ID A0A1M3DAN0_9SPHN Unreviewed; 381 AA.
AC A0A1M3DAN0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=BGO24_17775 {ECO:0000313|EMBL:OJV31075.1};
OS Sphingomonas sp. 67-36.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1895849 {ECO:0000313|EMBL:OJV31075.1, ECO:0000313|Proteomes:UP000183964};
RN [1] {ECO:0000313|EMBL:OJV31075.1, ECO:0000313|Proteomes:UP000183964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=67-36 {ECO:0000313|EMBL:OJV31075.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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:OJV31075.1}.
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DR EMBL; MKSU01000017; OJV31075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3DAN0; -.
DR STRING; 1895849.BGO24_17775; -.
DR Proteomes; UP000183964; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
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 PRINTS; PR00118; BLACTAMASEA.
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};
KW Hydrolase {ECO:0000313|EMBL:OJV31075.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..381
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012770093"
FT DOMAIN 81..339
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 381 AA; 40302 MW; 30971E8126DFFCD8 CRC64;
MTGSRIGWLT AGFGTLALAA CGPGTRPGTS ASAPAATYVG APAYVVSLPV PKVMRRPRIE
APRALVEQVD ALVRGFPGVA GIAIRAVDDG WTVESGGRRR MPQQSVSKLW VAMTVLDQRD
SGRLKLDDPV TLYPSDLTLF HQPIAALVKP SGYQTTVGAL LTRALTHSDN TANDRLLTLV
GGPAAVRSFI ERKQLGDIRF GPGERLLQSR TAGLTWQQSY SLGNGFEIAR SRLAPEVRAA
ALEAYIADPP DGAAPLAIAD ALARLARGEL LSETSTRFLL TTMGSTVTGR ARLKAALPPG
WSLEHKTGTG QELGRRNAGF NDVGLLTAPD GRRYAIAVMI GDTMRPMRDR QLLIQAAAGA
LTGHRADPRA IASTEDDAPG S
//
