ID C4NY28_PSEAI Unreviewed; 397 AA.
AC C4NY28;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
OS Pseudomonas aeruginosa.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287 {ECO:0000313|EMBL:ACQ82809.1};
RN [1] {ECO:0000313|EMBL:ACQ82809.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Paebeta-20 {ECO:0000313|EMBL:ACQ82809.1};
RX PubMed=19258272; DOI=10.1128/AAC.01410-08;
RA Rodriguez-Martinez J.M., Poirel L., Nordmann P.;
RT "Extended-spectrum cephalosporinases in Pseudomonas aeruginosa.";
RL Antimicrob. Agents Chemother. 53:1766-1771(2009).
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;
CC Evidence={ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007840, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; FJ666067; ACQ82809.1; -; Genomic_DNA.
DR RefSeq; WP_063864580.1; NG_049912.1.
DR AlphaFoldDB; C4NY28; -.
DR SMR; C4NY28; -.
DR KEGG; ag:ACQ82809; -.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..397
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002941725"
FT DOMAIN 38..386
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 397 AA; 43372 MW; A42618D2C4E8D637 CRC64;
MRDTRFPCLC GIAASTLLFA TTPAIAGEAP ADRLKALVDA AVQPVMKAND IPGLAVAISL
KGEPHYFSYG LASKEDGRRV TPETLFEIGS VSKTFTATLA GYALAQDEMR 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
//
