ID   D9S9L1_FIBSS            Unreviewed;       492 AA.
AC   D9S9L1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Peptidase, M16 family {ECO:0000313|EMBL:ADL25391.1};
GN   OrderedLocusNames=FSU_1159 {ECO:0000313|EMBL:ADL25391.1};
OS   Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC   Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC   Fibrobacter.
OX   NCBI_TaxID=59374 {ECO:0000313|EMBL:ADL25391.1, ECO:0000313|Proteomes:UP000000517};
RN   [1] {ECO:0000313|Proteomes:UP000000517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19169 / S85 {ECO:0000313|Proteomes:UP000000517};
RA   Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B.,
RA   Russell J.B., Cann I.K.O., Mackie R.I., White B.A.;
RT   "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; CP002158; ADL25391.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9S9L1; -.
DR   STRING; 59374.FSU_1159; -.
DR   KEGG; fsc:FSU_1159; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_1_2_0; -.
DR   Proteomes; UP000000517; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..492
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003127947"
FT   DOMAIN          46..91
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          249..425
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   492 AA;  55605 MW;  AA3D3D2B2A9BD19E CRC64;
     MSSMRKLFAR IAMCCAFVPA LLTGTSAAAV NLPVHKEVLD NGLTVLLYPN KQAPTVSCRL
     FYVTGSVHEV PGKSGLAHIL EHELFKGTKK VGVSDSVADV RFMATQDSLQ ALIRPAKIAG
     DTALVKKLTA EHDSVLNEHR KIFIKDELWG AYQAAGGTGL NAFTSDLLTA YTVTLPKNKI
     ELFLWLESDR MQNAVLREFY SERSVVREER RMRYDDRPTG RFYETLNSMI YEAFPYRVPT
     IGWPSDIDNL TREQAEEHYR KYYKPRNAIL VMAGDLDTLE TMKVVKKYFA PIPAGEAFPP
     LTVRDPEQAG EKRLTVKRKD APNLYTLVFK TPAVGDSTLY ALDIAEGVLN GRSGRLYKRL
     VEEEKLAVGV SASNSPNKYI SEFSVRVNLR PDANREKVEK VVWEELEKLK NEQVSAREFQ
     KVKNRAYAGL VRSLTDMENV ATMLGWYEVH GDYRIFLNWA DNLEKVNVAD VQNVSKKTFV
     REKSIAGFLV KE
//