ID Q1RKC6_RICBR Unreviewed; 266 AA.
AC Q1RKC6;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN Name=blaD {ECO:0000313|EMBL:ABE04188.1};
GN OrderedLocusNames=RBE_0107 {ECO:0000313|EMBL:ABE04188.1};
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407 {ECO:0000313|EMBL:ABE04188.1, ECO:0000313|Proteomes:UP000001951};
RN [1] {ECO:0000313|EMBL:ABE04188.1, ECO:0000313|Proteomes:UP000001951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C {ECO:0000313|EMBL:ABE04188.1,
RC ECO:0000313|Proteomes:UP000001951};
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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-D beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007898, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; CP000087; ABE04188.1; -; Genomic_DNA.
DR RefSeq; WP_011476803.1; NC_007940.1.
DR AlphaFoldDB; Q1RKC6; -.
DR KEGG; rbe:RBE_0107; -.
DR eggNOG; COG2602; Bacteria.
DR HOGENOM; CLU_035412_2_0_5; -.
DR OrthoDB; 9762883at2; -.
DR Proteomes; UP000001951; Chromosome.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
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; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR002137; Beta-lactam_class-D_AS.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627:SF6; BETA-LACTAMASE YBXI-RELATED; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00337; BETA_LACTAMASE_D; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Reference proteome {ECO:0000313|Proteomes:UP000001951};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..266
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004196971"
FT DOMAIN 38..253
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 48
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
FT MOD_RES 51
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
SQ SEQUENCE 266 AA; 30864 MW; 17CE2E0F5E190AC0 CRC64;
MKKITLYLTA LISFTVSFAI KADCFLVKEN DKVIKQDGDC KSRYAPCSTF KIVLSLMGYD
DGFLIDETHP KLPFKKGYDD YLEVWKQPHT PKDWMKNSCL WYSRLITKEL GYEKFHNYVT
KFNYGNQDTS GDKGKNNGLT NAWLSSSLEI SPEEQIAFLQ KLAADQLPVS LKAQEMTKNI
MFIEDFADGW KLYAKTGSGN RLNEDRTIKL KDCQIGWFIG WLQKDNRKVF FVHFIEDKEH
HDSYASFRSR EAAKEKLKGL ISKELK
//
