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Database: UniProt
Entry: E5AX58_RHIRD
LinkDB: E5AX58_RHIRD
Original site: E5AX58_RHIRD 
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
//
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