ID A0A0W0TM57_9GAMM Unreviewed; 351 AA.
AC A0A0W0TM57;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN Name=per1 {ECO:0000313|EMBL:SPX60652.1};
GN ORFNames=Lfee_1591 {ECO:0000313|EMBL:KTC96679.1}, NCTC12022_01384
GN {ECO:0000313|EMBL:SPX60652.1};
OS Legionella feeleii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=453 {ECO:0000313|EMBL:KTC96679.1, ECO:0000313|Proteomes:UP000054698};
RN [1] {ECO:0000313|EMBL:KTC96679.1, ECO:0000313|Proteomes:UP000054698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-44C {ECO:0000313|EMBL:KTC96679.1,
RC ECO:0000313|Proteomes:UP000054698};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SPX60652.1, ECO:0000313|Proteomes:UP000251942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12022 {ECO:0000313|EMBL:SPX60652.1,
RC ECO:0000313|Proteomes:UP000251942};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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|ARBA:ARBA00001526,
CC ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; LNYB01000080; KTC96679.1; -; Genomic_DNA.
DR EMBL; UASS01000011; SPX60652.1; -; Genomic_DNA.
DR RefSeq; WP_058445601.1; NZ_UASS01000011.1.
DR AlphaFoldDB; A0A0W0TM57; -.
DR STRING; 453.Lfee_1591; -.
DR PATRIC; fig|453.4.peg.1749; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000054698; Unassembled WGS sequence.
DR Proteomes; UP000251942; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam 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; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR023650; Beta-lactam_class-A_AS.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW Reference proteome {ECO:0000313|Proteomes:UP000054698};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..351
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033244697"
FT DOMAIN 51..322
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 351 AA; 40124 MW; 1D9BE8749EF8AC3F CRC64;
MKGKLFLKYI NRLLNLFLYL VFSMNCFAAN SEAQLVKKIY DIEKRSNAVI GITAIHIEKN
KVIGHNGNKR FFMASTIKLP IALAFLHLVD QKKDSLNRVV NLGLNNVVPG SGTLHYLCER
KKIRMSLQQI LKYMMANSDN SASDTLLQTV NGPAYVTKRM HALGFKNIVI NRSIIEMMMD
TNHVHPSLKQ PRTVYSWKKI FNRTPLKEKM LAWQRFEKDP RDTTTPAEMA KLLVKIYKNE
ALSESSTKVL MDIMEKCRTG RSRIRGLLPP YVKVAHKTGT WAIDEPQYIR YPGSNKLFRF
VSDVGIITLP NNKGHIAIAV YVKSRAVSNY TRSRAIALAS RAIYDHFMAQ K
//
