ID A0A136PRA7_9ACTN Unreviewed; 342 AA.
AC A0A136PRA7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=AWW66_17345 {ECO:0000313|EMBL:KXK60716.1};
OS Micromonospora rosaria.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK60716.1, ECO:0000313|Proteomes:UP000070620};
RN [1] {ECO:0000313|EMBL:KXK60716.1, ECO:0000313|Proteomes:UP000070620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 803 {ECO:0000313|EMBL:KXK60716.1,
RC ECO:0000313|Proteomes:UP000070620};
RA Yang H., He X., Zhu D.;
RT "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT which can produce antibacterial substance rosamicin.";
RL Submitted (JAN-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:KXK60716.1}.
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DR EMBL; LRQV01000061; KXK60716.1; -; Genomic_DNA.
DR RefSeq; WP_067367225.1; NZ_LRQV01000061.1.
DR AlphaFoldDB; A0A136PRA7; -.
DR OrthoDB; 4515847at2; -.
DR Proteomes; UP000070620; 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 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:UP000070620};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..342
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007478262"
FT DOMAIN 85..287
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 342 AA; 36558 MW; B54C06AF547A0371 CRC64;
MPDKVSRRVA LGLGAATAAL VAAPRPALAA PAPGADPAAD HAPLDPTQRI RQAYRTRTRQ
AGGVWHSHVA RVDATGALRT VLADDADRVT HGYSVQKLAV AVAVLDAIDR GQLRLDQRLD
LTADIILGGS GLYHLQTVWG DEVTVANFLT AMLLVSDNTA VRMCGRVVPA LEINEILAAK
GFTHTRVEPV ANPYRFFLGV TTPRETHDLL WRLANGTLLS VGSTTFLLGV LRWINGYHDG
IRRDMSSAER SRVATKYGAD YDERGAARHE VGIVFDQTGA PALTYAFFAD TLGDRDNYGG
THPAVRAHAH LGRVLFDTVG AGTAPAGVSR HTVAPFRPVD GG
//
