ID T0K1S1_9SPHN Unreviewed; 378 AA.
AC T0K1S1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=M529_19280 {ECO:0000313|EMBL:EQB30494.1};
OS Sphingobium ummariense RL-3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1346791 {ECO:0000313|EMBL:EQB30494.1, ECO:0000313|Proteomes:UP000015523};
RN [1] {ECO:0000313|EMBL:EQB30494.1, ECO:0000313|Proteomes:UP000015523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RL-3 {ECO:0000313|EMBL:EQB30494.1,
RC ECO:0000313|Proteomes:UP000015523};
RX PubMed=24233594;
RA Kohli P., Dua A., Sangwan N., Oldach P., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium ummariense Strain RL-3, a
RT Hexachlorocyclohexane-Degrading Bacterium.";
RL Genome Announc. 1:e00956-13(2013).
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 -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009}.
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:EQB30494.1}.
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DR EMBL; AUWY01000120; EQB30494.1; -; Genomic_DNA.
DR RefSeq; WP_021319454.1; NZ_AUWY01000120.1.
DR AlphaFoldDB; T0K1S1; -.
DR STRING; 1346791.M529_19280; -.
DR PATRIC; fig|1346791.3.peg.3721; -.
DR eggNOG; COG2367; Bacteria.
DR OrthoDB; 9784149at2; -.
DR Proteomes; UP000015523; Unassembled WGS sequence.
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 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Reference proteome {ECO:0000313|Proteomes:UP000015523};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..378
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004566155"
FT DOMAIN 91..349
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 31..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 40615 MW; 15AC932CB269C147 CRC64;
MSSHDARGGS ARLVLLIAAL SACVSAPPPP RAQAAAARPA QRVQPTTNTW PIKPVANPPR
PFQEIDQRET PSPALVSVVR NLGQSFNGKV GIAVRRIGSD WTVAWNGNQL FPQQSVSKLW
VSMAFLDAVD RGKLRLADTT TITKKDLTLF HQPTAALVGN TGWTTTYADL MKRAMTQSDN
TANDTLLRAV GGPDVVRGFL ARRLIKDIRF GPGERLLQAT TAGLDWRQDY SLGRNFYAAR
AKLPMAVRVK ALDNYLANPP DGAAPSSIVA ALAKLKEGDM LSAGSSRLLL SLMEEAKTGP
QRIKGGVPAG WHYLHKTGTG QDLPPRSTGF NDVGIMTAPD GTSYAVAVMI GSTTEPIPVR
WQLMQAVAKA VAANHEKR
//
