AMPC_ENTCL
ID AMPC_ENTCL Reviewed; 381 AA.
AC P05364;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Beta-lactamase;
DE EC=3.5.2.6;
DE AltName: Full=Cephalosporinase;
DE Flags: Precursor;
GN Name=ampC;
OS Enterobacter cloacae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=550;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MHN1, P99, and Q908R;
RX PubMed=3260487; DOI=10.1042/bj2500753;
RA Galleni M., Lindberg F., Normark S., Cole S., Honore N., Joris B.,
RA Frere J.-M.;
RT "Sequence and comparative analysis of three Enterobacter cloacae ampC beta-
RT lactamase genes and their products.";
RL Biochem. J. 250:753-760(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC STRAIN=P99;
RX PubMed=8248237; DOI=10.1073/pnas.90.23.11257;
RA Lobkovsky E., Moews P.C., Liu H., Zhao H., Frere J.-M., Knox J.R.;
RT "Evolution of an enzyme activity: crystallographic structure at 2-A
RT resolution of cephalosporinase from the ampC gene of Enterobacter cloacae
RT P99 and comparison with a class A penicillinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11257-11261(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RC STRAIN=P99;
RX PubMed=8204611; DOI=10.1021/bi00188a004;
RA Lobkovsky E., Billings E.M., Moews P.C., Rahil J., Pratt R.F., Knox J.R.;
RT "Crystallographic structure of a phosphonate derivative of the Enterobacter
RT cloacae P99 cephalosporinase: mechanistic interpretation of a beta-
RT lactamase transition-state analog.";
RL Biochemistry 33:6762-6772(1994).
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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The sequence shown is that of strain P99.
CC -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; X07274; CAA30257.1; -; Genomic_DNA.
DR EMBL; X08082; CAA30879.1; -; Genomic_DNA.
DR EMBL; X08081; CAA30878.1; -; Genomic_DNA.
DR PIR; S00404; PNKBP.
DR PIR; S00405; PNKBQ.
DR PIR; S00406; PNKBM.
DR RefSeq; WP_049134845.1; NZ_BGKQ01000008.1.
DR PDB; 1BLS; X-ray; 2.30 A; A/B=21-381.
DR PDB; 1GCE; X-ray; 1.80 A; A=21-381.
DR PDB; 1RGZ; X-ray; 1.37 A; A=22-381.
DR PDB; 1XX2; X-ray; 1.88 A; A/B=21-381.
DR PDB; 1Y54; X-ray; 2.10 A; A=21-381.
DR PDB; 2Q9M; X-ray; 2.05 A; A=22-380.
DR PDB; 2Q9N; X-ray; 2.20 A; A=22-380.
DR PDB; 3S4X; X-ray; 1.95 A; A=21-381.
DR PDB; 4XUX; X-ray; 1.75 A; A=21-381.
DR PDB; 5HAI; X-ray; 2.74 A; A=21-381.
DR PDB; 5XHR; X-ray; 1.80 A; A=21-381.
DR PDBsum; 1BLS; -.
DR PDBsum; 1GCE; -.
DR PDBsum; 1RGZ; -.
DR PDBsum; 1XX2; -.
DR PDBsum; 1Y54; -.
DR PDBsum; 2Q9M; -.
DR PDBsum; 2Q9N; -.
DR PDBsum; 3S4X; -.
DR PDBsum; 4XUX; -.
DR PDBsum; 5HAI; -.
DR PDBsum; 5XHR; -.
DR AlphaFoldDB; P05364; -.
DR SMR; P05364; -.
DR BindingDB; P05364; -.
DR ChEMBL; CHEMBL2725; -.
DR DrugBank; DB08110; (1R,4S,7AS)-1-(1-FORMYLPROP-1-EN-1-YL)-4-METHOXY-2,4,5,6,7,7A-HEXAHYDRO-1H-ISOINDOLE-3-CARBOXYLIC ACID.
