ID A0A0W0VNL7_9GAMM Unreviewed; 331 AA.
AC A0A0W0VNL7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Signal peptide peptidase {ECO:0000313|EMBL:KTD21674.1};
GN Name=sppA {ECO:0000313|EMBL:KTD21674.1};
GN ORFNames=Llon_0839 {ECO:0000313|EMBL:KTD21674.1};
OS Legionella londiniensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45068 {ECO:0000313|EMBL:KTD21674.1, ECO:0000313|Proteomes:UP000054997};
RN [1] {ECO:0000313|EMBL:KTD21674.1, ECO:0000313|Proteomes:UP000054997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49505 {ECO:0000313|EMBL:KTD21674.1,
RC ECO:0000313|Proteomes:UP000054997};
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:KTD21674.1}.
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DR EMBL; LNYK01000014; KTD21674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0VNL7; -.
DR STRING; 45068.Llon_0839; -.
DR PATRIC; fig|45068.5.peg.899; -.
DR Proteomes; UP000054997; 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:UP000054997};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..282
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
SQ SEQUENCE 331 AA; 37358 MW; 51E65F74FB0B2E07 CRC64;
MWVFALKKSS LFMNNHSSTD NAESQALVNK LVLEYMREQK RKRFWRWVFR FIIFLFIMWF
GYQILALRSA NLAAKAKPHV GLIDIEGTIF ADQSANSDNF VKGLEDAYEN ESLKALIIRI
DSPGGSPVQA DYMFNALMHY RKKYPDIKTY AVCVDACASA AYYVAAAADE IYANPSSLVG
SIGVLYNGFG FVDTLDKLGV SRRLYTAGRY KGFMDQFSPE NEKEVKILQN MLDIIHQQFI
KRVKEGRGKR LVIDDQTFSG LFWTGAQAKK RGLIDGFASS GQLARDIIKI DRIVDYTHKD
NLLERVAKNI GTAMASQTAL ILGARPGVQL R
//
