ID A0A126R543_9SPHN Unreviewed; 323 AA.
AC A0A126R543;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=K663_03685 {ECO:0000313|EMBL:AMK17124.1};
OS Sphingobium sp. MI1205.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=407020 {ECO:0000313|EMBL:AMK17124.1, ECO:0000313|Proteomes:UP000060707};
RN [1] {ECO:0000313|Proteomes:UP000060707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI1205 {ECO:0000313|Proteomes:UP000060707};
RA Tabata M.;
RT "Genome sequence of gamma-HCH degrading bacterium Sphingobium sp. MI1205.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMK17124.1, ECO:0000313|Proteomes:UP000060707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI1205 {ECO:0000313|EMBL:AMK17124.1,
RC ECO:0000313|Proteomes:UP000060707};
RX PubMed=27056230;
RA Tabata M., Ohhata S., Nikawadori Y., Sato T., Kishida K., Ohtsubo Y.,
RA Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of a gamma-Hexachlorocyclohexane-Degrading
RT Bacterium, Sphingobium sp. Strain MI1205.";
RL Genome Announc. 4:0-0(2016).
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 -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009}.
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; CP005188; AMK17124.1; -; Genomic_DNA.
DR RefSeq; WP_062114229.1; NZ_CP005188.1.
DR AlphaFoldDB; A0A126R543; -.
DR STRING; 407020.K663_03685; -.
DR KEGG; spmi:K663_03685; -.
DR PATRIC; fig|407020.3.peg.775; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000060707; Chromosome 1.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 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.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..323
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007273114"
FT DOMAIN 58..289
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 323 AA; 34322 MW; 53F303A7B9A71950 CRC64;
MPRRFSVAAL LAGFGLFLAP LPAADAFGPK PDMVQQTAQS RLLGEFARFA TLSDGTVGIA
VRDLHNGETL QYNGDTLFPM ASIYKVAVAG KILSLADAGT LRLDEKLPRL GTPLSVTTLL
DLMLTRSDNE ATDTLVARAG GPQAVHGWLK SIGIRGQRVD SNTAQLLARA KADFGAAGDE
AESVLSSRQR DARDLPNMAF AADPRDTSTP RAMNDLLSAI HHGKALKGSS TAMLLGIMSR
CKTGKARLVG MLPPGTPIAH KTGTLNGLGN DTGIITLPDG RRIAISVFVM KDHRGHAARD
RIMAEVARAA YDYFLFAPDL HTA
//