AMPC_PSEFL
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-AUG-2022, entry version 41.
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; Proteobacteria; 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; -; 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.
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