DR DrugBank; DB08109; (1S,4R,7AR)-4-BUTOXY-1-[(1R)-1-FORMYLPROPYL]-2,4,5,6,7,7A-HEXAHYDRO-1H-ISOINDOLE-3-CARBOXYLIC ACID.
DR DrugBank; DB03970; (7R)-7-(6,7-Dihydro-5H-cyclopenta[d]imidazo[2,1-b][1,3]thiazol-2-yl)-2,7-dihydro-1,4-thiazepine-3,6-dicarboxylic acid.
DR DrugBank; DB04123; (P-Iodophenylacetylamino)Methylphosphinic Acid.
DR DrugBank; DB02876; 3-(4-carbamoyl-1-carboxy-2-methylsulfonyl-buta-1,3-dienylamino)-indolizine-2-carboxylic acid.
DR DrugBank; DB02122; 4-iodo-acetamido phenylboronic acid.
DR DrugBank; DB02816; 7-(1-Methyl-1,2,3-Triazol-4-Yl)-6-Formyl-2,7-Dihydro-[1,4]Thiazepine-3-Carboxylic Acid, Brl42715, C6-(N1-Methyl-1,2,3-Triazolylmethylene)Penem.
DR DrugBank; DB09060; Avibactam.
DR DrugBank; DB12377; Relebactam.
DR DrugBank; DB12107; Vaborbactam.
DR DrugCentral; P05364; -.
DR MEROPS; S12.006; -.
DR BRENDA; 3.5.2.6; 155.
DR SABIO-RK; P05364; -.
DR EvolutionaryTrace; P05364; -.
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; Hydrolase; Periplasm; Signal.
FT SIGNAL 1..20
FT CHAIN 21..381
FT /note="Beta-lactamase"
FT /id="PRO_0000016959"
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 VARIANT 3
FT /note="R -> I (in strain: MHN1)"
FT VARIANT 14
FT /note="I -> L (in strain: MHN1)"
FT VARIANT 21
FT /note="T -> A (in strain: MHN1)"
FT VARIANT 36
FT /note="I -> V (in strain: MHN1 and Q980R)"
FT VARIANT 58
FT /note="P -> S (in strain: MHN1)"
FT VARIANT 108
FT /note="A -> P (in strain: MHN1 and Q980R)"
FT VARIANT 152
FT /note="L -> V (in strain: Q980R)"
FT VARIANT 262
FT /note="N -> K (in strain: MHN1)"
FT VARIANT 319
FT /note="A -> V (in strain: Q980R)"
FT VARIANT 362
FT /note="T -> K (in strain: MHN1)"
FT HELIX 25..42
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:1RGZ"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:1RGZ"
FT TURN 198..203
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 247..258
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 329..338
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1RGZ"
FT STRAND 354..362
FT /evidence="ECO:0007829|PDB:1RGZ"
FT HELIX 366..379
FT /evidence="ECO:0007829|PDB:1RGZ"
SQ SEQUENCE 381 AA; 41302 MW; 90F56ABAF07AA304 CRC64;
MMRKSLCCAL LLGISCSALA TPVSEKQLAE VVANTITPLM KAQSVPGMAV AVIYQGKPHY
YTFGKADIAA NKPVTPQTLF ELGSISKTFT GVLGGDAIAR GEISLDDAVT RYWPQLTGKQ
WQGIRMLDLA TYTAGGLPLQ VPDEVTDNAS LLRFYQNWQP QWKPGTTRLY ANASIGLFGA
LAVKPSGMPY EQAMTTRVLK PLKLDHTWIN VPKAEEAHYA WGYRDGKAVR VSPGMLDAQA
YGVKTNVQDM ANWVMANMAP ENVADASLKQ GIALAQSRYW RIGSMYQGLG WEMLNWPVEA
NTVVEGSDSK VALAPLPVAE VNPPAPPVKA SWVHKTGSTG GFGSYVAFIP EKQIGIVMLA
NTSYPNPARV EAAYHILEAL Q
