ID A0A0N1C5A7_9SPHN Unreviewed; 322 AA.
AC A0A0N1C5A7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Beta-lactamase {ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|RuleBase:RU361140};
GN ORFNames=IP81_06240 {ECO:0000313|EMBL:KPF92473.1};
OS Novosphingobium sp. AAP83.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523425 {ECO:0000313|EMBL:KPF92473.1, ECO:0000313|Proteomes:UP000037998};
RN [1] {ECO:0000313|EMBL:KPF92473.1, ECO:0000313|Proteomes:UP000037998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP83 {ECO:0000313|EMBL:KPF92473.1,
RC ECO:0000313|Proteomes:UP000037998};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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-A beta-lactamase family.
CC {ECO:0000256|RuleBase:RU361140}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPF92473.1}.
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; LJHY01000012; KPF92473.1; -; Genomic_DNA.
DR RefSeq; WP_054107127.1; NZ_LJHY01000012.1.
DR AlphaFoldDB; A0A0N1C5A7; -.
DR STRING; 1523425.IP81_06240; -.
DR PATRIC; fig|1523425.4.peg.413; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000037998; Unassembled WGS sequence.
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:SF4; SLR0121 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|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW Reference proteome {ECO:0000313|Proteomes:UP000037998};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..322
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005867661"
FT DOMAIN 58..282
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 322 AA; 34495 MW; 32C7F488B1FE4E31 CRC64;
MKFSTARIIA ALLVAAPAFV ITVPAVQSRT QDSILDQRDQ FIQQQIAAIA AEGRGRIGVA
AMDLDGGGQI MVNGDMPFPM ASTAKIAVAA TFLEQVEKGA HRLDQEFPMM LPVRETGQIS
PVAPLRAGTV LTAQSLMELM ITRSHNEATD GLINAVGGIE NINYWLTRNG IAGQRLDHTM
ATLVRDDGKV DPARVIDTRT SSTPRAMIAL LAAIDRGGVL SPESRAVLLD TMTRTSTGKT
RIRAGLPEGT LVAHKTGTLS GVTDDVGIVR LPDGRHLAVA FFVTGPEGHA VHAKLIARMM
RVIYDGYSAP VMNNTQDIAR RR
//
