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Database: UniProt
Entry: A0A1R1BW06_9BACL
LinkDB: A0A1R1BW06_9BACL
Original site: A0A1R1BW06_9BACL 
ID   A0A1R1BW06_9BACL        Unreviewed;       385 AA.
AC   A0A1R1BW06;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=BK127_19155 {ECO:0000313|EMBL:OMF14053.1};
OS   Paenibacillus sp. FSL H7-0331.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1920421 {ECO:0000313|EMBL:OMF14053.1, ECO:0000313|Proteomes:UP000187480};
RN   [1] {ECO:0000313|EMBL:OMF14053.1, ECO:0000313|Proteomes:UP000187480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0331 {ECO:0000313|EMBL:OMF14053.1,
RC   ECO:0000313|Proteomes:UP000187480};
RA   Beno S.M.;
RT   "Paenibacillus species isolates.";
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:OMF14053.1}.
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DR   EMBL; MRTH01000012; OMF14053.1; -; Genomic_DNA.
DR   RefSeq; WP_076233098.1; NZ_MRTH01000012.1.
DR   AlphaFoldDB; A0A1R1BW06; -.
DR   STRING; 1920421.BK127_19155; -.
DR   OrthoDB; 975092at2; -.
DR   Proteomes; UP000187480; 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; 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};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187480};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          60..174
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   385 AA;  42838 MW;  D167B2027CB6802B CRC64;
     MKKWVWIVII VVVLIIGLAG WIIGTLVWAG KPNADYVWEF VKKHPEQASV TLVSNGVIVA
     QTEPDRPMPL ASTVKIIVAI EYAKQAAAGT VKPDEPVLLQ KLESYYLPDL DGGAHPSWLS
     DMESKQRVRD GAVTLEEVAK GMIMFSSNAN TEYLMEKLGL ANINRNIGEL GMKSHEPLYP
     FVSSLLIPYE LMQTYPGLER NDALAKAITE LKDMPMEVFR VKAVGIHEKL RQDNDGAYKR
     QANIKDWYNE KLDRMNSDKL IAASTADYAS LLAKMNGKTY FAPAVQKNLD IIMEGLMENP
     ANRSMFEHAG RKGGSTAFVL TDAMYATDKE GNRTELAIFF NNLDEIQAMK LSASLNAFEV
     ELLKNADFRS KAAAGMDSTQ RPLNK
//
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