ID A0A1H1ZTI9_9ACTN Unreviewed; 332 AA.
AC A0A1H1ZTI9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
DE AltName: Full=Penicillinase {ECO:0000256|ARBA:ARBA00030171};
GN ORFNames=SAMN04489716_3495 {ECO:0000313|EMBL:SDT37141.1};
OS Actinoplanes derwentensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=113562 {ECO:0000313|EMBL:SDT37141.1, ECO:0000313|Proteomes:UP000198688};
RN [1] {ECO:0000313|EMBL:SDT37141.1, ECO:0000313|Proteomes:UP000198688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43941 {ECO:0000313|EMBL:SDT37141.1,
RC ECO:0000313|Proteomes:UP000198688};
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}.
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DR EMBL; LT629758; SDT37141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1ZTI9; -.
DR STRING; 113562.SAMN04489716_3495; -.
DR Proteomes; UP000198688; Chromosome i.
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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Reference proteome {ECO:0000313|Proteomes:UP000198688};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..332
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009268069"
FT DOMAIN 70..271
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 311..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 35442 MW; B98FAEFADD8ECE40 CRC64;
MSRRAALGIG AAAAVAGAGV SSPAQAALSG PAAIRKVYNK EKVKAGGVWH THIAAIDATG
TIAPIIEDDA DHVTYGYSVQ KLFVATAVMD KIDRGELTLG TKLDLTAGII LGGSGIYHLH
RVWGDDITVA NFLTAMLLVS DNTAVRMCGR VVPALELNEI LAAKGFVHTR VEPVANPNRF
FLGTTTPRET HDMLWRLANK TLLSPESCDF LLSITRWLNG YHDGVRRVMS SKERERVATK
YGADFNTLGE SRHEAGIMFS ADGLPLLTYA MFAEGLGEPL NYGATHPAVE AHAKIGRTLF
DNLPAVPATL STARTSSVPR TLPKPFSPVN GG
//
