ID A0A109QWV6_9MICO Unreviewed; 270 AA.
AC A0A109QWV6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=AWU67_08275 {ECO:0000313|EMBL:AMB58864.1};
OS Microterricola viridarii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microterricola.
OX NCBI_TaxID=412690 {ECO:0000313|EMBL:AMB58864.1, ECO:0000313|Proteomes:UP000058305};
RN [1] {ECO:0000313|EMBL:AMB58864.1, ECO:0000313|Proteomes:UP000058305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS5:02 {ECO:0000313|EMBL:AMB58864.1,
RC ECO:0000313|Proteomes:UP000058305};
RX PubMed=26854947; DOI=10.1016/j.jbiotec.2016.02.011;
RA Himanshu, Swarnkar M.K., Singh D., Kumar R.;
RT "First complete genome sequence of a species in the genus Microterricola,
RT an extremophilic cold active enzyme producing bacterial strain ERGS5:02
RT isolated from Sikkim Himalaya.";
RL J. Biotechnol. 222:17-18(2016).
RN [2] {ECO:0000313|Proteomes:UP000058305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS5:02 {ECO:0000313|Proteomes:UP000058305};
RA Kumar R., Singh D., Swarnkar M.K.;
RT "First complete genome sequence of a species in the genus Microterricola,
RT an extremophilic cold active enzyme producing strain ERGS5:02 isolated from
RT Sikkim Himalaya.";
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}.
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DR EMBL; CP014145; AMB58864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109QWV6; -.
DR KEGG; mvd:AWU67_08275; -.
DR OrthoDB; 3673924at2; -.
DR Proteomes; UP000058305; 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 Hydrolase {ECO:0000313|EMBL:AMB58864.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000058305}.
FT DOMAIN 17..240
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 270 AA; 29761 MW; 346BC205919FD8B3 CRC64;
MTQMTPRFYS EHDTQWSVLA VDIDSGEELV RLDAERVLDT ASVGKIFLLH RLLSEADAGT
RSLEEQVTRR PVEWMDNSGL WYLLQADTLS LYDAAALVGA VSDNAATNTL CRVIGLPVVQ
EHTRALGYTE SALDDVVRWP LPPGAPRTLS HANAEELVRF VQRTARAEDL SPASADTLQR
WLGAGMDLSM TASAFGLDPL AHYYFDRDIW LWNKTGTIST VRADVGLVMS GERRIAYAVL
ANWRSGADAR DGVLASMREV GEVIRAALRG
//