ID   A0A172T6B9_9DEIO        Unreviewed;       568 AA.
AC   A0A172T6B9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:ANE42521.1};
GN   ORFNames=SU48_00680 {ECO:0000313|EMBL:ANE42521.1};
OS   Deinococcus puniceus.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=1182568 {ECO:0000313|EMBL:ANE42521.1, ECO:0000313|Proteomes:UP000077363};
RN   [1] {ECO:0000313|EMBL:ANE42521.1, ECO:0000313|Proteomes:UP000077363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY1 {ECO:0000313|EMBL:ANE42521.1,
RC   ECO:0000313|Proteomes:UP000077363};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Deinococcus puniceus/DY1/ whole genome sequencing.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; CP011387; ANE42521.1; -; Genomic_DNA.
DR   RefSeq; WP_064013565.1; NZ_CP011387.1.
DR   AlphaFoldDB; A0A172T6B9; -.
DR   STRING; 1182568.SU48_00680; -.
DR   KEGG; dpu:SU48_00680; -.
DR   PATRIC; fig|1182568.3.peg.142; -.
DR   OrthoDB; 9762795at2; -.
DR   Proteomes; UP000077363; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09606; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF48; PUTATIVE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077363};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          171..559
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   568 AA;  63919 MW;  057A99DC4743CFEB CRC64;
     MTAQLEAVER ILAVPEDQTR WDTFAPRYQA LQDADLTADG VPAWLAQWSA VDADLTQARS
     KLSTHADLHT DDEAIQARFQ AFVQDVIPGV QRAEQALTEK LLAVPGYVPA PDFALNYRRF
     RDAAALFREA NVELGTTHEQ QMSRHGVITG NQTVTLDGES VTVPQAKARL DDPDRAARES
     AWQALAASNL AVAPDLDALM LELIATRQQL ARNADLGNFR DYMWKRLDRV DYTPADCTAF
     HEAVREEVVP LTTRMMADIA ATLGLDTVRP WDYNRNNLLD PQGRAPLKPF TTGAELEELA
     QAAFDSLDAD LGARFRSMRG GLLDLESRPG KMAHAYCEYY PVENQPFVLM NVVGTGEDVR
     VLFHEVGHAF HGFYSGDAQP LLWNRWSPIE FVEIPSMAME FLTLDHLGHA LTPDELTRYR
     AKQLEGVVAF LPWAAQMDAF QHWLYAEAPA DLTIADLDNK WLELDRTFHP FINWDGLDEG
     IRAKGWQYYH IFRAPFYYIE YAMCYLAAVG IWQGARLDPA AALTNYKTAL RLGSTAPNPE
     LYRAAGVEFR FDREYIKGLM AFLGEQLA
//