ID A0A261FKF3_9BIFI Unreviewed; 351 AA.
AC A0A261FKF3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=BMYO_1197 {ECO:0000313|EMBL:OZG59629.1};
OS Bifidobacterium myosotis.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1630166 {ECO:0000313|EMBL:OZG59629.1, ECO:0000313|Proteomes:UP000216871};
RN [1] {ECO:0000313|EMBL:OZG59629.1, ECO:0000313|Proteomes:UP000216871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100196 {ECO:0000313|EMBL:OZG59629.1,
RC ECO:0000313|Proteomes:UP000216871};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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:OZG59629.1}.
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; MWWW01000013; OZG59629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261FKF3; -.
DR Proteomes; UP000216871; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
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 SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 177..326
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 47..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 351 AA; 36015 MW; 4679070991E8782C CRC64;
MARHQRRHAV SRAGFGARGM IVVAVAALVA VAVVLAGVFV WWMPRPSTST GESSRNASEP
ASGRSIASED VSGAADLTTP GHEVLNRSGV PQPNAGIVGR KAGEARMADV KTAIATAMSA
SGGTWSAYAE DLTSGATVSL NEQPMVAASE IKLYVMLTIY DRLASGTLNT GGRNTDALLG
EMITVSSNSA TNQLVLMIGD GDMAVGMQRV TDTAARYGFA SSRQLRALSD AGTDGSGTEN
WTSSADCGRL LAALYRGQLV SPEASQSMLT LLEGQTRRNK IPSGVPAGIQ VANKTGELGG
VENDAAIIWG KAADGSARDY VLVIMTSGVD SATAQQAIVG ASSAVYAAMT A
//
