ID D2EGV4_PEDAC Unreviewed; 400 AA.
AC D2EGV4;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-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=HMPREF9024_00016 {ECO:0000313|EMBL:EFA27199.1};
OS Pediococcus acidilactici 7_4.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus; Pediococcus acidilactici group.
OX NCBI_TaxID=563194 {ECO:0000313|EMBL:EFA27199.1, ECO:0000313|Proteomes:UP000005738};
RN [1] {ECO:0000313|EMBL:EFA27199.1, ECO:0000313|Proteomes:UP000005738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7_4 {ECO:0000313|EMBL:EFA27199.1,
RC ECO:0000313|Proteomes:UP000005738};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., 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., Allen-Vercoe E., Strauss J., Ambrose C., McDonald J., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Pediococcus acidilactici strain 7_4.";
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; GG730083; EFA27199.1; -; Genomic_DNA.
DR RefSeq; WP_002829257.1; NZ_GG730083.1.
DR AlphaFoldDB; D2EGV4; -.
DR HOGENOM; CLU_031960_9_4_9; -.
DR Proteomes; UP000005738; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 4.10.1060.50; -; 1.
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; IPR038587; Ribosomal_eL40_sf.
DR InterPro; IPR026870; Zinc_ribbon_dom.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR Pfam; PF13240; zinc_ribbon_2; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..24
FT /note="Zinc-ribbon"
FT /evidence="ECO:0000259|Pfam:PF13240"
FT DOMAIN 161..374
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 26..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 43622 MW; FD40C2A0A9C280C6 CRC64;
MFCQNCGTKN KPGAKFCRKC GTALRQPATQ PTPVTSQTAP TIPQPAPKQS APTEPSVTRE
EHQAAVKRKK HTGWLWITAG IILAIGFVGF FIYKNNPTIL SGVTHSDQAK VASSKSTSSV
SSTPQKKTSS ASTKKHLAFP KSTVEGTIRD AFGDISGDTA VYVSPVDSDT EVDFNDQPQR
AASDIKLFVM IAAYQQVKDG ELSLSDDYTL TDSDKVDGTG KLREMADGTK ISIKDLIGYM
MEDSDNTAAN IMIRKLGGMA AVNHQIDKMG ATDTKLERML MDTDALEDGK DNYTSAKDLG
TALKKIYNHQ MVSRKYDEEM LTILKQNGNH TKLPHDLPTE ATVYNKTGEF DDYGVENDAA
IFGNQKGAFV IVVMSQDGQR DEQINAMNSF GSVMYKGLLE
//
