ID A0A1H0Z1T4_9ACTN Unreviewed; 321 AA.
AC A0A1H0Z1T4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=SAMN05428996_1119 {ECO:0000313|EMBL:SDQ21467.1};
OS Quadrisphaera sp. DSM 44207.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Quadrisphaera.
OX NCBI_TaxID=1881057 {ECO:0000313|EMBL:SDQ21467.1, ECO:0000313|Proteomes:UP000199015};
RN [1] {ECO:0000313|EMBL:SDQ21467.1, ECO:0000313|Proteomes:UP000199015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44207 {ECO:0000313|EMBL:SDQ21467.1,
RC ECO:0000313|Proteomes:UP000199015};
RA de Groot N.N.;
RL Submitted (OCT-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNKA01000001; SDQ21467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0Z1T4; -.
DR STRING; 1881057.SAMN05428996_1119; -.
DR Proteomes; UP000199015; 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 Reference proteome {ECO:0000313|Proteomes:UP000199015};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..321
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039054221"
FT DOMAIN 79..293
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 34..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 321 AA; 32817 MW; 042F208930CEB744 CRC64;
MTTTHPPPTS RPGRAARAGV AAVLALIPLT GCSATGQPAD PPAATASSSA APSAPSSAPA
SAAQAAFAQL EADHDARLGV YALDTGSGRS VEHRADERFA HASTYKALAA AAVLERTSSA
DLERVVPVTD ADLVTHSPIA EQRAGTGMTL REVADAAIRY SDNTAGNLLL RELGGPDGFE
RSLRSLGDAV TDPERLETDL NEAVPGDVRD TSTPRALATD LHAYAVGDAL PEDDRALLTG
WLRENTTGDA LVRAGAPAGW VVGDKTGAGG YGTRNDIAVL WPPSGDPVVL AVLSSRDEPD
ADHDDALVAD ATRVALAALT G
//
