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Database: UniProt
Entry: A0A1G1C6I6_9BACT
LinkDB: A0A1G1C6I6_9BACT
Original site: A0A1G1C6I6_9BACT 
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
//
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