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Database: UniProt
Entry: G8UII0_TANFA
LinkDB: G8UII0_TANFA
Original site: G8UII0_TANFA 
ID   G8UII0_TANFA            Unreviewed;       655 AA.
AC   G8UII0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   OrderedLocusNames=BFO_1168 {ECO:0000313|EMBL:AEW20287.1};
OS   Tannerella forsythia (strain ATCC 43037 / JCM 10827 / CCUG 21028 A / KCTC
OS   5666 / FDC 338) (Bacteroides forsythus).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Tannerella.
OX   NCBI_TaxID=203275 {ECO:0000313|EMBL:AEW20287.1, ECO:0000313|Proteomes:UP000005436};
RN   [1] {ECO:0000313|Proteomes:UP000005436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43037 / JCM 10827 / CCUG 33226 / KCTC 5666 / FDC 338
RC   {ECO:0000313|Proteomes:UP000005436};
RA   Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., Hostetler J.,
RA   Shetty J., Torralba M., Gill S., Nelson K.;
RT   "Complete sequence of Tannerella forsythia ATCC 43037.";
RL   Submitted (DEC-2011) 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; CP003191; AEW20287.1; -; Genomic_DNA.
DR   RefSeq; WP_014224577.1; NC_016610.1.
DR   AlphaFoldDB; G8UII0; -.
DR   GeneID; 34758407; -.
DR   KEGG; tfo:BFO_1168; -.
DR   PATRIC; fig|203275.8.peg.1047; -.
DR   eggNOG; COG3227; Bacteria.
DR   HOGENOM; CLU_418514_0_0_10; -.
DR   Proteomes; UP000005436; 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   Gene3D; 3.10.170.10; -; 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   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
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   Pfam; PF18962; Por_Secre_tail; 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:UP000005436};
KW   Secreted {ECO:0000256|RuleBase:RU366073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT   DOMAIN          57..204
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          218..374
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   DOMAIN          574..653
FT                   /note="Secretion system C-terminal sorting"
FT                   /evidence="ECO:0000259|Pfam:PF18962"
SQ   SEQUENCE   655 AA;  73752 MW;  5B4D892B38EFEFD9 CRC64;
     MIIKEILEKT DTLPALVYRV YLYADYPQNT EVGFIDAHTG SLRMTEPVFI DFSAQGTFAT
     RYSGSQQGTT HNYQGSYHLV DSTRNTIIHT WNLEGRTNIL SRVDITDNDN NWTQAEHRPN
     NNDMGLDVQW ALQRICDRLY NTHNINSMDD DGFTIDAHIR YSNNYDNAFW NSIDRTLSFG
     EGGSDFQPLA SVDVVAHEFG HGITHFQIGW NNTTDQRAFN EGMSDIWGVI MEHRIHPNSV
     WQIGEQITRN YSCLRNLQNT NASNAMSQIA NTYASPQYNS GDSYVRGGVF SHWFYLLVNG
     GTGVNTLGRN YSVWGIGMDN AENLIVKAVF GGYLRFTTSY AQIRTSMINA AREIAGTNSF
     LEHQIENAWY AVGVGNTQYQ PHLSGPASVC DQATYTIENL PAGAIVQWSL SNNNAIILSS
     TTDKVTLKRR NTGDVELRAN IRINSNPLNI NRNIWLFDPI LEASVYDNGI GWHNADMSYG
     QIGLNLYQVT PNRDIHFRIN NAPLINIPIS NWEWVNYNPN IVSVSHQGGY IAHLTPLREG
     RARINVRVKQ QGCYTNSIAL SIEVTSRSHF TLSPNPATDA VTLQLTETDE VNGLSVLSTD
     RSPYEIQLWS GMTMLRSFRT NEPTFQISMA GLPAGLYFVR VVKDGQTYTQ KLIKK
//
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