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Database: UniProt
Entry: B0MWK8_9BACT
LinkDB: B0MWK8_9BACT
Original site: B0MWK8_9BACT 
ID   B0MWK8_9BACT            Unreviewed;       322 AA.
AC   B0MWK8;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, 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=ALIPUT_01542 {ECO:0000313|EMBL:EDS03331.1};
OS   Alistipes putredinis DSM 17216.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=445970 {ECO:0000313|EMBL:EDS03331.1, ECO:0000313|Proteomes:UP000005819};
RN   [1] {ECO:0000313|EMBL:EDS03331.1, ECO:0000313|Proteomes:UP000005819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17216 {ECO:0000313|EMBL:EDS03331.1,
RC   ECO:0000313|Proteomes:UP000005819};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS03331.1, ECO:0000313|Proteomes:UP000005819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17216 {ECO:0000313|EMBL:EDS03331.1,
RC   ECO:0000313|Proteomes:UP000005819};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Alistipes putredinis (DSM 17216).";
RL   Submitted (NOV-2007) 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:EDS03331.1}.
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DR   EMBL; ABFK02000019; EDS03331.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0MWK8; -.
DR   eggNOG; COG2367; Bacteria.
DR   HOGENOM; CLU_031960_0_1_10; -.
DR   OrthoDB; 9772863at2; -.
DR   Proteomes; UP000005819; 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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..322
FT                   /note="beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002750587"
FT   DOMAIN          45..266
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   322 AA;  35998 MW;  F62340252DAB6A54 CRC64;
     MRTLISILWI SFFPLAAAAQ GDDLSYRLKK VIKDKKAEIG IAVILDAQDT VTVNNDDRYP
     LMSVFKFHQA LAVADYLDRN GLTPDTEIFI PEEELVPDTY SPLRKEFPEG EISLSVSRLL
     EYSLQLSDNN ACDILFEHTG GPAATDRYVR SLGLRNFAIA ATEQQMHDDP QTCYENWSTP
     LEAAALLELL VTEQILTPTL REMIRQNLIN CKTGADRLPK PLSGTGAVIG HKTGTSDRDE
     RGIFAGTNDP GFVILPDGTR YTIAVFIKDS AENPETNARI IADISETVYR YVHDEYREND
     IRPGKKHVDQ GAGIGFESDY FY
//
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