ID A0A171C1Q9_9ACTN Unreviewed; 319 AA.
AC A0A171C1Q9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=PS9374_01604 {ECO:0000313|EMBL:GAT65960.1};
OS Planomonospora sphaerica.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Planomonospora.
OX NCBI_TaxID=161355 {ECO:0000313|EMBL:GAT65960.1, ECO:0000313|Proteomes:UP000077701};
RN [1] {ECO:0000313|EMBL:GAT65960.1, ECO:0000313|Proteomes:UP000077701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9374 {ECO:0000313|EMBL:GAT65960.1,
RC ECO:0000313|Proteomes:UP000077701};
RA Dohra H., Suzuki T., Inoue Y., Kodani S.;
RT "Draft Genome Sequence of Planomonospora sphaerica JCM9374, a Rare
RT Actinomycete.";
RL Genome Announc. 4:e00779-16(2016).
RN [2] {ECO:0000313|Proteomes:UP000077701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9374 {ECO:0000313|Proteomes:UP000077701};
RA Suzuki T., Dohra H., Kodani S.;
RT "Planomonospora sphaerica JCM9374 whole genome shotgun sequence.";
RL Submitted (APR-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 -!- 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:GAT65960.1}.
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DR EMBL; BDCX01000003; GAT65960.1; -; Genomic_DNA.
DR RefSeq; WP_068895763.1; NZ_BDCX01000003.1.
DR AlphaFoldDB; A0A171C1Q9; -.
DR STRING; 161355.PS9374_01604; -.
DR OrthoDB; 503335at2; -.
DR Proteomes; UP000077701; 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 Hydrolase {ECO:0000313|EMBL:GAT65960.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077701};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..319
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007905519"
FT DOMAIN 52..168
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 319 AA; 33629 MW; F377D51552FFF595 CRC64;
MNAILSISLA TALVATPTAP AAAPAPADLK DAEAVLAHIA AHPGDVALVT RGISHNAGRL
APVASTIKIV HLAAYADAVR RGRAAPGDRV PVALWNAYHV PGTDGGAHEA ALKRLAPGAS
VTLDQLVSAM IEESDNAAAD LLRDRLGPGE LRKIARTGVG TINGEILRAF GGCTLPADAC
LKRYVKAGKQ VTPALPDFAR QAAWAATVTR VEPGVLRRVL AGLRKDPVAS RHLEWPMRLP
GADPAELRIG TKGGALPGVI SEAMYTARPG ERPRETVLVL HRLPETTWFS GMRSYAHQDF
IRKLATEPAF FAKVRAALK
//
