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Database: UniProt
Entry: A0A2A5YFA4_9SPHN
LinkDB: A0A2A5YFA4_9SPHN
Original site: A0A2A5YFA4_9SPHN 
ID   A0A2A5YFA4_9SPHN        Unreviewed;       372 AA.
AC   A0A2A5YFA4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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=CNE89_15045 {ECO:0000313|EMBL:PDH63094.1};
OS   Sphingomonadaceae bacterium MED-G03.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae.
OX   NCBI_TaxID=1986231 {ECO:0000313|EMBL:PDH63094.1, ECO:0000313|Proteomes:UP000219365};
RN   [1] {ECO:0000313|EMBL:PDH63094.1, ECO:0000313|Proteomes:UP000219365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED-G03 {ECO:0000313|EMBL:PDH63094.1};
RA   Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA   Rodriguez-Valera F.;
RT   "Fine stratification of microbial communities through a metagenomic profile
RT   of the photic zone.";
RL   Submitted (AUG-2017) 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:PDH63094.1}.
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DR   EMBL; NTKY01000068; PDH63094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A5YFA4; -.
DR   Proteomes; UP000219365; 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.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Hydrolase {ECO:0000313|EMBL:PDH63094.1}.
FT   DOMAIN          79..333
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   372 AA;  39733 MW;  4E84345F913518EF CRC64;
     MPPLTRSPLA RSIPTRFGAP RVRASRLAAA LAGFGLFFAP LPSADAFGPP PRPLVEQTAQ
     AKLLAEFERF AALSDGTVGI AVRDLQTGET QSFNGDTLFP MASAYKVAVA GRIFALVDAG
     ELRLDDQLAL DPALASEGGI AWMFSRPGAA LSVQRLLELM LQKSDNNATD VLVARAGGPQ
     AITRFVTGLG VNGLRVDSDT AHLLYRAMGI HPSSGSFRHN ADAARRADPM IVTRDMRDLP
     NLSFATEIED TSTPRAMLDL LSAYESGRAL SADSTQRLFT IMAHCETGKH RIVGMLPPGT
     AVAHKTGSLN GTGNDVGVVR LPDGRRFAVV AFVMKDGKGH KARDRIIAEA ARAAYDYFLY
     APERAHGSTH KS
//
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