAGLSVAVIQ NGKAQYFNYG VANKDSKQPI TENTLFEIGS
     VSKTFTATLA GYALANGKLK LSDPASQYLP ALRGDKFDHI SLLNLGTYTA GGLPLQFPEE
     SDNTGKMISY YQHWKPAFAP GTQRLYSNPS IGLFGHLAAQ SLGQPFEKLM EQTVLPKLGL
     KHTFISVPET QMSLYAQGYD KAGKPVRVSP GALDAEAYGI KTSTSDLIHY VEVNMHPAKL
     EKPLQQAIAA THTGYYTVDG MTQGLGWEMY PYPIKVDALV EGNSTQMAME PHKVNWLTPP
     QAAPLDTLVN KTGSTGGFGA YVAYVPSKGL GVVILANKNY PNAERVKAAH AILSAMDQ
//