ID A0A0W0Z5H6_LEGSP Unreviewed; 441 AA.
AC A0A0W0Z5H6;
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=Zinc protease {ECO:0000313|EMBL:KTD64394.1};
GN ORFNames=Lspi_1201 {ECO:0000313|EMBL:KTD64394.1};
OS Legionella spiritensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=452 {ECO:0000313|EMBL:KTD64394.1, ECO:0000313|Proteomes:UP000054877};
RN [1] {ECO:0000313|EMBL:KTD64394.1, ECO:0000313|Proteomes:UP000054877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mt.St.Helens-9 {ECO:0000313|EMBL:KTD64394.1,
RC ECO:0000313|Proteomes:UP000054877};
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 M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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:KTD64394.1}.
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DR EMBL; LNYX01000013; KTD64394.1; -; Genomic_DNA.
DR RefSeq; WP_058483135.1; NZ_LT906457.1.
DR AlphaFoldDB; A0A0W0Z5H6; -.
DR STRING; 452.Lspi_1201; -.
DR PATRIC; fig|452.5.peg.1329; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000054877; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KTD64394.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054877};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..441
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006918299"
FT DOMAIN 30..174
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 187..366
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 441 AA; 49779 MW; 43443CF2C63BD651 CRC64;
MRFALLLLCA AFTCQAANDV HKYTLDNGLK VVVKEDHRAP VAVSMIWYNI GSADEPGGIT
GVSHALEHMM FKGTPQYPAG TFSRTIANIG GQENAFTNYD YTAYFEKIAA NQLPIAFELE
ADRMRNLLLD KDEFAREIKV IQEERRLRTD DNPQALTYER YLATAHLADP YHHPVIGWMS
DLKNMHVDDL KSWYRSFYAP NNATLVVVGD VKPDKVYELA NLYFGKLPRQ PDYIRKPQQE
PPSLGPKTVA INAPAKLPML MFGFTVPGVK TADEDWEPYA LELIAGILDA GESARFAKNL
VRGNHVASGV DAFYDLYSRY QTQFIFFGIP SQNRSIEEMK AGILKEIKKL QTEPVSVKEL
NRVKTQIIAQ KVFEKDSIFG QAMEIGLLET LGLGWKTAQI YTDKINGVTP EQIQKAAQRY
FQPKLMTEAQ LFPVLQPEGQ Q
//
