ID   A0A1N7DCE3_9ACTN        Unreviewed;       563 AA.
AC   A0A1N7DCE3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Signal peptide peptidase A. Serine peptidase. MEROPS family S49 {ECO:0000313|EMBL:SIR73496.1};
GN   ORFNames=SAMN05421833_11454 {ECO:0000313|EMBL:SIR73496.1};
OS   Microbispora rosea.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Microbispora.
OX   NCBI_TaxID=58117 {ECO:0000313|EMBL:SIR73496.1, ECO:0000313|Proteomes:UP000186096};
RN   [1] {ECO:0000313|EMBL:SIR73496.1, ECO:0000313|Proteomes:UP000186096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12950 {ECO:0000313|EMBL:SIR73496.1,
RC   ECO:0000313|Proteomes:UP000186096};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S49 family.
CC       {ECO:0000256|ARBA:ARBA00008683}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FTNI01000014; SIR73496.1; -; Genomic_DNA.
DR   RefSeq; WP_076436977.1; NZ_FTNI01000014.1.
DR   AlphaFoldDB; A0A1N7DCE3; -.
DR   STRING; 58117.SAMN05421833_11454; -.
DR   OrthoDB; 9764363at2; -.
DR   Proteomes; UP000186096; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd07018; S49_SppA_67K_type; 1.
DR   CDD; cd07023; S49_Sppa_N_C; 1.
DR   Gene3D; 6.20.330.10; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR004634; Pept_S49_pIV.
DR   InterPro; IPR004635; Pept_S49_SppA.
DR   InterPro; IPR002142; Peptidase_S49.
DR   InterPro; IPR047217; S49_SppA_67K_type_N.
DR   InterPro; IPR047272; S49_SppA_C.
DR   NCBIfam; TIGR00706; SppA_dom; 1.
DR   PANTHER; PTHR33209; PROTEASE 4; 1.
DR   PANTHER; PTHR33209:SF1; SERINE PROTEASE SPPA, CHLOROPLASTIC; 1.
DR   Pfam; PF01343; Peptidase_S49; 2.
DR   PIRSF; PIRSF001217; Protease_4_SppA; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   DOMAIN          97..246
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
FT   DOMAIN          347..496
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
FT   ACT_SITE        168
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT   ACT_SITE        363
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ   SEQUENCE   563 AA;  60052 MW;  F41B698A7FF7511D CRC64;
     MDATRTIVET VGKLRQRRTA PLVLELDLTE GLSEGPPADP ITALLSMRKA RLAEVLSGLR
     RARKDPRVTA LIVKIGGNPL GLGMVQELRT AVVKLRAAGK RTVAFAETFG EFGAGTVPYY
     LASAFERVYL QPSGDVGLTG VALEQRFLRD ALAKAGVEYQ LGQRHEYKTA ANTFTQNHMT
     DAHRESAGRI AESVTEQVVA GVAEGRGLDP KRVRELIDQG PFIGPEAVEA GLVDGLKYRD
     EVYAETVDEG AHLLYVSRYA KSALSRRVPH PGAATVALVH GTGMIRLGRS GRSPLGGGGA
     MGSDTICAAL RSARRDEKVK AIVFRVDSPG GSYVASDAIW REVVLARRAG KPVIVSMGDL
     AASGGYFVSM AADVIVAQPG TLTGSIGVFG GKPVVGELLG KLGVVTESVS EGANAGMFSP
     STAFSDEQWE RVNAWLDRIY GDFVGKVAQG RGLTEERAHE LARGRVWTGA DARQAGLADE
     LGGLEEALAL ARRRAGLPGD APVRTYPRMH PLERLRPPES SEDKSAALAR VRLEAWGPLA
     RMAGQLGLPA YGPLVLPGWW TIR
//