ID L0A5I6_DEIPD Unreviewed; 425 AA.
AC L0A5I6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:AFZ68452.1};
GN OrderedLocusNames=Deipe_3001 {ECO:0000313|EMBL:AFZ68452.1};
OS Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS KR-200).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ68452.1, ECO:0000313|Proteomes:UP000010467};
RN [1] {ECO:0000313|Proteomes:UP000010467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC {ECO:0000313|Proteomes:UP000010467};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT 19664.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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; CP003382; AFZ68452.1; -; Genomic_DNA.
DR RefSeq; WP_015236754.1; NC_019793.1.
DR AlphaFoldDB; L0A5I6; -.
DR STRING; 937777.Deipe_3001; -.
DR KEGG; dpd:Deipe_3001; -.
DR PATRIC; fig|937777.3.peg.3017; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_3_3_0; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000010467; Chromosome.
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:InterPro.
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:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000010467}.
FT DOMAIN 29..174
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 181..353
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 425 AA; 46056 MW; E93F9408605C24C8 CRC64;
MPWPDPGARP SPARGPQVLQ IVLPNGLTVL GESDEHAETV ALGYFVRTGA RDETLQDLGA
SHFIEHLLFK GSERVSGREL NVRLDALGAN VNAFTSEETT VYHAACLPET WPELLSLLTE
LMQPAFRPAD VEIERGVILE EIAMYADDPS SRTFDELRAQ AWGTHPLGHL VLGTPQTVAG
LTLERLQDNF RSRYGTGSVT LVACGRFDWN ALVTAALALT SAWPQGNFTR ALSPHSFSAG
LQIVEDTDMN RANIAFLAPG LQASHPLREA AVVLAEILGG DNGRLYWALV DGGLADSVDL
SHVEFEETGA FEGAWSCDPT RAGQTLEVVR GELQRVQLES VTEAELARAR KKLAVSVALR
AETPYARLFT LGMDHTYLGR TPSVAESVAA FERVSRTEVE EVLALRPFDA LNIVVLGPPA
GQFPA
//
