ID B9EC94_MACCJ Unreviewed; 281 AA.
AC B9EC94;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN Name=blaZm {ECO:0000313|EMBL:BAH18702.1};
GN OrderedLocusNames=MCCL_plsB0024 {ECO:0000313|EMBL:BAH18702.1};
OS Macrococcus caseolyticus (strain JCSC5402).
OG Plasmid pMCCL2 {ECO:0000313|EMBL:BAH18702.1,
OG ECO:0000313|Proteomes:UP000001383}.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=458233 {ECO:0000313|EMBL:BAH18702.1, ECO:0000313|Proteomes:UP000001383};
RN [1] {ECO:0000313|EMBL:BAH18702.1, ECO:0000313|Proteomes:UP000001383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC5402 {ECO:0000313|EMBL:BAH18702.1,
RC ECO:0000313|Proteomes:UP000001383};
RC PLASMID=pMCCL2 {ECO:0000313|EMBL:BAH18702.1,
RC ECO:0000313|Proteomes:UP000001383};
RX PubMed=19074389; DOI=10.1128/JB.01058-08;
RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL J. Bacteriol. 191:1180-1190(2009).
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; AP009486; BAH18702.1; -; Genomic_DNA.
DR AlphaFoldDB; B9EC94; -.
DR MEROPS; S11.A01; -.
DR KEGG; mcl:MCCL_plsB0024; -.
DR HOGENOM; CLU_031960_6_1_9; -.
DR Proteomes; UP000001383; Plasmid pMCCL2.
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 Plasmid {ECO:0000313|EMBL:BAH18702.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001383}.
FT DOMAIN 38..255
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 281 AA; 31600 MW; 00C40709DE75B50C CRC64;
MLIIALIFLS GCNSNNINSS KIKEDIKVIE NKYNIQAGVY VNDLTDKQKL SYNEELLFPY
ASTFKVINSA LLIEKLGMNN LDKEVKVSER DIVLYSPIIE KYKNKNVSLK MLIEAALLYS
DNTANNLIIE ELGGLKEVEK RLSALGIKGV NVNRKEVALN FYDPKKNEDT ISAKNMSKAL
IKMLTGDVLE YKEQIFLIDL MKKNKTGTTL IKKGMDKKFI VGDKSGQGAN YGVRNDIAVV
YKKQSNKPII VVVFTKAKNE KQKPSDTPIV EISKVINKNI K
//
