ID   BLAC_RHOCA              Reviewed;         293 AA.
AC   P14171;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SP108;
RX   PubMed=2788410; DOI=10.1042/bj2600803;
RA   Campbell J.I.A., Scahill S., Gibson T., Ambler R.P.;
RT   "The phototrophic bacterium Rhodopseudomonas capsulata sp108 encodes an
RT   indigenous class A beta-lactamase.";
RL   Biochem. J. 260:803-812(1989).
CC   -!- FUNCTION: Hydrolyzes beta-lactams antibiotics. Rates of hydrolysis
CC       relative to benzylpenicillin =100: ampicillin = 27, carbenicillin = 25,
CC       cloxacillin = 0, cephaloridine = 4.
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10101};
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; X15791; CAA33795.1; -; Genomic_DNA.
DR   PIR; S04649; S04649.
DR   RefSeq; WP_028030786.1; NZ_SWJZ01000009.1.
DR   AlphaFoldDB; P14171; -.
DR   SMR; P14171; -.
DR   OrthoDB; 9784149at2; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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   InterPro; IPR023650; Beta-lactam_class-A_AS.
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.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Periplasm; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..293
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000017009"
FT   ACT_SITE        74
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         238..240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  31296 MW;  60925BBE658917F1 CRC64;
     MRFTATVLSR VATGLALGLS MATASLAETP VEALSETVAR IEEQLGARVG LSLMETGTGW
     SWSHREDELF LMNSTVKVPV CGAILARWDA GRLSLSDALP VRKADLVPYA PVTETRVGGN
     MTLDELCLAA IDMSDNVAAN ILIGHLGGPE AVTQFFRSVG DPTSRLDRIE PKLNDFASGD
     ERDTTSPAAM SETLRALLLG DVLSPEARGK LAEWMRHGGV TGALLRAEAE DAWLILDKSG
     SGSHTRNLVA VIQPEGGAPW IATMFISDTD AEFEVRNEAL KDLGRAVVAV VRE
//