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Database: UniProt
Entry: A0A1F3E8T7_9BACT
LinkDB: A0A1F3E8T7_9BACT
Original site: A0A1F3E8T7_9BACT 
ID   A0A1F3E8T7_9BACT        Unreviewed;       428 AA.
AC   A0A1F3E8T7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Peptidase S49 domain-containing protein {ECO:0000259|Pfam:PF01343};
GN   ORFNames=A2X13_14660 {ECO:0000313|EMBL:OFX50114.1};
OS   Bacteroidetes bacterium GWC2_33_15.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1797324 {ECO:0000313|EMBL:OFX50114.1, ECO:0000313|Proteomes:UP000177978};
RN   [1] {ECO:0000313|EMBL:OFX50114.1, ECO:0000313|Proteomes:UP000177978}
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   -!- SIMILARITY: Belongs to the peptidase S49 family.
CC       {ECO:0000256|ARBA:ARBA00008683}.
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:OFX50114.1}.
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DR   EMBL; MENN01000019; OFX50114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F3E8T7; -.
DR   Proteomes; UP000177978; Unassembled WGS sequence.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd07022; S49_Sppa_36K_type; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR002142; Peptidase_S49.
DR   InterPro; IPR033855; Protein_C.
DR   PANTHER; PTHR42987; PEPTIDASE S49; 1.
DR   PANTHER; PTHR42987:SF4; PROTEASE SLR0021-RELATED; 1.
DR   Pfam; PF01343; Peptidase_S49; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          141..289
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
FT   REGION          335..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   428 AA;  46832 MW;  DC7888C2FFA881D7 CRC64;
     MHNLISEILS GVWLIEPQKA SGYLPIVANL LKGESNDLIK NLSEKRLESK ALLFDAATGY
     RISEYGVADS PEKAPENSVV IIPVAGPITK YDQFCGPSGT KTKADILQRA DSNPNIVAAI
     LEIDSGGGEG AGTQHFAQVI KNTNMPVIAF VEDMAASAAY WIASQCDIIV MQEKTSQVGS
     IGAYTTLVDV KRYFKNIGLD ILEVYAKQST EKNKAFREAF NNDDTSLIKD KISEFNQFFI
     NDIKSFRGEK IKSDPFKGQM YFAEQAVEIG LADEIGTLDY AIKIAANLSK NYNQNPDKMK
     IKESWKALVA LFGSDTTELK EEGVEKINNE LQSKTDELAT KTSENSQLKT DLETEKAARV
     AAENSLKTEQ EKVATLETEK AALETKLAAK PAVSSASPEG TDPNPVLNSI EEPFDEADEV
     AKSILKHK
//
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