ID A0A1F5ZGB5_9BACT Unreviewed; 317 AA.
AC A0A1F5ZGB5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=A2Z00_04810 {ECO:0000313|EMBL:OGG11538.1};
OS Candidatus Gottesmanbacteria bacterium RBG_13_45_10.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798370 {ECO:0000313|EMBL:OGG11538.1, ECO:0000313|Proteomes:UP000177268};
RN [1] {ECO:0000313|EMBL:OGG11538.1, ECO:0000313|Proteomes:UP000177268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGG11538.1}.
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DR EMBL; MFIZ01000024; OGG11538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5ZGB5; -.
DR STRING; 1798370.A2Z00_04810; -.
DR Proteomes; UP000177268; 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 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..289
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 317 AA; 35522 MW; 4761E507CC3ED481 CRC64;
MNLEAANQAR KQPQKRKRRL WLLLTIIAGV ALLWYIIVPK RTQVISPLAQ TETAVEFSIL
ALFRRPKNST ELRRKVEETI KDTWKNYSVL VVDYHSNFTM GINDAVIFNA ASINKIPILA
ALYTDVQKGD VDFDKVIILQ SQDVQDYGTG IIRYDPEGTA YTVKTLIRLM MQKSDNTAAH
ILGNYIIGLD RVQTLVNAWG LTQTDMANNK TSNKDMAILM DKIFRGKIAG VALTQEILAF
LKDSDFEDRI PALLPKNVTV YHKVGTGTGT VHDVGVVTQG KTAYYIGIFS SDITDEERAS
KLAAQVSKVV YDYMSSH
//
