ID D4LXX9_9FIRM Unreviewed; 482 AA.
AC D4LXX9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=CK5_09850 {ECO:0000313|EMBL:CBL22482.1};
OS Blautia obeum A2-162.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=657314 {ECO:0000313|EMBL:CBL22482.1, ECO:0000313|Proteomes:UP000008955};
RN [1] {ECO:0000313|EMBL:CBL22482.1, ECO:0000313|Proteomes:UP000008955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2-162 {ECO:0000313|EMBL:CBL22482.1,
RC ECO:0000313|Proteomes:UP000008955};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Ruminococcus obeum A2-162.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL22482.1, ECO:0000313|Proteomes:UP000008955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2-162 {ECO:0000313|EMBL:CBL22482.1,
RC ECO:0000313|Proteomes:UP000008955};
RA Pajon A.;
RL Submitted (MAR-2010) 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 -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009}.
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DR EMBL; FP929054; CBL22482.1; -; Genomic_DNA.
DR AlphaFoldDB; D4LXX9; -.
DR KEGG; rob:CK5_09850; -.
DR PATRIC; fig|657314.3.peg.746; -.
DR HOGENOM; CLU_558593_0_0_9; -.
DR Proteomes; UP000008955; Chromosome.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..482
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003060822"
FT DOMAIN 249..458
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 482 AA; 52991 MW; 9158DAD73602450B CRC64;
MKTGNRLKNW KILAAGLVFM TTASAATAPV AASSLLSVTG ESQIRPIEDG SGKYILKSDG
FYCLKEDGSK DAAPAVHYFD HVNIDGTILD GFYYHDESGC FQAGSSNMVK ITKLSCAKST
DEDAETVDFD GYYMVNNLGK LTAAPQVRYI SNYVIDNTTY DGYYYFDENG KMVTETGTHE
LEMASNGQIF SGIYYFGGPN GALLQEAGVT EEGFPVDATG KVTALDDLGM DTLEPQLTSM
LSGYDGTWSV YVKDLATDEE IILNDTQIYS ASLIKVFVMA KTYEDMDTVL EHEAALMKTD
KDNAKVKAKV DTLLRNMITV SDNESCNELG RLQSEKHDFL DGAELVNKYL KKEGYTETTY
QNTLHPSSSQ KLSLGGHNMT TVKDCGKLLE RIYKGECVSR EASEEMLNLL SNQENTTKIP
EGVPADVKTA NKTGETDENQ HDIAIVYGPK TTYILCVMSE DSTNAIANIR SISKVVYNYL
NL
//
