ID A0A0T6UT53_9PSED Unreviewed; 260 AA.
AC A0A0T6UT53;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN ORFNames=AO726_07195 {ECO:0000313|EMBL:KRW61114.1};
OS Pseudomonas sp. TTU2014-080ASC.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1729724 {ECO:0000313|EMBL:KRW61114.1, ECO:0000313|Proteomes:UP000051864};
RN [1] {ECO:0000313|EMBL:KRW61114.1, ECO:0000313|Proteomes:UP000051864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTU2014-080ASC {ECO:0000313|EMBL:KRW61114.1,
RC ECO:0000313|Proteomes:UP000051864};
RA Webb H.E., Bugarel M., Den Bakker H.C., Nightingale K., Granier S.A.,
RA Loneragan G.H.;
RT "Carbapenem-non-susceptible Bacteria Recovered from the Faeces of Dairy
RT Cattle.";
RL Submitted (SEP-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|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007898, ECO:0000256|RuleBase:RU361140}.
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:KRW61114.1}.
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DR EMBL; LKKK01000002; KRW61114.1; -; Genomic_DNA.
DR RefSeq; WP_058067392.1; NZ_LKKK01000002.1.
DR AlphaFoldDB; A0A0T6UT53; -.
DR STRING; 1729724.AO726_07195; -.
DR OrthoDB; 9762883at2; -.
DR Proteomes; UP000051864; Unassembled WGS sequence.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR002137; Beta-lactam_class-D_AS.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00337; BETA_LACTAMASE_D; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Reference proteome {ECO:0000313|Proteomes:UP000051864};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..260
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006673071"
FT DOMAIN 54..244
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 66
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
FT MOD_RES 69
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
SQ SEQUENCE 260 AA; 29159 MW; 3B29C5C1DADE2A74 CRC64;
MKRLLLATLL MLAAQVHAQE WLENPAVGAL FKQAGVDGTF VLHEVGSDQL QGYNQTRAQT
RFYPASTFKI PNSLIGIGTG AVSSVDEVFP WDGKPKYLKS WEHDMSLREA FKVSNYPVYQ
VLARRVGLKR MQDQVVALNY GNAEVGDQVD TFWLDGPLMI SAIEQTEFLE RLVQDKLPFS
SQVQASVREI SLLEEGPNWR LYAKTGWSTA SKPGIGWWVG WVEQDGRYYT FALNMPMVDI
KDAGKRIELG KASLKSLGLL
//
