ID D2EMI2_9STRE Unreviewed; 423 AA.
AC D2EMI2;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=HMPREF0850_00984 {ECO:0000313|EMBL:EFA25189.1};
OS Streptococcus sp. M143.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=563037 {ECO:0000313|EMBL:EFA25189.1, ECO:0000313|Proteomes:UP000002766};
RN [1] {ECO:0000313|EMBL:EFA25189.1, ECO:0000313|Proteomes:UP000002766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M143 {ECO:0000313|EMBL:EFA25189.1,
RC ECO:0000313|Proteomes:UP000002766};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S.,
RA Surette M.G., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. strain M143.";
RL Submitted (OCT-2009) 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; GG730093; EFA25189.1; -; Genomic_DNA.
DR RefSeq; WP_001224824.1; NZ_GG730093.1.
DR AlphaFoldDB; D2EMI2; -.
DR eggNOG; COG2367; Bacteria.
DR HOGENOM; CLU_053694_0_0_9; -.
DR OrthoDB; 2240388at2; -.
DR Proteomes; UP000002766; 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 202..403
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 423 AA; 48202 MW; AAC6A6C2BA9B4EEA CRC64;
MRKFLVVLSL LSVFIITSRV VSTEKQLPYS SQEIYYLTES DHGFYYKEVL ESPMVYGETA
VYANEDLVKE SGKLTSETTF KIVEWRLNRQ GIPVFKLNNH QFIVADKRLV YDQSQVQTQN
RQVWLEPGFV IYNSPYGAKE ISSSLSPYQR VTVDRTLFAE GQEFLHIDQV GWVSKEFVSE
EDNRIQKVQE VLSNNYQNEN YSIYVKQLST GKEAGVNEDS KLYAASILKL AYLYYAQDKI
NQGEYTLNSN FKYIPEVNSF PGSYKPEGSG SLPKTGDNKD YSLQQLITKV TKESDNVAHN
ILGYYVTNQS DGAFKEKMST IMGEDWDVND KLTSSKMAGK VMEAIYNQNG FVLESLSKTN
FDNQRIAKGV SVKVAHKIGD ADEFKHDTAI VYTDSPFVLS IFTKNSDYDT IAKIAKDVYE
VLK
//
