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Database: UniProt
Entry: A0A1G0NTA6_9BACT
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Original site: A0A1G0NTA6_9BACT 
ID   A0A1G0NTA6_9BACT        Unreviewed;       495 AA.
AC   A0A1G0NTA6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Serine hydrolase {ECO:0000313|EMBL:OGU26691.1};
GN   ORFNames=A2X66_01030 {ECO:0000313|EMBL:OGU26691.1};
OS   Ignavibacteria bacterium GWA2_54_16.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1798420 {ECO:0000313|EMBL:OGU26691.1, ECO:0000313|Proteomes:UP000182282};
RN   [1] {ECO:0000313|EMBL:OGU26691.1, ECO:0000313|Proteomes:UP000182282}
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   -!- 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:OGU26691.1}.
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DR   EMBL; MGZS01000053; OGU26691.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0NTA6; -.
DR   STRING; 1798420.A2X66_01030; -.
DR   Proteomes; UP000182282; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR   PANTHER; PTHR46825:SF9; PROTEIN FLP; 1.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:OGU26691.1}; Signal {ECO:0000256|SAM:SignalP};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..495
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009229269"
FT   DOMAIN          37..355
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
FT   REPEAT          449..482
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   495 AA;  54414 MW;  414FEE212D7BEAC6 CRC64;
     MRLPNRIRAA GLVLSLALLV AGMSSAILAQ DKAKQIDDLI GKYHEYAQFN GAVLVADQGK
     VLFRKGYGEA NKEWNIPNTP DTKFRLGSIT KQFTATLILQ LAEQGRINLG GKITDYIAEY
     PKATGDKITI SQLLTHSSGI PGYTEMPNFG KELSRNPFTP MDFIKVFWDL PLQFEPGTKF
     TYSNSGYFIL GVIIEKLTSK PYARVVVENI FKPLGMTNSG YDMPEPVLPK RAAGYQKRGS
     GYINAPYLDM TVPYSAGSLY STAEDLYLWD QALYGEKILS EKSKATMFEP RITAGGGPAS
     MRYAYGWFVG KQRVGSSQDS VSVISHGGGI NGFNTLITRI PGTKSLVVLL NNTGGAPLGP
     MAESVLGILY GKPFRPASRP LVDLLREMIR TSGIEAAVSR FNELRTKKDE YSLSEAQMNA
     LGYEYLQEKK LNEAIAVFKL NVESYPKSSN VYDSLGEAYA LAGERELAIK NYEKSLELDP
     ASESGIEALK KLKAQ
//
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