ID A0A1Q4EZK9_9SPHI Unreviewed; 400 AA.
AC A0A1Q4EZK9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=BGP14_07765 {ECO:0000313|EMBL:OJY81239.1};
OS Sphingobacteriales bacterium 44-15.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895837 {ECO:0000313|EMBL:OJY81239.1, ECO:0000313|Proteomes:UP000186250};
RN [1] {ECO:0000313|EMBL:OJY81239.1, ECO:0000313|Proteomes:UP000186250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44-15 {ECO:0000313|EMBL:OJY81239.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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:OJY81239.1}.
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DR EMBL; MKWG01000045; OJY81239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4EZK9; -.
DR STRING; 1895837.BGP14_07765; -.
DR Proteomes; UP000186250; 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}.
FT DOMAIN 58..333
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 400 AA; 47441 MW; A22971BEADA1D2D3 CRC64;
MAHAQDRTDQ WLEDLLRAKA SPLLKMILNN PDSFHYQLIY TKIDRDKHNI PSFHHYYLHV
DREQYFNPAS TVKMPLAFLA LEKLHKINVP GVDKFTTMLT DSGYNGQTTV LYDSSAENNM
PSVAQYIRKI FLVSDNDAYN RLYEFIGQQA INERLWQMGY KDIRITRRFV RATEEENRHT
NPERFVDNDG KVLYSQPAAY SDLQFDFSKK VLIGNAHYDR DENLVQAPMD FTTHNNAPLE
DLQQIMQSVL FPEQASSRQR FKLTGDDYRF LYRYMSELPC ESAYPKYDTT EFFDSYTKFF
LFKAGKQKIP EYIRVFNKTG WSYGFLTDIA YIVDFKHNVE FMLTGNIYVN RDGVLNDDKY
EYEELGYPFF KEVGNIIYDY ELKRKRAHRP DLGKFKTEYR
//
