ID A0A098G2M7_9GAMM Unreviewed; 357 AA.
AC A0A098G2M7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 ORFNames=LFA_0266 {ECO:0000313|EMBL:CEG55740.1};
OS Legionella fallonii LLAP-10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1212491 {ECO:0000313|EMBL:CEG55740.1, ECO:0000313|Proteomes:UP000032430};
RN [1] {ECO:0000313|Proteomes:UP000032430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC700992 {ECO:0000313|Proteomes:UP000032430};
RA Gomez-Valero L.;
RL Submitted (SEP-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|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; LN614827; CEG55740.1; -; Genomic_DNA.
DR RefSeq; WP_045094565.1; NZ_LN614827.1.
DR AlphaFoldDB; A0A098G2M7; -.
DR STRING; 1212491.LFA_0266; -.
DR KEGG; lfa:LFA_0266; -.
DR HOGENOM; CLU_031960_0_0_6; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000032430; Chromosome.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000032430};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..357
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001942073"
FT DOMAIN 63..329
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 357 AA; 40924 MW; FF3447663BB30720 CRC64;
MKIKLLAQYT NLFRIKKHWQ CGLFSLLLSM SCWATSSDAE LAKKIDTIEK KSKSVIGITA
IYIEKNKIVG HNSNKRFFMA STIKLPIALA FLHRVDEKQD SLNRVIKMDM KNSVPGSGSL
HHLFEKKKLN MSMQQILKYM MRNSDNSASD TVLHAVNGPE YVKKRMDALG FKNIYVNRSI
LEMFLDTNHV DHAYLNKPQP VNAWQKTFNQ VPLEQKKLAW QRFENDTRDT TTPEDMAKLL
VKVYKKQALS EASTKVLMNI MEQCRTGRSR IRGLLPGSVK VAHKTGTWAI YEQDYLRYPG
VKKLYRFASD VGIITLPNNK GHIAIAVYVK SQSASDYPRS RAIALASRAV YDHFMRQ
//
