ID A0A1H8PQJ4_9ACTN Unreviewed; 326 AA.
AC A0A1H8PQJ4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05216267_1026106 {ECO:0000313|EMBL:SEO44230.1};
OS Actinacidiphila rubida.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310780 {ECO:0000313|EMBL:SEO44230.1, ECO:0000313|Proteomes:UP000181951};
RN [1] {ECO:0000313|EMBL:SEO44230.1, ECO:0000313|Proteomes:UP000181951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2026 {ECO:0000313|EMBL:SEO44230.1,
RC ECO:0000313|Proteomes:UP000181951};
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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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; FODD01000026; SEO44230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8PQJ4; -.
DR STRING; 310780.SAMN05216267_1026106; -.
DR Proteomes; UP000181951; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000181951};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..326
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039660964"
FT DOMAIN 81..296
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 27..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 326 AA; 33336 MW; BB18CB77B1B9B272 CRC64;
MLRRTRAGAT AAGVALALGA LSGCGGGPGT AGRAPGAGEE TATATGSAAP GSASASASAS
SSPSTDHAFR ELEQRFHAHL GLFVLDTGSG RSVTYGADRR FAMCSTAKVL AAGALLRQDD
DADLARTLTY SRSDLLDHAP ITSQHVDHGM PLRDVIAAAL QHSDNTAENL MLRELGGPAG
LQRAVTALGD TTTHVNRTEP ALNEATPGDP RDTSTARALA ADLRTLLLGT ALPAAHRARL
TDWMLRNTTG GPYVRAALPK GWKAADKTGS GGHGTRNDIA VAWPPAGAPI LVSVLTDRDD
PAAASDDALI ATSVRTALTA LHRVTP
//
