ID A0A1C4XQ95_MICEC Unreviewed; 311 AA.
AC A0A1C4XQ95;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN ORFNames=GA0070618_3256 {ECO:0000313|EMBL:SCF10668.1};
OS Micromonospora echinospora (Micromonospora purpurea).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1877 {ECO:0000313|EMBL:SCF10668.1, ECO:0000313|Proteomes:UP000198253};
RN [1] {ECO:0000313|EMBL:SCF10668.1, ECO:0000313|Proteomes:UP000198253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43816 {ECO:0000313|EMBL:SCF10668.1,
RC ECO:0000313|Proteomes:UP000198253};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; LT607413; SCF10668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4XQ95; -.
DR InParanoid; A0A1C4XQ95; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000198253; Chromosome i.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
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 InterPro; IPR023650; Beta-lactam_class-A_AS.
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; PS00146; BETA_LACTAMASE_A; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140}.
FT DOMAIN 69..283
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 180..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 32088 MW; 3D110D1A04CEDFF1 CRC64;
MALTGRVRRA VAGVVVTGLL GLAACGSGEP SSPVPAPTGA VASTPTAAAP SAADRSFDAL
EARFAARLGV FAIDTGSGAT VTHRADERFA YASTFKALIA AALLDATTPA QLDRVVRYTR
ADLLAHAPVT REHVGTGMSL RDLADAAVRY SDNTAANLIL AELGGPAGLA RHLRALGDRT
TKPVRTEPAL NEATPGDERD TSTPRALATD LRAYVLGDAL DAGDRALLTD WLRRNTTGDA
LIRAGVPAGW TVGDKTGTAA YGTRNDIAVL WPPEGAPIVL AVLSSRAAED AEHDDALIAE
ATRVTLDALG R
//
