ID I3VUE7_THESW Unreviewed; 418 AA.
AC I3VUE7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, 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 OrderedLocusNames=Tsac_1129 {ECO:0000313|EMBL:AFK86142.1};
OS Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacterium.
OX NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK86142.1, ECO:0000313|Proteomes:UP000006178};
RN [1] {ECO:0000313|Proteomes:UP000006178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RA Brown S.D., Land M.L., Herring C.D.;
RT "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFK86142.1, ECO:0000313|Proteomes:UP000006178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RX PubMed=24907337; DOI=10.1128/AEM.00998-14;
RA Currie D.H., Guss A.M., Herring C.D., Giannone R.J., Johnson C.M.,
RA Lankford P.K., Brown S.D., Hettich R.L., Lynd L.R.;
RT "Profile of Secreted Hydrolases, Associated Proteins, and SlpA in
RT Thermoanaerobacterium saccharolyticum during the Degradation of
RT Hemicellulose.";
RL Appl. Environ. Microbiol. 80:5001-5011(2014).
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; CP003184; AFK86142.1; -; Genomic_DNA.
DR AlphaFoldDB; I3VUE7; -.
DR STRING; 1094508.Tsac_1129; -.
DR KEGG; tsh:Tsac_1129; -.
DR PATRIC; fig|1094508.3.peg.1142; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG2367; Bacteria.
DR eggNOG; COG3409; Bacteria.
DR BioCyc; TSAC1094508:GLMA-1151-MONOMER; -.
DR Proteomes; UP000006178; Chromosome.
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 CDD; cd00118; LysM; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251}.
FT DOMAIN 109..153
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 418 AA; 46639 MW; 26EADDDD02320FCC CRC64;
MRKIKMLFLY LLMLAVVFMP VISYGDNGLP QFQFGSRLLY TGTYGTDVSE LQSILNSIGF
NTGTIDGIFG NNTLNGVLDF QKAENLVVDG IVGPNTYNAI QNGLWENPVV YDVQPNDNIY
FIAKKYGTSV QDILDENGLS DNASLYVGEK LLIPHPPVTV PQQLDNASNY QQLKDNIETL
LSQHTGNYGV YFIDLNSGET FDINGYGSFI AASTYKVPLN FYVYTLITEG KIDPNMEVQY
TSQDYEGGSG SIQYDPVGTY YTIRELSKKS IEESDNIASN MLMRVVGYDN YLNFIKSLGA
YVVPYSDNVT SPRDLSIYME DILNYANAYS STSGELLSYL ENTIYNDRIS YPLPSNITVA
HKIGNLSNVV NDTAIVFYPS KPYILTVMGN NVDGSDNSDA YTVIREISKM VYDFQNSH
//
