ID A0A0W0VT35_9GAMM Unreviewed; 359 AA.
AC A0A0W0VT35;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Membrane associated zinc metalloprotease {ECO:0000313|EMBL:KTD23202.1};
GN ORFNames=Llon_0087 {ECO:0000313|EMBL:KTD23202.1};
OS Legionella londiniensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45068 {ECO:0000313|EMBL:KTD23202.1, ECO:0000313|Proteomes:UP000054997};
RN [1] {ECO:0000313|EMBL:KTD23202.1, ECO:0000313|Proteomes:UP000054997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49505 {ECO:0000313|EMBL:KTD23202.1,
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931}.
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:KTD23202.1}.
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DR EMBL; LNYK01000001; KTD23202.1; -; Genomic_DNA.
DR RefSeq; WP_058528107.1; NZ_UGON01000002.1.
DR AlphaFoldDB; A0A0W0VT35; -.
DR STRING; 45068.Llon_0087; -.
DR PATRIC; fig|45068.5.peg.92; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000054997; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00989; PDZ_metalloprotease; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:KTD23202.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KTD23202.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054997};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 6..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..344
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 359 AA; 40562 MW; FC5D5F0A4D7CA1C7 CRC64;
MTVVYAVLAI IISLLAVVGL HEAGHAIAAR IFAVKIKRIA IGFGKPLLKK TSRRGIEWVW
GLWPLGGYVL LLNSRHHAVE PKNKRFCFDK KHVWQRIIIL SAGALVNILV AWFAFLFIYL
IGYKTILPVS AYVRPNSIAA QAGMQQKDRF ISIAGQPAES WRQVAMAFIM NLGEKDVLVE
IMDPAGKKRT AYFDLTRWEY NRKNNTLFKL IGVKPDTDKK YHLKISGLPV WQAARKAFEK
LYELIAFYLV LLKQLAAGVL PISVLLGPLG LFTEMIASFT QGLRMFLYFI GNLSLAVAVI
NLLPIPGLDG GSIFYAMIEK IRGRPMSIAM EILLHRLAII LFFVFLVQLL MNDMQRYLQ
//
