ID A0A124FPS8_9FIRM Unreviewed; 328 AA.
AC A0A124FPS8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, 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=XD78_0883 {ECO:0000313|EMBL:KUK53786.1};
OS Desulfotomaculum sp. 46_296.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=1635262 {ECO:0000313|EMBL:KUK53786.1, ECO:0000313|Proteomes:UP000053813};
RN [1] {ECO:0000313|Proteomes:UP000053813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK53786.1}.
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DR EMBL; LGFZ01000021; KUK53786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124FPS8; -.
DR STRING; 1635262.XD78_0883; -.
DR PATRIC; fig|1635262.3.peg.1232; -.
DR Proteomes; UP000053813; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251}.
FT DOMAIN 97..299
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 328 AA; 36331 MW; 9925B3A8F26D6F2C CRC64;
MKRSNALRVL FVILLLFVFT GCGLAKDSSV MNRNVTGKDT TEKRIVSSEK PASDKIVTEA
PVSEKIMISE KPVSNKNYSQ LIKQINEYTM TQPGFYGIYF KDLDSGAVFD INGNEPITAA
SLVKVPAVLY LNTLIDQGEL NWDDTVAYES GVDYQSGAGT LQFSARDGDE YSLRTLANLS
ITVSDNIAYR MIVRKVGKDN LANFMRSLGG ETVFPGGWNI TTAEDMGKYV EAILKFNEKN
PEMGQKLLYD MAHSIYNVGL NGRIDKSVTV SHKEGDVTGV ANDAGIVFAE RPYILVVLTK
NVDDIDRGFE RIAEISRIVY DYHINEPA
//
