ID A0A163YVQ1_9BRAD Unreviewed; 289 AA.
AC A0A163YVQ1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=A4A58_28895 {ECO:0000313|EMBL:KZD22634.1};
OS Tardiphaga robiniae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Tardiphaga.
OX NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD22634.1, ECO:0000313|Proteomes:UP000076574};
RN [1] {ECO:0000313|EMBL:KZD22634.1, ECO:0000313|Proteomes:UP000076574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vaf07 {ECO:0000313|EMBL:KZD22634.1,
RC ECO:0000313|Proteomes:UP000076574};
RA Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT "Microsymbionts genomes from the relict species Vavilovia formosa (Stev.)
RT Fed.";
RL Submitted (MAR-2016) 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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, 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:KZD22634.1}.
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DR EMBL; LVYV01000018; KZD22634.1; -; Genomic_DNA.
DR RefSeq; WP_068734275.1; NZ_LVYV01000018.1.
DR AlphaFoldDB; A0A163YVQ1; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000076574; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000076574};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..289
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007848012"
FT DOMAIN 45..263
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 165..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 289 AA; 30883 MW; 3921E1B900BDB545 CRC64;
MMINRRTLLA AAPALMAWPA FAKEAAKDAP AALQAYERDT GGRIGVYAEN LKTGAKIAWR
ANERFVMCST FKASLAACVL ARIDRGEDKP DQMISYAAAD LLDYAPVARD NLAKGALSVA
DMCKAIVELS DNTCANMLLA RVGGPAALTA FWNRTGDSVS RLDHNEPLLN RSRPGNPQDT
TTPAAMAGNV KRFVTGDVLT SASRNQLTDW MVNCKTGDKR LRAGLPKTWK IGDKTGNNGK
DAAGDIAVTW PKPDQPVVIA AYTQGGAPTA PQFETVFKAI GEMVGQRLG
//
