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Database: UniProt
Entry: A0A076MNC8_AMYME
LinkDB: A0A076MNC8_AMYME
Original site: A0A076MNC8_AMYME 
ID   A0A076MNC8_AMYME        Unreviewed;       292 AA.
AC   A0A076MNC8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   Name=penP {ECO:0000313|EMBL:AIJ22368.1};
GN   ORFNames=AMETH_2276 {ECO:0000313|EMBL:AIJ22368.1};
OS   Amycolatopsis methanolica 239.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX   NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ22368.1, ECO:0000313|Proteomes:UP000062973};
RN   [1] {ECO:0000313|EMBL:AIJ22368.1, ECO:0000313|Proteomes:UP000062973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=239 {ECO:0000313|EMBL:AIJ22368.1,
RC   ECO:0000313|Proteomes:UP000062973};
RA   Tang B.;
RT   "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL   Submitted (JUL-2014) 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}.
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DR   EMBL; CP009110; AIJ22368.1; -; Genomic_DNA.
DR   RefSeq; WP_038532948.1; NZ_CP009110.1.
DR   AlphaFoldDB; A0A076MNC8; -.
DR   STRING; 1068978.AMETH_2276; -.
DR   KEGG; amq:AMETH_2276; -.
DR   PATRIC; fig|1068978.7.peg.2420; -.
DR   eggNOG; COG2367; Bacteria.
DR   HOGENOM; CLU_031960_6_0_11; -.
DR   OrthoDB; 9784149at2; -.
DR   Proteomes; UP000062973; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000062973};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..292
FT                   /note="beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038588347"
FT   DOMAIN          55..265
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   292 AA;  30911 MW;  CE1827B21CD30128 CRC64;
     MLVRTLRAVV VLLVFGLVGA CATEPPPPPP AASTAAPAPR VDFADLEARF DARLGVYAID
     TGTGREIAHR ADERFNYASA IKSLLAGAVL RRNVDLDKVV AYTDADVQPN SPVTKDRRSV
     TVREAAEAAL LQSDNTAANL LFAEVGGPAG LAAVLRDIGD TTTHPDRLEV ELNSAIPGDV
     RDTSTPRAMA GSLRAFLLGE ALPADKRDLL VGIMRRNKTG TELIRAGVPS EWPVADKTGT
     GDYGTRNDIG VIWPPGHAPI VLALMSSRAT ADASYDNKLL AEATSRVMDA LR
//
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