ID A0A1I5UX17_9BACT Unreviewed; 783 AA.
AC A0A1I5UX17;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Zn-dependent metalloprotease {ECO:0000313|EMBL:SFP99587.1};
GN ORFNames=SAMN05444277_10478 {ECO:0000313|EMBL:SFP99587.1};
OS Parafilimonas terrae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Parafilimonas.
OX NCBI_TaxID=1465490 {ECO:0000313|EMBL:SFP99587.1, ECO:0000313|Proteomes:UP000199031};
RN [1] {ECO:0000313|EMBL:SFP99587.1, ECO:0000313|Proteomes:UP000199031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28286 {ECO:0000313|EMBL:SFP99587.1,
RC ECO:0000313|Proteomes:UP000199031};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388}.
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; FOXQ01000004; SFP99587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5UX17; -.
DR STRING; 1465490.SAMN05444277_10478; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000199031; Unassembled WGS sequence.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.490; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR045474; GEVED.
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; PF20009; GEVED; 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};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:SFP99587.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SFP99587.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199031};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 64..111
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 229..370
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 373..537
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT DOMAIN 609..684
FT /note="GEVED"
FT /evidence="ECO:0000259|Pfam:PF20009"
FT ACT_SITE 363
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 448
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 783 AA; 85324 MW; A1A1A277FACB075A CRC64;
MKTRLLSIVM LGLALHGFSQ NNLKTLIRGE NGTTKHFVKL AQDQQLPFNT SQAAKLLGLN
DKSSLVLKST EKDNLGFVHY RFQQTYQGIP VNHSMYIVNT KNGRVVSLSG TVITDFNESA
TATGAAKISP AQAIAYALRN VPATKYMWQD KGMEAALKAQ FKNSSATYYP VAEKCWFSEV
SSINPANLKL AYKIDVYAAE PYSRAYYYID AATGKLLGRE ERIHTADVTG TANTLYSGTQ
TIHSEQTGTN AYRLHDLSRG NGVITLRVGG DDFTSTSANW NLSLPDQNAL DAHWGVEMTY
DFYKEVFNRN SIDNNGYALY SYVNRKSILY RDNASWSGTA MNYGIRSGGS QKGVTGIDVT
GHELTHGVTQ YTSGLVYQNE PGAMNESMSD IMGKSVQFWA KPNDIDWRLS NDMNWFIRDM
SNPNAYQQPD TYKGTYWVNG GSDNGGVHTN SGVGNFMYYL LVTGGSGTND NGDAYNVQGI
GIEKAEQIIY RTETAYLTST SVYADWREAS VNAATDLYGA SSNEVAQVKN AWDAVGVYGE
DEPAYCVSKG LSTANEYINL VNFNGSDYVS GDNGGYGDFT SVVSDVVAGQ KATIQVRAGF
PGVVRKEGWT MYIDYNGDGD FNDAGEKVGS VVVKSAAILT KTFKVPASAK AGLTRMRIQM
HYNTAITDPC ATFDQGEVED YSVNITAAGA ATETLISDIS VYPNPIVSSS VKLNYTLVNS
GKVTFRLADA MGVSKNSYEA GVQTKGKNSF TLNNLSALHN GYYYVAVEQD GVVIGKITLL
VAH
//
