ID Q211J8_RHOPB Unreviewed; 272 AA.
AC Q211J8;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
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 OrderedLocusNames=RPC_3398 {ECO:0000313|EMBL:ABD88938.1};
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD88938.1};
RN [1] {ECO:0000313|EMBL:ABD88938.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD88938.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) 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; CP000301; ABD88938.1; -; Genomic_DNA.
DR AlphaFoldDB; Q211J8; -.
DR STRING; 316056.RPC_3398; -.
DR KEGG; rpc:RPC_3398; -.
DR eggNOG; COG2602; Bacteria.
DR HOGENOM; CLU_035412_3_2_5; -.
DR OrthoDB; 9762883at2; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
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 Hydrolase {ECO:0000256|RuleBase:RU361140, ECO:0000313|EMBL:ABD88938.1}.
FT DOMAIN 53..249
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 75
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
FT MOD_RES 78
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602137-50"
SQ SEQUENCE 272 AA; 29644 MW; BEE6D833D7B43BC9 CRC64;
MLNRRHAIGL FAATAVAPLS ARAEVAPPRS EIRVALAKRF ADVGTAGTFV GYKTEDYLII
ASDPDRSGQG FHPASTFKIA HSLIALETGV VADPDKDVFK WDGVTRDIEG WNRDHTLRSA
IAASAVPVYQ EIARRIGAER MQKHLDLFDY GNRNIGGGID QFWLTGELRI DPIQQIDFVD
RLRRGVLPIS ARSQDLVRDI LPVGKVGDAL IRAKTGLLGA EIGKPTLGWL VGWAEKGGAH
TVFALNLDIR EPRHVALRMA LAEQCLGDIG AI
//
