ID A0A160T6S9_9CHLR Unreviewed; 500 AA.
AC A0A160T6S9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 2.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=CFX0092_A2867 {ECO:0000313|EMBL:CUS04745.2};
OS Candidatus Promineifilum breve.
OC Bacteria; Chloroflexota; Ardenticatenia; Candidatus Promineifilales;
OC Candidatus Promineifilaceae; Candidatus Promineifilum.
OX NCBI_TaxID=1806508 {ECO:0000313|EMBL:CUS04745.2, ECO:0000313|Proteomes:UP000215027};
RN [1] {ECO:0000313|EMBL:CUS04745.2, ECO:0000313|Proteomes:UP000215027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cfx-K {ECO:0000313|EMBL:CUS04745.2,
RC ECO:0000313|Proteomes:UP000215027};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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 -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009}.
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; LN890655; CUS04745.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A160T6S9; -.
DR KEGG; pbf:CFX0092_A2867; -.
DR OrthoDB; 138826at2; -.
DR Proteomes; UP000215027; Chromosome i.
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 Reference proteome {ECO:0000313|Proteomes:UP000215027};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 224..444
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 330..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 54765 MW; CA94ABD7E08B9D56 CRC64;
MLRVLRRILL FTLLFVGAAF LLYQGFLFWR ALDKLPPTTT IAGVAVGGLT PDAARDAVND
RYLSPVVVYN GEERAAELMP ADAGFTIDTE GMLAQARAEW EKQEMWLRYV EFVVGISPQP
IIIPIRARHD DAALAGQLDT IADFIDSPAR GPQLLADTGE IQPGQSGLVT DRAASLHHLR
SALYSPTDRQ ASLTLIEQPA PEWDIQVLQD AIENQLSAFE GFASVFILDL QTGEEVSINS
DVAVSALSIL KIAIFVEAYR ALDAPPNEYE QELFLSTATA SSNHSANLLL HVIAGEDNTY
EGAEVLTAEM RRMGMLNSFM AIPYDATEVP SRPSTYSTPA NANPSIDTRP DTSMQTTAED
IGGLLAMIYY CAQGEGGLLA VYPGEITQEE CQAIVDLMIQ NVEGNLIRFG VPDGVAVSHK
HGWSFNEHGD AGIVYSPGGD FVIYTLLAQP ESDWLSSEYS FPILREIARA SYNYFNRENP
YEGRAMDDLE ELEEIRAGGN
//
