ID A0A0W0Y0X2_9GAMM Unreviewed; 642 AA.
AC A0A0W0Y0X2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Serine protease, subtilase family {ECO:0000313|EMBL:KTD50453.1};
GN ORFNames=Lqui_1778 {ECO:0000313|EMBL:KTD50453.1};
OS Legionella quinlivanii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45073 {ECO:0000313|EMBL:KTD50453.1, ECO:0000313|Proteomes:UP000054618};
RN [1] {ECO:0000313|EMBL:KTD50453.1, ECO:0000313|Proteomes:UP000054618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC#1442-AUS-E {ECO:0000313|EMBL:KTD50453.1,
RC ECO:0000313|Proteomes:UP000054618};
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01032}.
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:KTD50453.1}.
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; LNYS01000008; KTD50453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0Y0X2; -.
DR STRING; 45073.Lqui_1778; -.
DR PATRIC; fig|45073.5.peg.1876; -.
DR OrthoDB; 9002785at2; -.
DR Proteomes; UP000054618; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01032,
KW ECO:0000313|EMBL:KTD50453.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054618};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT DOMAIN 219..642
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 307
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 311
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 523
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 642 AA; 69963 MW; 2DA5B9DCF36B6FDD CRC64;
MLVKGLIFIL LQCIITSLFA HTAHVRLPNP ELSLIQKAER LGPLNHEKKL SVTLWLKLRN
PTQLDQQVKS IYDPQSPAFQ QFLNADQVKR DYLPDDETIR AIKAYFEHQG MQVEPLYSNL
KITGTAEQIE QIFHIKLNHY RYKNKIVYGN DQAPLLPREI AAHVAGVSGL SNIPYASPKR
RFKPKNLNID TAHWQPEEIK LLWDSFTPAA LPTTTSLQGV SGSHLRTVYQ LNQIPPVNGV
AIDGANQTIV IIDGCGNSTP NQILAHVNHY NTENSLPQLN ASNFAVVKPD GSPYTGPCAN
PNGWDGEIIL DIDASHTIAP AANIVLVMTD DVNNAEVAHA LTTITSNQFS IGGFSNAYVV
SNSWDNDVEH PFEMLEAILQ LSAAQGLSVN FAAGDCGDQT YASSWPCSIM GAEPSVQYPV
SSAFVTAVSG TSLFVDQLWN YAFETGWGTL VNGSFYSGSM GGVSRYRSAP VWQSSISNFI
VGGYPQGTNN KRALPDIAML GDLYTGLLTY SDGCNPCWDG GASLATPLFS GTLTLVNQAR
AALAGNPHPI GLAAPYFYVY NASLLQNKAI NLITPPHLVI SGATPINGGP VSAFKLHDPY
FNQEIGFNWD SSLTIVENQF WNDVVGVGSP NIPNFVQMMA RM
//
