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Database: UniProt
Entry: A0A023X6K6_9ACTN
LinkDB: A0A023X6K6_9ACTN
Original site: A0A023X6K6_9ACTN 
ID   A0A023X6K6_9ACTN        Unreviewed;       344 AA.
AC   A0A023X6K6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=RradSPS_2347 {ECO:0000313|EMBL:AHY47630.1};
OS   Rubrobacter radiotolerans.
OC   Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=42256 {ECO:0000313|EMBL:AHY47630.1, ECO:0000313|Proteomes:UP000025229};
RN   [1] {ECO:0000313|EMBL:AHY47630.1, ECO:0000313|Proteomes:UP000025229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSPS-4 {ECO:0000313|EMBL:AHY47630.1,
RC   ECO:0000313|Proteomes:UP000025229};
RA   Egas C.C., Barroso C.C., Froufe H.J.C., Pacheco J.J., Albuquerque L.L.,
RA   da Costa M.M.S.;
RT   "Complete genome sequence of the Radio-Resistant Rubrobacter radiotolerans
RT   RSPS-4.";
RL   Submitted (MAR-2014) 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   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00009009}.
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DR   EMBL; CP007514; AHY47630.1; -; Genomic_DNA.
DR   RefSeq; WP_038682898.1; NZ_CP007514.1.
DR   AlphaFoldDB; A0A023X6K6; -.
DR   STRING; 42256.RradSPS_2347; -.
DR   KEGG; rrd:RradSPS_2347; -.
DR   eggNOG; COG2367; Bacteria.
DR   HOGENOM; CLU_806286_0_0_11; -.
DR   OrthoDB; 33989at2; -.
DR   Proteomes; UP000025229; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
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; 2.
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   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000025229};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        53..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          117..319
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  37973 MW;  FC663AE10361A6CA CRC64;
     MENEEKDTAP AADRVALSGE PGRGPVVRER RYRRKVHAGL VRLRRRRLRQ RRFVLSLFVA
     VCALVGLWAA EELRPEPAAV ERAVAPVTGE RLVPPAPDGD LEARIRAIAE IYPGEFGVVV
     RDPRTGETAG LNPDQTFTAA SLAKLPVLLA LYGEAADGRL DLEEKIVMEA QDVQLYGAGV
     LQNYPVGHEM TLRECAELLI KESDNTAWVM LERRLGRERI EHEIESLKLS GTDYAALTTT
     PEDVLRMLEA IADPDHTTPE LSAEMLAHMT DTAYEGRIPE PLPKDVRVAH KVGTLNDTRS
     DAAIVFRQPG DRVDYMIVVI ASGGTERSAT DAIRRISLSA YEAL
//
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