ID Q936V5_PROMI Unreviewed; 291 AA.
AC Q936V5;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 84.
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 Name=blaCTX-M-20 {ECO:0000313|EMBL:CAC95175.1};
OS Proteus mirabilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=584 {ECO:0000313|EMBL:CAC95175.1};
RN [1] {ECO:0000313|EMBL:CAC95175.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TLR {ECO:0000313|EMBL:CAC95175.1};
RA Arlet G.J.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAC95175.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TLR {ECO:0000313|EMBL:CAC95175.1};
RX PubMed=12007800;
RA Saladin M., Bao Cao V.T., Lambert T., Donay J.L., Herrmann J.L.,
RA Ould Hocine Z., Verdet C., Delisle F., Philippon A., Arlet G.;
RT "Diversity of CTX-M beta-lactamases and their promoter regions from
RT Enterobacteriaceae isolated in three Parisian hospitals.";
RL FEMS Microbiol. Lett. 209:161-168(2002).
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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ416344; CAC95175.1; -; Genomic_DNA.
DR RefSeq; WP_063860038.1; NG_048969.1.
DR AlphaFoldDB; Q936V5; -.
DR SMR; Q936V5; -.
DR KEGG; ag:CAC95175; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam 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; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR023650; Beta-lactam_class-A_AS.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..291
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004321581"
FT DOMAIN 50..264
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 291 AA; 31412 MW; 82277CD9C1B2E7C0 CRC64;
MMTQSIRRSM LTVMATLPLL FSSATLHAQA NSVQQQLEAL EKSSGGRLGV ALINTADNSQ
ILYRADERFA MCSTSKVMAA AAVLKQSESD KHLLNQRVEI KKSDLVNYNP IAEKHVNGTM
TLAELGAAAL QYSDNTAMNK LIAHLGGPDK VTAFARSLGD ETFRLDRTEP TLNTAIPGDP
RDTTTPLAMA QTLKNLTLGK ALAETQRAQL VTWLKGNTTG SASIRAGLPK SWVVGDKTGS
GDYGTTNDIA VIWPENHAPL VLVTYFTQPE QKAESRRDFL AAAAKIVTHG F
//
