ID A0A1Q9YE49_9FIRM Unreviewed; 428 AA.
AC A0A1Q9YE49;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=BM735_05830 {ECO:0000313|EMBL:OLU40300.1};
OS Erysipelotrichaceae bacterium NYU-BL-F16.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=1917462 {ECO:0000313|EMBL:OLU40300.1, ECO:0000313|Proteomes:UP000186748};
RN [1] {ECO:0000313|EMBL:OLU40300.1, ECO:0000313|Proteomes:UP000186748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NYU-BL-F16 {ECO:0000313|EMBL:OLU40300.1,
RC ECO:0000313|Proteomes:UP000186748};
RA Cox L.M., Sohn J., Tyrrell K.L., Citron D.M., Lawson P.A., Patel N.B.,
RA Iizumi T., Perez-Perez G.I., Goldstein E.J., Blaser M.J.;
RT "Description of two novel members of the family Erysipelotrichaceae:
RT Ileibacterium lipovorans gen. nov., sp. nov. and Dubosiella newyorkensis,
RT gen. nov., sp. nov.";
RL Submitted (NOV-2016) 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}.
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:OLU40300.1}.
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DR EMBL; MPJX01000126; OLU40300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9YE49; -.
DR Proteomes; UP000186748; Unassembled WGS sequence.
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.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251}.
FT DOMAIN 128..331
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 399..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 48464 MW; 63E20AE9D330957A CRC64;
MGTKHSKNST GSKRKRSRRI NYKRLAVVGV CALTLAGALV YGGYKAYSFV DYKLNGRKPI
VLESGEELPF IDLYSLRAEI QDVMTMKNLK HLRSDIQTFM FNNQLSDLKD QINAYLTENQ
IDSSKIAWAV QDLTTNAYTE SDNAHQNYTA ASTYKLPLSM LWYEKVQDGS AKMDDTFELT
ERMLEKEDTE NPDQPIGRKY RLGDRIPLSE LLEGAALYSD NIAGHILFEN LGGYTAYKTQ
ALKYSDTLQD KEFTSSQNVL NPHYTMNLVN YMWNHPGTFD ELKYWLYCAI QGNFLNRSAQ
LGYIQKIGNI EEVRNAIGLM PGEFPYSVSV YSSIDAKKGE EVIGDIGLIC YNYFLNKYNS
GFYDPAQLEG NLEKSNMAYK ESALAPYATS SWTGGSVYDA FQKDEKKDEN QSDSQNNNQQ
SDNQAAPA
//
