AMPC_CITFR
ID AMPC_CITFR Reviewed; 381 AA.
AC P05193;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Beta-lactamase;
DE EC=3.5.2.6;
DE AltName: Full=Cephalosporinase;
DE Flags: Precursor;
GN Name=ampC; Synonyms=blaC;
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=OS60;
RX PubMed=3486121; DOI=10.1111/j.1432-1033.1986.tb09601.x;
RA Lindberg F., Normark S.;
RT "Sequence of the Citrobacter freundii OS60 chromosomal ampC beta-lactamase
RT gene.";
RL Eur. J. Biochem. 156:441-445(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GN346;
RX PubMed=1969344; DOI=10.1111/j.1432-1033.1990.tb15365.x;
RA Tsukamoto K., Tachibana K., Yamazaki N., Ishii Y., Ujiie K., Nishida N.,
RA Sawai T.;
RT "Role of lysine-67 in the active site of class C beta-lactamase from
RT Citrobacter freundii GN346.";
RL Eur. J. Biochem. 188:15-22(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-381, AND INHIBITION BY SULBACTAM.
RC STRAIN=GN346;
RX PubMed=3263684; DOI=10.1093/clinids/10.4.721;
RA Sawai T., Yamaguchi A., Tsukamoto K.;
RT "Amino acid sequence, active-site residue, and effect of suicide inhibitors
RT on cephalosporinase of Citrobacter freundii GN346.";
RL Rev. Infect. Dis. 10:721-725(1988).
RN [4]
RP PROTEIN SEQUENCE OF 66-87.
RX PubMed=3496243; DOI=10.1016/0014-5793(87)81031-1;
RA Yamaguchi A., Adachi H., Sawai T.;
RT "Identification of the active site of Citrobacter freundii beta-lactamase
RT using dansyl-penicillin.";
RL FEBS Lett. 218:126-130(1987).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=2300174; DOI=10.1038/343284a0;
RA Oefner C., D'Arcy A.A., Daly J.J., Gubernator K., Charnas R.L., Heinze I.,
RA Hubschwerlen C., Winkler F.K.;
RT "Refined crystal structure of beta-lactamase from Citrobacter freundii
RT indicates a mechanism for beta-lactam hydrolysis.";
RL Nature 343:284-288(1990).
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 -!- ACTIVITY REGULATION: Sulbactam is an effective progressive inhibitor
CC but a poor competitive inhibitor.
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; X03866; CAA27494.1; -; Genomic_DNA.
DR EMBL; X51632; CAA35959.1; -; Genomic_DNA.
DR PIR; S08296; S08296.
DR PDB; 1RGY; X-ray; 1.52 A; A=22-381.
DR PDBsum; 1RGY; -.
DR AlphaFoldDB; P05193; -.
DR SMR; P05193; -.
DR STRING; 1333848.CFNIH1_08415; -.
DR BindingDB; P05193; -.
DR ChEMBL; CHEMBL1255130; -.
DR DrugBank; DB00355; Aztreonam.
DR DrugCentral; P05193; -.
DR MEROPS; S12.006; -.
DR SABIO-RK; P05193; -.
DR EvolutionaryTrace; P05193; -.
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; IMP:CACAO.
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; Signal.
FT SIGNAL 1..20
FT CHAIN 21..381
FT /note="Beta-lactamase"
FT /id="PRO_0000016957"
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 /evidence="ECO:0000250"
FT VARIANT 97
FT /note="R -> A (in strain: GN346)"
FT VARIANT 143
FT /note="G -> D (in strain: GN346)"
FT VARIANT 145
FT /note="V -> I (in strain: GN346)"
FT VARIANT 150
FT /note="E -> A (in strain: GN346)"
FT VARIANT 185
FT /note="S -> P (in strain: GN346)"
FT VARIANT 224
FT /note="L -> R (in strain: GN346)"
FT VARIANT 243
FT /note="V -> L (in strain: GN346)"
FT VARIANT 325
FT /note="A -> V (in strain: GN346)"
FT VARIANT 368
FT /note="A -> V (in strain: GN346)"
FT CONFLICT 98
FT /note="I -> T (in Ref. 3)"
FT /evidence="ECO:0000305"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:1RGY"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:1RGY"
FT TURN 183..187
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:1RGY"
FT TURN 198..203
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 247..258
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 300..306
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 329..338
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1RGY"
FT STRAND 354..362
FT /evidence="ECO:0007829|PDB:1RGY"
FT HELIX 366..378
FT /evidence="ECO:0007829|PDB:1RGY"
SQ SEQUENCE 381 AA; 41975 MW; 3F955F6933F0D76B CRC64;
MMKKSICCAL LLTASFSTFA AAKTEQQIAD IVNRTITPLM QEQAIPGMAV AIIYEGKPYY
FTWGKADIAN NHPVTQQTLF ELGSVSKTFN GVLGGDRIAR GEIKLSDPVT KYWPELTGKQ
WRGISLLHLA TYTAGGLPLQ IPGDVTDKAE LLRFYQNWQP QWTPGAKRLY ANSSIGLFGA
LAVKSSGMSY EEAMTRRVLQ PLKLAHTWIT VPQSEQKNYA WGYLEGKPVH VSPGQLDAEA
YGVKSSVIDM ARWVQANMDA SHVQEKTLQQ GIELAQSRYW RIGDMYQGLG WEMLNWPLKA
DSIINGSDSK VALAALPAVE VNPPAPAVKA SWVHKTGSTG GFGSYVAFVP EKNLGIVMLA
NKSYPNPARV EAAWRILEKL Q
