ID H8LLW2_RICSL Unreviewed; 90 AA.
AC H8LLW2;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 ORFNames=MC3_06895 {ECO:0000313|EMBL:AFD20228.1};
OS Rickettsia slovaca str. D-CWPP.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=1105109 {ECO:0000313|EMBL:AFD20228.1, ECO:0000313|Proteomes:UP000007592};
RN [1] {ECO:0000313|EMBL:AFD20228.1, ECO:0000313|Proteomes:UP000007592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D-CWPP (RSB) {ECO:0000313|Proteomes:UP000007592};
RA Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.;
RL Submitted (MAR-2012) 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-D beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007898, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; CP003375; AFD20228.1; -; Genomic_DNA.
DR RefSeq; WP_014419951.1; NC_017065.1.
DR AlphaFoldDB; H8LLW2; -.
DR KEGG; rsw:MC3_06895; -.
DR PATRIC; fig|1105109.3.peg.1454; -.
DR HOGENOM; CLU_2438870_0_0_5; -.
DR Proteomes; UP000007592; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 8..89
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 18
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
FT MOD_RES 21
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
SQ SEQUENCE 90 AA; 10595 MW; 0E6958BC6BFE6D7D CRC64;
MKIIKQEGNC ESRYVPCSTF KIAISLMGYD DGFLIDETHP KLPVKEGYAD YLEVWKQSQT
PKDWMKNSCV WYSQIITKEL GMEKFRDYVT
//
