ID A0A0W0YQ57_9GAMM Unreviewed; 318 AA.
AC A0A0W0YQ57;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Signal peptide peptidase {ECO:0000313|EMBL:KTD59036.1};
GN Name=sppA {ECO:0000313|EMBL:KTD59036.1};
GN ORFNames=Lsha_2068 {ECO:0000313|EMBL:KTD59036.1};
OS Legionella shakespearei DSM 23087.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD59036.1, ECO:0000313|Proteomes:UP000054600};
RN [1] {ECO:0000313|EMBL:KTD59036.1, ECO:0000313|Proteomes:UP000054600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD59036.1,
RC ECO:0000313|Proteomes:UP000054600};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD59036.1}.
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DR EMBL; LNYW01000052; KTD59036.1; -; Genomic_DNA.
DR RefSeq; WP_018576645.1; NZ_LNYW01000052.1.
DR AlphaFoldDB; A0A0W0YQ57; -.
DR STRING; 1122169.Lsha_2068; -.
DR PATRIC; fig|1122169.6.peg.2369; -.
DR eggNOG; COG0616; Bacteria.
DR OrthoDB; 9764363at2; -.
DR Proteomes; UP000054600; 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:0006508; P:proteolysis; IEA:InterPro.
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; IPR002142; Peptidase_S49.
DR InterPro; IPR047272; S49_SppA_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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054600};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 136..271
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
SQ SEQUENCE 318 AA; 35633 MW; 0437E915F62EC902 CRC64;
MNNDVSSNSN ADSQTLLNQI VIDYMKEKKW KRRWRWFFRT IFLLFILYMV YLMATYNSDA
SSSDSKDHVG LVDLNGEIFD AKGANADDFA KGVDSAYKNK NLKALIIRIN SPGGSPVQAE
YMYNTLKYYK AKYPDIKTYA VCVDLCASAA YYVAVATDQI YASPASMVGS IGVIYSGFGF
VDAIEKIGVS RRLQTSGANK GFLDPFSPTN DFQKQKLQTM LDLIHQQFIK RVKEGRGDRL
HIDDETFSGL FWTGEQAFAN GLIDGYASSG QLARDVIKID RLVDYTHKQN LFDRVSKNLG
TALADELPMS LGIKPGLR
//