ID A0A0W0YXZ6_LEGSP Unreviewed; 518 AA.
AC A0A0W0YXZ6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN Name=lasB_2 {ECO:0000313|EMBL:KTD61760.1};
GN ORFNames=Lspi_2390 {ECO:0000313|EMBL:KTD61760.1};
OS Legionella spiritensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=452 {ECO:0000313|EMBL:KTD61760.1, ECO:0000313|Proteomes:UP000054877};
RN [1] {ECO:0000313|EMBL:KTD61760.1, ECO:0000313|Proteomes:UP000054877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mt.St.Helens-9 {ECO:0000313|EMBL:KTD61760.1,
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 -!- 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}.
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:KTD61760.1}.
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DR EMBL; LNYX01000031; KTD61760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0YXZ6; -.
DR STRING; 452.Lspi_2390; -.
DR PATRIC; fig|452.5.peg.2638; -.
DR OrthoDB; 5378341at2; -.
DR Proteomes; UP000054877; Unassembled WGS sequence.
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 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; IPR011096; FTP_domain.
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; PF07504; FTP; 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:UP000054877};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 18..518
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023027789"
FT DOMAIN 43..73
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 196..359
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 362..513
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 352
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 441
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 518 AA; 58099 MW; BC62F0D480228F90 CRC64;
MKKTLLLLTL IPLTVHAAEI QPIWGKIPPS IAATQFKNQL QLVKDKNGHR RYQVVYKGIP
VWGYQLIEHS KGKISYSGYM VSGIEKDISS LTPALNKGSV IRTIAARGGK NITLKTVIYI
RNKKARLAYH VKYYTMDNHK PANPNKIIDA NDGTVLKAFN ALRTRRVGQG SGGNYIRLPS
RSGDFYYGQP DSRINSLGRF DVTVAGGTCR VANSNFEVVN LQNKAFDWDL FPISAATQDQ
YPVFSYPCSR HTQYVNYDDG GYAPINEGLS PVNDAMYFAQ TTLDMYQQLY GDDKPFGDDL
PVRAYVHVAN LDNAFAIGTE YENGRIHSHQ QIVIGNGEEY FAPMSQTTIP HELSHNVTNN
YSGLIYDGQS GGIDEAFSDM ADLALRDYLS RLYPWYWDGK DWSIGREEAL DGIPLRYMEN
PGDDGYSIAS AEEYHEGLDV HFSSGVFNRA FFLLAHQPGW NAQKAFQVMF DANRYYWVPN
TNFDFASCGV IQAAMDRGWD TAAVIDAFHV VAVRCPLV
//
