ID A0A0W0TZT0_9GAMM Unreviewed; 551 AA.
AC A0A0W0TZT0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=E4T54_04155 {ECO:0000313|EMBL:QBS12002.1}, Lgee_0878
GN {ECO:0000313|EMBL:KTD00973.1};
OS Legionella geestiana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45065 {ECO:0000313|EMBL:KTD00973.1, ECO:0000313|Proteomes:UP000054785};
RN [1] {ECO:0000313|EMBL:KTD00973.1, ECO:0000313|Proteomes:UP000054785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49504 {ECO:0000313|EMBL:KTD00973.1,
RC ECO:0000313|Proteomes:UP000054785};
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.
RN [2] {ECO:0000313|EMBL:QBS12002.1, ECO:0000313|Proteomes:UP000294523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1308 {ECO:0000313|EMBL:QBS12002.1,
RC ECO:0000313|Proteomes:UP000294523};
RA Durieux I., Ginevra C., Attaiech L., Picq K., Juan P.A., Jarraud S.,
RA Charpentier X.;
RT "Diverse conjugative elements silence natural transformation in Legionella
RT species.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Extracellular zinc metalloprotease.
CC {ECO:0000256|RuleBase:RU366073}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU366073};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366073}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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DR EMBL; LNYC01000031; KTD00973.1; -; Genomic_DNA.
DR EMBL; CP038271; QBS12002.1; -; Genomic_DNA.
DR RefSeq; WP_028386079.1; NZ_UGNZ01000001.1.
DR AlphaFoldDB; A0A0W0TZT0; -.
DR STRING; 45065.Lgee_0878; -.
DR KEGG; lgt:E4T54_04155; -.
DR PATRIC; fig|45065.4.peg.942; -.
DR OrthoDB; 5378341at2; -.
DR Proteomes; UP000054785; Unassembled WGS sequence.
DR Proteomes; UP000294523; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.40; -; 1.
DR Gene3D; 3.10.450.490; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU366073};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Reference proteome {ECO:0000313|Proteomes:UP000054785};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Signal {ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 20..551
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5034038877"
FT DOMAIN 216..354
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 357..544
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 347
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 474
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 551 AA; 60318 MW; 383CDEB4E74DC6D4 CRC64;
MYKKILFSLT LTLAHSAMAA SLQELYQTPL SALDGFNLVK LSPKASVTPS STGENTLQEV
GQTRLDGALI RRYQQYFRGI PVVGAQVAVR EAANARAAVA NGLLVNAISL ETRASVSQSR
AKTLAKAAWF AGETPRNTRA EAASLQIRMT DDNTPRLTWL VTFETTDTSG LRAIARVVID
AQNGEVLNAW NNLQTIAESG PGGNEKVKGY WYGLDANPTL DVPSSGAQCT MDNALVRLVR
LNHEWDEDGK ILGAFSYPCG QNTEDRVNGA FSPGNDAYYF ANTVVDMYKN WYGLHALQKP
DGSFMQLITR VHFGEKYDNA FWDSKTLTFG DGDALYPLTS LDIVGHEATH GFTEQHAGLE
YHDQPGALNE SMSDMAGMAA RAFLLQTNPA FYNKTHVTPN ALTWTIGESV MKGSGGAALR
YMDKPSKDGD SADCVDATLA KKSGESCGIT WSRLMLKARI YYPDYNQRQS YIVHTASGIF
NKAFYLLSKS MGVREAYKLM LRANMVYWTP TSSFESAACG VRRAAKDLNM NAAMVKLAFD
KVGIQTSKCT L
//
