ID A0A0W0WUP8_9GAMM Unreviewed; 471 AA.
AC A0A0W0WUP8;
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=Zn-dependent protease {ECO:0000313|EMBL:KTD36065.1};
GN ORFNames=Lnau_1049 {ECO:0000313|EMBL:KTD36065.1};
OS Legionella nautarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD36065.1, ECO:0000313|Proteomes:UP000054725};
RN [1] {ECO:0000313|EMBL:KTD36065.1, ECO:0000313|Proteomes:UP000054725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD36065.1,
RC ECO:0000313|Proteomes:UP000054725};
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=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KTD36065.1}.
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DR EMBL; LNYO01000013; KTD36065.1; -; Genomic_DNA.
DR RefSeq; WP_058504091.1; NZ_LNYO01000013.1.
DR AlphaFoldDB; A0A0W0WUP8; -.
DR STRING; 45070.Lnau_1049; -.
DR PATRIC; fig|45070.6.peg.1110; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000054725; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR22726:SF25; BETA-BARREL ASSEMBLY-ENHANCING PROTEASE; 1.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KTD36065.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 64..252
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 471 AA; 53577 MW; 2AF2AEC97E2E2BAB CRC64;
MGLLHRSKRQ RFLKKSLGLL LAILQFFSPN AFSFSPYSTR ELEELEKEFV QLINQSDSLE
RNPLATQYIN HLGKRLARVA HIPTPYFFIV KSNEINAFAG PGGYIGINTR LILATENESE
LAAVMAHEIA HVRLHHLYNM IEHQKQMRIP MIASMLASIA LGVINPTLGS GAFMASVSGF
AQDSINFTRA NEKEADRIGI DMLIKSGLDP RAMASFFRKM QENSRYYYTA NIPAILRTHP
LDEDRIAEAE NRSDRIAKKQ YPDNLDYRLF KELIRVSVTN DSKQLLDYYH YHCAKKNNST
CEYGYALSLM SLNQFQPAET HLSPLLSRDH DNLFYQIAMA QAETGTKQYS SALNRLNALQ
TNYPENYAAL MAYAQGLLAA GQAERAASIL LKGSRIFKRD LPLCEELARA QATSHRKSYA
YFTQAQCQLL QGRHRDAVRQ LKQAKILAKN DAYLQARINA MIDEIKFYTE K
//
