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Database: UniProt
Entry: A0A0N1AE18_9PROT
LinkDB: A0A0N1AE18_9PROT
Original site: A0A0N1AE18_9PROT 
ID   A0A0N1AE18_9PROT        Unreviewed;       333 AA.
AC   A0A0N1AE18;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN   ORFNames=D621_15105 {ECO:0000313|EMBL:KPF49122.1};
OS   beta proteobacterium AAP51.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1523421 {ECO:0000313|EMBL:KPF49122.1, ECO:0000313|Proteomes:UP000037990};
RN   [1] {ECO:0000313|EMBL:KPF49122.1, ECO:0000313|Proteomes:UP000037990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP51 {ECO:0000313|EMBL:KPF49122.1,
RC   ECO:0000313|Proteomes:UP000037990};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KPF49122.1}.
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DR   EMBL; LJHT01000060; KPF49122.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1AE18; -.
DR   Proteomes; UP000037990; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR013424; PEP_exosort_dom.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   NCBIfam; TIGR02595; PEP_CTERM; 1.
DR   PANTHER; PTHR24260; -; 1.
DR   PANTHER; PTHR24260:SF136; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07589; PEP-CTERM; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..333
FT                   /note="Peptidase S1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005865586"
FT   TRANSMEM        310..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..301
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   333 AA;  33587 MW;  2730E27BEF55CCB9 CRC64;
     MFKLAAHTRQ LLALATLALC LPAAQASTAD YDAMVASGFT EEGIFPRIVI RDDIGLAASA
     TFAANPAFSG VVSISGCTGV LIAPTTILSA RHCSPTVGGT VRFGTNRNSP TFSTSIQSVL
     FPGGGTAGSP LLDGNDVAIL RLSSVVPANI ATPFALTAAT TELTGFSVVT LGYGGRGIGS
     TGATGSDGIR RGGTNVLDRY GAAVNTTTNI GGTTNIFSTD FDNPTGTSNT LGWLGSSATA
     TGFEATTAGG DSGGPLLFDN GGVWTLMGVL SGGTTTNSVY GDISWWTGVA PFRTQIEAAG
     GVFIAVVPEP GTYVMMLLGL GLIGLRLRRS AQA
//
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