ID A0A077F745_9PSED Unreviewed; 389 AA.
AC A0A077F745;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
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 ORFNames=PSAKL28_20770 {ECO:0000313|EMBL:AIL61298.1};
OS Pseudomonas alkylphenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL61298.1, ECO:0000313|Proteomes:UP000028931};
RN [1] {ECO:0000313|EMBL:AIL61298.1, ECO:0000313|Proteomes:UP000028931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KL28 {ECO:0000313|EMBL:AIL61298.1,
RC ECO:0000313|Proteomes:UP000028931};
RA Lee K., Lim J.Y., Hwang I.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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; CP009048; AIL61298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077F745; -.
DR KEGG; palk:PSAKL28_20770; -.
DR eggNOG; COG1680; Bacteria.
DR HOGENOM; CLU_020027_10_0_6; -.
DR Proteomes; UP000028931; 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:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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 Carboxypeptidase {ECO:0000313|EMBL:AIL61298.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Protease {ECO:0000313|EMBL:AIL61298.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..389
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001718478"
FT DOMAIN 41..386
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 389 AA; 42202 MW; 48A63F87CC6AE4F4 CRC64;
MMHYKTRLKP GILLAVTLCI AAGQSIASPL CEAQLESTVS TAIQPLMQQQ AIPGMAVAIS
VNGKQHYFNY GEASKHSGQP VSAETLFEIG SVSKTFTATL AAYAEASGKL SLSDPASKHW
PELKGSAFDG ITLLNLGTYS AGGLPLQFPE QVKDQASLLG YYRHWKADYA PGTHRLYSNP
SLGLFGYLAA KSMDTPFAEL MQKQLLPQLG LLHTYVQVPA TQMGHYAQGY DKDNQAVRVG
PGPLDAEAYG LKTTSADLLR FVEANLQPQS LSAPLQRAIA TTQTGYYRVG EMTQGLGWEQ
YRYPVSLDQL LAGNSTAMTL EPQRVTWLKP ARPLQDDMLL NKTGSTNGFG AYVLFVPSKH
IGIVLLANKN YPNAERVKVA HAILTALDH
//
