ID B1LXB8_METRJ Unreviewed; 315 AA.
AC B1LXB8;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
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};
GN OrderedLocusNames=Mrad2831_5292 {ECO:0000313|EMBL:ACB27239.1};
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB27239.1, ECO:0000313|Proteomes:UP000006589};
RN [1] {ECO:0000313|EMBL:ACB27239.1, ECO:0000313|Proteomes:UP000006589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC 0-1 {ECO:0000313|Proteomes:UP000006589};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-2008) 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; CP001001; ACB27239.1; -; Genomic_DNA.
DR AlphaFoldDB; B1LXB8; -.
DR STRING; 426355.Mrad2831_5292; -.
DR MEROPS; S12.006; -.
DR KEGG; mrd:Mrad2831_5292; -.
DR PATRIC; fig|426355.14.peg.5348; -.
DR eggNOG; COG1680; Bacteria.
DR HOGENOM; CLU_020027_10_0_5; -.
DR OrthoDB; 5377431at2; -.
DR Proteomes; UP000006589; Chromosome.
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 1..302
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 315 AA; 33919 MW; F643C31874D73275 CRC64;
MDESTLFEIG SISKTITVAL AAYAAETGAL RWDAAPGRYI TELKASALDR VSLLNLATHT
TGGMPLQLSD DVKIDADLIA YFRKWTPPSP PGSVRTYANP SIGLLGLVTA RAMKGQFAVL
VREHVTRPLG LQRTFHDVPK AEQPHYAQGY TRDGKPVRVS MAPLATEAYG LRTTARDLLR
FVEAQLGLID VSPTLQRALS ATQVGRFLAG PMTQALIWEW YPLPVSDDDL AVGNGDAMVL
KPTPVTRLDP PRAPPADSLV TKTGATNGFG AYVAFIPGRK IGLVLMANRN HPTAVRLTLA
KQVFTALNVQ GIPAQ
//
