ID A0A0M9WV75_9BACI Unreviewed; 270 AA.
AC A0A0M9WV75;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=AN161_11830 {ECO:0000313|EMBL:KOS62981.1};
OS Lysinibacillus sp. FJAT-14222.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1932366 {ECO:0000313|EMBL:KOS62981.1, ECO:0000313|Proteomes:UP000037693};
RN [1] {ECO:0000313|EMBL:KOS62981.1, ECO:0000313|Proteomes:UP000037693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17725 {ECO:0000313|EMBL:KOS62981.1,
RC ECO:0000313|Proteomes:UP000037693};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-2015) 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-D beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007898, ECO:0000256|RuleBase:RU361140}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOS62981.1}.
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DR EMBL; LIYL01000021; KOS62981.1; -; Genomic_DNA.
DR RefSeq; WP_053594533.1; NZ_LIYL01000021.1.
DR AlphaFoldDB; A0A0M9WV75; -.
DR STRING; 1932366.AN161_11830; -.
DR PATRIC; fig|380630.3.peg.5876; -.
DR OrthoDB; 9762883at2; -.
DR Proteomes; UP000037693; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
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; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR002137; Beta-lactam_class-D_AS.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627:SF6; BETA-LACTAMASE YBXI-RELATED; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00337; BETA_LACTAMASE_D; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..270
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005839952"
FT DOMAIN 53..251
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 79
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
FT MOD_RES 82
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
SQ SEQUENCE 270 AA; 31166 MW; 7AFCB656F55EB67A CRC64;
MKKIFYYVLT LLLTLGIVGC SAQPESNNPN ILSEVNVNQV QADPFFKDHD GTFILRDLKT
EETYIYNEQR ANEKLTPQST FKVPNALIGL QLGVVRDEYD IKKWDGTEHE IISWNHDYTL
GSGMRDSVVW YYQAMARDIG EQGMKEWLHK LSYGNENISG GIDQFWLQSS LKISPLEEVD
FMEKLYKEDL PFDKSVMKTV KRMMIQEEGD HYILYGKTGT RITDMGLGWF VGFIVVENHP
YVFVTNLDDS GTVAKNITLE MLKQYNLITE
//
