ID Q9JP71_ACIAN Unreviewed; 298 AA.
AC Q9JP71;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=blaCARB-5 {ECO:0000313|EMBL:AAF61417.1};
OS Acinetobacter calcoaceticus subsp. anitratus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=107673 {ECO:0000313|EMBL:AAF61417.1};
RN [1] {ECO:0000313|EMBL:AAF61417.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A85 {ECO:0000313|EMBL:AAF61417.1};
RX PubMed=2786828; DOI=10.1016/0378-1097(89)90456-4;
RA Paul G., Joly-Guillou M.L., Bergogne-Berezin E., Nevot P., Philippon A.;
RT "Novel carbenicillin-hydrolyzing beta-lactamase (CARB-5) from Acinetobacter
RT calcoaceticus var. anitratus.";
RL FEMS Microbiol. Lett. 50:45-50(1989).
RN [2] {ECO:0000313|EMBL:AAF61417.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A85 {ECO:0000313|EMBL:AAF61417.1};
RA Choury D., Paul G., Joly-Guillou M.L.;
RL Submitted (MAR-1999) 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|ARBA:ARBA00001526,
CC ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF135373; AAF61417.1; -; Genomic_DNA.
DR RefSeq; WP_063859341.1; NG_048750.1.
DR AlphaFoldDB; Q9JP71; -.
DR SMR; Q9JP71; -.
DR KEGG; ag:AAF61417; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam 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; 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 {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..298
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004328231"
FT DOMAIN 48..264
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 298 AA; 32797 MW; 43B3ECE3094DD209 CRC64;
MNVRKHKASF FSVVITFLCL TLSLNANATD SVLEAVTNAE TELGARIGLA VHDLETGKRW
EHKSNERFPL SSTFKTLACA NVLQRVDLGK ERIDRVVRFS ESNLVTYSPV TEKHVGKKGM
SLAELCQATL STSDNSAANF ILQAIGGPKA LTKFLRSIGD DTTRLDRWET ELNEAVPGDK
RDTTTPIAMV TTLEKLLIDE TLSIKSRQQL ESWLKGNEVG DALFRKGVPS DWIVADRTGA
GGYGSRAITA VMWPPNRKPI VAALYITETD ASFEERNAVI AKIGEQIAKT VLMENSRN
//
