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Database: UniProt
Entry: A0A0P0SIV5_9PSEU
LinkDB: A0A0P0SIV5_9PSEU
Original site: A0A0P0SIV5_9PSEU 
ID   A0A0P0SIV5_9PSEU        Unreviewed;       366 AA.
AC   A0A0P0SIV5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-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=AD017_11055 {ECO:0000313|EMBL:ALL84517.1};
OS   Pseudonocardia sp. EC080619-01.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL84517.1, ECO:0000313|Proteomes:UP000066228};
RN   [1] {ECO:0000313|EMBL:ALL84517.1, ECO:0000313|Proteomes:UP000066228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL84517.1,
RC   ECO:0000313|Proteomes:UP000066228};
RX   PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA   Van Arnam E.B., Sit C.S.;
RT   "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL   J. Am. Chem. Soc. 137:14272-14274(2015).
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; CP012184; ALL84517.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P0SIV5; -.
DR   STRING; 1096856.AD017_11055; -.
DR   KEGG; pecq:AD017_11055; -.
DR   PATRIC; fig|1096856.3.peg.2322; -.
DR   Proteomes; UP000066228; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000066228};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..366
FT                   /note="beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038707210"
FT   DOMAIN          55..186
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   366 AA;  38461 MW;  DB29E7E25BE3C0C0 CRC64;
     MSVLLPVVCA LLAAGCSAAP ARSSDGPCPP VESDVGTVDG WLGYVAAHPE DVALVADDGR
     GTSLVHRSEA VHPMASASKA LNTVAYARAV ARGVVSPDEP VRVGDWERWA VRGSGEDAHA
     MALDHVGIPR QGFWARDPDQ TVTLDQVVEQ MMIWSDNAAP DFLRDRLGDR ALTDAAEAVG
     WRDGELPSTT GLTVLFFAPE LMPSSTDRAA RRAVEWQLAR RYASEPAFRA DVDSRPVPAG
     VDEPAFVDGG PGGTAGQLAA LWSAVGHGTF EGADIARRLT EQDPDPGPGL IGVGVKGGST
     PGVLARGTEV RRDDGTVGVA VLLVRRRSPE DTAAVARSSQ AFGDVVQAMA QDPALLEQLR
     CRLPQT
//
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