ID A0A099BVR2_9BACT Unreviewed; 587 AA.
AC A0A099BVR2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Signal peptidase {ECO:0000313|EMBL:KGI60135.1};
GN ORFNames=HMPREF0671_07800 {ECO:0000313|EMBL:KGI60135.1};
OS Prevotella sp. S7 MS 2.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1287488 {ECO:0000313|EMBL:KGI60135.1, ECO:0000313|Proteomes:UP000029732};
RN [1] {ECO:0000313|EMBL:KGI60135.1, ECO:0000313|Proteomes:UP000029732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7 MS 2 {ECO:0000313|EMBL:KGI60135.1,
RC ECO:0000313|Proteomes:UP000029732};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KGI60135.1}.
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DR EMBL; JRPT01000037; KGI60135.1; -; Genomic_DNA.
DR RefSeq; WP_036898944.1; NZ_JRPT01000037.1.
DR AlphaFoldDB; A0A099BVR2; -.
DR eggNOG; COG0616; Bacteria.
DR Proteomes; UP000029732; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
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; TIGR00705; SppA_67K; 1.
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, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000029732};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 120..271
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 369..522
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 188
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT ACT_SITE 386
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 587 AA; 65275 MW; F35DDBD2C1549066 CRC64;
MKDFFKNVLA TIVGLFIFGI ITVFFCFIGA IGMITANSST KKLESNSVLL LKLDGNMSEQ
DETTLSDQLY GNTGVSFKTY IEAINEAAHN DNISCIYLES GNLTADIAQR QELRDALLEF
KKSGKKVIAY GENYSLLNYY LATAADKVYM NPIGSITWKG IGGEMVYVKD LLAKVGVRVV
PFRMGKYKSA VEMFTEDKMS DPNREQTERY IHGWWDTVLN AVSGSRKISK DSLNAYADRL
IGMEETSKMV GYKMVDGLYY NDQIKDVVKK AIGIDKDEEL NLITPSELVA QKSESAEKHI
AVYYAYGNIV NNKMPQSMFG ENHEIVAKDV CRDLQDLADD DDIKAVVIRI NSGGGDAYAS
EQLWHQVAEL RKKKPVVISM SGAAASGGYY MSCPANWIVA DPTTITGSIG IFGLLPDQSE
LMTKKLGLKF DEVKTNRNSV FGASGHFLTG EQFNIMQTAI ENGYKLFKKR VAEGRKLSME
QVENIAQGHV YLGADAIKIG LVDELGGLNK AIAKAAELAK LKNYGTASYP EAKSWLDNIM
AIPDNSSFLD KQLETTFGEY YTTFKLIKDM QHRDRLQAAM PYILRIQ
//