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Database: UniProt
Entry: A0A0Q0XX06_9FLAO
LinkDB: A0A0Q0XX06_9FLAO
Original site: A0A0Q0XX06_9FLAO 
ID   A0A0Q0XX06_9FLAO        Unreviewed;       317 AA.
AC   A0A0Q0XX06;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=AAU57_04300 {ECO:0000313|EMBL:KQC34505.1};
OS   Nonlabens sp. YIK11.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Nonlabens.
OX   NCBI_TaxID=1453349 {ECO:0000313|EMBL:KQC34505.1, ECO:0000313|Proteomes:UP000051409};
RN   [1] {ECO:0000313|EMBL:KQC34505.1, ECO:0000313|Proteomes:UP000051409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIK11 {ECO:0000313|EMBL:KQC34505.1,
RC   ECO:0000313|Proteomes:UP000051409};
RA   Kwon Y.M., Kim S.-J.;
RT   "Complete genome of flavobacterium.";
RL   Submitted (APR-2015) 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:KQC34505.1}.
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DR   EMBL; LBMJ01000001; KQC34505.1; -; Genomic_DNA.
DR   RefSeq; WP_055413668.1; NZ_LBMJ01000001.1.
DR   AlphaFoldDB; A0A0Q0XX06; -.
DR   STRING; 1453349.AAU57_04300; -.
DR   PATRIC; fig|1453349.3.peg.895; -.
DR   Proteomes; UP000051409; 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; 2.
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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..317
FT                   /note="beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006186844"
FT   DOMAIN          69..117
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
FT   DOMAIN          119..274
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   317 AA;  35807 MW;  38BFFEA43BA2EA7B CRC64;
     MLNRILIFLF LAASWNMSAA DDDAPLVNLA LNNKDVKTFQ NTTLQLNLKA QLMANPDWRK
     LIQQKRMSVS LVDLNDAENI KYASINGSNM MYAASLPKIA VLYAAMDAIE NGELKDTPKV
     RDDMWLMISK SNNAASTRMI DRVGFQKIED LMCDPSNPFY DKDGVGGLWV GKRYAAQGKR
     NPEPIRGLSH AATTDAVAKF YYQLATGQLI NKTRSKEMLD IMENPSLHHK FVNTLDRIAP
     DARLFRKSGS WKNWHSDSIL VWGEDGRKYI LVALIEDPNG EQIIRNLVQP AELALRKSVI
     LPVELEQENE VVVRQDT
//
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