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Database: UniProt
Entry: A0A126R543_9SPHN
LinkDB: A0A126R543_9SPHN
Original site: A0A126R543_9SPHN 
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}.
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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
//
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