ID E5AX58_RHIRD Unreviewed; 317 AA.
AC E5AX58;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 03-MAY-2023, entry version 27.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE Flags: Fragment;
GN Name=ampC {ECO:0000313|EMBL:CBX26001.1};
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358 {ECO:0000313|EMBL:CBX26001.1};
RN [1] {ECO:0000313|EMBL:CBX26001.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CFBP 7064 {ECO:0000313|EMBL:CBX26001.1};
RA Costechareyre D., Bahena-Ramirez M., Muller D., D'Angelo-Picard C.,
RA Nesme J., Bertolla F., Daubin V., Nesme X.;
RT "Circular and linear chromosome multilocus analysis of the Agrobacterium
RT tumefaciens / biovar 1 species complex.";
RL Submitted (OCT-2010) 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-C beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007840, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; FR695087; CBX26001.1; -; Genomic_DNA.
DR AlphaFoldDB; E5AX58; -.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001586; Beta-lactam_class-C_AS.
DR PANTHER; PTHR46825:SF8; BETA-LACTAMASE-RELATED; 1.
DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00336; BETA_LACTAMASE_C; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 15..271
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CBX26001.1"
FT NON_TER 317
FT /evidence="ECO:0000313|EMBL:CBX26001.1"
SQ SEQUENCE 317 AA; 34092 MW; 761DBF9236E6AC1A CRC64;
QTFAADDARL KAITDAAIKP VMEKNGIPGL AVGISVDGEN HVFTYGVMSK TTGQPVTPQT
LFELGSISKT FTVTLSTYAE THGKLSLSGK VEDYLPSMKG KPFGDVTLMH LGTHTAGGFP
LQVPDNVKTE PQLLAYLKAW KPAYKAGTHR TYANPSIGML GYVTAKAMGQ SYDSAMQDVL
FPALGLKSTF TVVPKAKMAD YAQGYKRTGE PARMTPAILS SEAYGVRSTA TDMIRFVNAN
MGLEKLDGKL QQAIANTHTG YFSVGAMTQD MIWEQYAHPA ALKTLIETNS GALLKTVPVS
EISPPMKPRG DVFINKT
//