ID R5DIB0_9CLOT Unreviewed; 442 AA.
AC R5DIB0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:CCX79990.1};
GN ORFNames=BN763_00916 {ECO:0000313|EMBL:CCX79990.1};
OS Clostridium sp. CAG:715.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262834 {ECO:0000313|EMBL:CCX79990.1, ECO:0000313|Proteomes:UP000018125};
RN [1] {ECO:0000313|EMBL:CCX79990.1, ECO:0000313|Proteomes:UP000018125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:715 {ECO:0000313|Proteomes:UP000018125};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:CCX79990.1}.
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DR EMBL; CAXB010000031; CCX79990.1; -; Genomic_DNA.
DR AlphaFoldDB; R5DIB0; -.
DR Proteomes; UP000018125; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CCX79990.1};
KW Protease {ECO:0000313|EMBL:CCX79990.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018125}.
FT DOMAIN 26..134
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 195..373
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 442 AA; 51005 MW; 342CAE81D1088F21 CRC64;
MQKSTVKYPF LTEDVEIYER ENGHKIVLAH KEGELVNVST WVKTGSINED DKINGISHFL
EHLMFKGTHK HKAGYFDKTL EAKGAIVNAA TWKDYTFYYV TLPKGAEGKD LDLAIELHAD
MMLDPILPEE EIGSPFDLNN PKVTDKRERH VVIEEIRMRK DQNWTKVYNA CNFNMYKKHP
YKRDVIGTPE IISQVTRDEI MNYYKTFYSP ENMTTIIVGD FNKEKILAKV EKEFDFKGRP
NAPKRVNEID SPTDHTIVVE NKGQTNTSYL MIGFLGPKAN QLKENIELDI ISIILGESTS
SRMYQNLIEK QPEQIFMVAN AEHYQFKDGN NFFIQANFKP EKKDIAIKLV KEEISNLINN
KISEEELEKA KKKIKSRFAY AAETVSEIGE TIGYYMTVCE DLKLIEDYLK DLDAITISDL
ENIVKKYLNI NNAVISILEP EK
//
