ID A0A0C1FUC2_9SPHI Unreviewed; 415 AA.
AC A0A0C1FUC2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=OC25_21605 {ECO:0000313|EMBL:KIA91474.1};
OS Pedobacter kyungheensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1069985 {ECO:0000313|EMBL:KIA91474.1, ECO:0000313|Proteomes:UP000031246};
RN [1] {ECO:0000313|EMBL:KIA91474.1, ECO:0000313|Proteomes:UP000031246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 16221 {ECO:0000313|EMBL:KIA91474.1,
RC ECO:0000313|Proteomes:UP000031246};
RA Anderson B.M., Newman J.D.;
RT "Pedobacter Kyungheensis.";
RL Submitted (OCT-2014) 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:KIA91474.1}.
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DR EMBL; JSYN01000029; KIA91474.1; -; Genomic_DNA.
DR RefSeq; WP_039480419.1; NZ_JSYN01000029.1.
DR AlphaFoldDB; A0A0C1FUC2; -.
DR OrthoDB; 1884322at2; -.
DR Proteomes; UP000031246; 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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..415
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002150218"
FT DOMAIN 71..291
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 415 AA; 47521 MW; A9E55C7A51F581CA CRC64;
MRKFLTLACS LISLSAMAQK TDTVFLKKLM ESKPGLFSSV LNHPNKNQIQ ILYTQVNRNT
QNKPSFKTFS YNLDPHHYFY PASTVKLAAV IFALEKVNRL KNTGLTASST MITDSAFNGQ
SKVLTDTSAK NGLPSIAHYV KKILLTSDND AFNRLFEFIG RAEINQQLKA NGFNDSRILN
RLAIGDAGES ARHSNPIKFY NGDKLVYNQP AQYDPKDYDL TLSNLTMGKG YLDSADKLVN
KPFSLAGKNA FAINDQQKLM QKLIFPEAFP AKERFKLTAA DYKLIYTYMS KYPTESDFPK
YDPKEFWPTY AKMLYYGREN VSPDPNIRIF NKYGDSYGYI IDNSYFVDFK NGIEYFLTAV
VHSNEDGIFN DNKYEYDTVC FPFMKNLGQS IYEVELNRKK SHQPDLSKFK LDYSH
//
