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Database: UniProt
Entry: A0A0M2HTG1_9MICO
LinkDB: A0A0M2HTG1_9MICO
Original site: A0A0M2HTG1_9MICO 
ID   A0A0M2HTG1_9MICO        Unreviewed;       313 AA.
AC   A0A0M2HTG1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, 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=RS84_01397 {ECO:0000313|EMBL:KJL47769.1};
OS   Microbacterium hydrocarbonoxydans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=273678 {ECO:0000313|EMBL:KJL47769.1, ECO:0000313|Proteomes:UP000033900};
RN   [1] {ECO:0000313|EMBL:KJL47769.1, ECO:0000313|Proteomes:UP000033900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA35 {ECO:0000313|EMBL:KJL47769.1,
RC   ECO:0000313|Proteomes:UP000033900};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) 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:KJL47769.1}.
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DR   EMBL; JYJB01000008; KJL47769.1; -; Genomic_DNA.
DR   RefSeq; WP_045257060.1; NZ_JYJB01000008.1.
DR   AlphaFoldDB; A0A0M2HTG1; -.
DR   STRING; 273678.RS84_01397; -.
DR   PATRIC; fig|273678.4.peg.1395; -.
DR   OrthoDB; 3673924at2; -.
DR   Proteomes; UP000033900; 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   Reference proteome {ECO:0000313|Proteomes:UP000033900}.
FT   DOMAIN          60..285
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   313 AA;  33420 MW;  D01376B389BF8DC8 CRC64;
     MGAPEPVEGF RHSSSSDSSS GRRSQRATRR LPRRAAIGRR SFTSTLRSLE TLADAGAQVS
     VHVVDLDSHV HVLSGDDHVT MPIAGLGVVP LLVEVAAAFE AGTLDPLEIV ERTATEQVLT
     SGVWRHLHAP ALPLEDLAVL AAAAGDPIAA NALLQKVGHD RVRERIESLG LRRTALLDRF
     RDQRGPDDAP HVAVGSSREL AGLFSALVNS QVVDAAVSAQ VSEWLSLNQD LSLVAASTGL
     DPFAHDHDAH GLLFINKTGR DRGVRAEAGV LAGPRAGVAY SLIVCFDDLS IAHRLRAHDA
     FRVLGVELME YTH
//
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