ID Q3K9U3_PSEPF Unreviewed; 388 AA.
AC Q3K9U3;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 103.
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};
GN OrderedLocusNames=Pfl01_3723 {ECO:0000313|EMBL:ABA75461.1};
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA75461.1, ECO:0000313|Proteomes:UP000002704};
RN [1] {ECO:0000313|EMBL:ABA75461.1, ECO:0000313|Proteomes:UP000002704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA75461.1,
RC ECO:0000313|Proteomes:UP000002704};
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(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; CP000094; ABA75461.1; -; Genomic_DNA.
DR RefSeq; WP_011335056.1; NC_007492.2.
DR AlphaFoldDB; Q3K9U3; -.
DR MEROPS; S12.006; -.
DR KEGG; pfo:Pfl01_3723; -.
DR eggNOG; COG1680; Bacteria.
DR HOGENOM; CLU_020027_10_0_6; -.
DR Proteomes; UP000002704; Chromosome.
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..388
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004227161"
FT DOMAIN 39..383
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 388 AA; 41922 MW; A08884EB7DABA36B CRC64;
MSSTNLRKLK SYSAFGLFFS AATCLAAPQT DDQLQALVKA TVTPVMQQQD IAGLAVAVTV
NGKAHYFNYG VADKSTGQAV SENTLFEIGS VSKTFTAILA AYAQASGKLQ LSDKASQHWP
ELKGSAFDHI SLLQLGTYSA GGLPLQFPDA ADSADKMLGY YQQWKPTYPA GSHRLYSNPS
IGLFGYLAAK SLGQPFNQVM TETLLPKLGL KHTFLSVPAS EQKLYAQGYD KNNKPIRVSP
GALDSEAYGV KTSAADLLQY VQANLDTAKL ETPLQKAIAL THTGYYTVGD MTQGLGWERY
AYPISLDRLL DGNSTPMAME AHKVKWLNPP QPEPANVLLN KTGSTGGYGA YVAFVPSKKV
GIVILANRNY PNGERVKIAH RILGELTR
//
