ID A0A1Y6F7K3_9SPHN Unreviewed; 340 AA.
AC A0A1Y6F7K3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN06297468_1541 {ECO:0000313|EMBL:SMQ69340.1};
OS Altererythrobacter xiamenensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=1316679 {ECO:0000313|EMBL:SMQ69340.1, ECO:0000313|Proteomes:UP000194420};
RN [1] {ECO:0000313|Proteomes:UP000194420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) 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}.
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DR EMBL; FXWG01000002; SMQ69340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6F7K3; -.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000194420; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000194420};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..340
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013119789"
FT DOMAIN 72..283
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 340 AA; 36084 MW; 6AF7B66D5B9ED196 CRC64;
MLTRLKGIAL IALVAAGATM SPAQAQGTNL EAAFDNALGT ELREPRTFEA VYESGFERRI
AQLADGTRGR IGVYAIDLSS GDEVSVLGDQ FFPMASTSKV AVAATYLAGV DEGRWGLTSE
WQLPRRGGAH VPAYRLIELM ISKSCNDCTD ALLDAVGGPA AVNAWVKKAG ISGFNLNRNI
RALIRDDGEV DPASVVDTRD AATPRAMGQL LAGIYQGRWL SSSSRQVILD SMEQTTTGKR
RMRSAVPLSA KLAHKTGTLS RTASDIGIFH TPDGRPIAVA IYVTGQSPSM AVENGSRAAK
LDARSQRDMR IATIAGALYE GFGGRNSDGR VWTSSGYGGE
//
