ID A0A1G1C6I6_9BACT Unreviewed; 305 AA.
AC A0A1G1C6I6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=A2Z41_03575 {ECO:0000313|EMBL:OGV89825.1};
OS Microgenomates group bacterium RBG_19FT_COMBO_39_10.
OC Bacteria.
OX NCBI_TaxID=1817748 {ECO:0000313|EMBL:OGV89825.1, ECO:0000313|Proteomes:UP000176844};
RN [1] {ECO:0000313|EMBL:OGV89825.1, ECO:0000313|Proteomes:UP000176844}
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:OGV89825.1}.
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DR EMBL; MHDD01000005; OGV89825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1C6I6; -.
DR STRING; 1817748.A2Z41_03575; -.
DR Proteomes; UP000176844; 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:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
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; D-ALANYL-D-ALANINE ENDOPEPTIDASE; 1.
DR Pfam; PF13354; Beta-lactamase2; 2.
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 33..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..191
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT DOMAIN 200..279
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 305 AA; 34780 MW; 50A6A5E6C321AA47 CRC64;
MIFKPKSEQQ ALPGIKPIKK QERKERRGEG RKAIIVLFIV TVLASVLFYL QAELPKIWGE
ITAPKVISRL PKGYFDPDQT ITQLKELTQD LSGTYGIYVY RFKDDYNYGL NQEKVFPAAS
LNKLPVMIAA YQQAEEGKVN LETKYTLKEE DKVQGVGLLQ SEPASSQYTY RQLIEYMAQH
SDNTAFKIMR QITREEIVEK MTPEEVGLLF RQIYEGELIN QENTDELLQF LTETDFEDRL
PQGVPGDIRV SHKIGTLTGV YSDAGIIFAE PPFVLVIMTE GARESEALEA LPQITQIVWD
FETAL
//