ID A0A072NBW7_9DEIO Unreviewed; 594 AA.
AC A0A072NBW7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:KEF34458.1};
GN ORFNames=RDMS_07370 {ECO:0000313|EMBL:KEF34458.1};
OS Deinococcus sp. RL.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1489678 {ECO:0000313|EMBL:KEF34458.1, ECO:0000313|Proteomes:UP000027898};
RN [1] {ECO:0000313|EMBL:KEF34458.1, ECO:0000313|Proteomes:UP000027898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RL {ECO:0000313|EMBL:KEF34458.1,
RC ECO:0000313|Proteomes:UP000027898};
RA Lal R., Mahato N.K., Tripathi C., Verma H., Kumari R., Singh N.;
RT "Draft genome sequence of Deinococcus sp. strain RL isolated from sediments
RT of hot springs located at Manikaran, India.";
RL Submitted (MAY-2014) 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}.
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:KEF34458.1}.
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DR EMBL; JMQF01000031; KEF34458.1; -; Genomic_DNA.
DR RefSeq; WP_034404456.1; NZ_JMQF01000031.1.
DR AlphaFoldDB; A0A072NBW7; -.
DR eggNOG; COG1164; Bacteria.
DR OrthoDB; 9769691at2; -.
DR Proteomes; UP000027898; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09607; M3B_PepF; 1.
DR Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR InterPro; IPR034006; M3B_PepF_2.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR001333; Peptidase_M32_Taq.
DR PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000027898};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 200..579
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 594 AA; 66118 MW; 4F89917476134557 CRC64;
MTTTESRELP RWRTDDLYAG LQDPRLNADL AALREEVAAL EATFDRYGVR KDGDPATPEG
LEAVLGGLNA LLTRLTTLRG FISAFVTTDS RDALAQQKMG ELTTLTLPLG PLRSRLTAWL
GGQDVEALLR GSEVARQHEH FIRRSAERAR YQMTPEEEDL AARLRPSGAG GWAKLHGNVS
SQLRGEFRGQ SLPVTALRAL ATDPDESVRR DAYEAELKVW QGAEVVLAAA LNGVKGEEGT
LAARRGFPDA VAPSLLTHGI DRETLEAMQG AVVRSFPDFR RYFAAKARAL GKGQLDWWDL
FAPVGRSQTE WTYEAGTRFV EEQFRSYSDR LGDYAARAFA GDWIDAGPRD GKRGGAFCMG
WQGEESRILM NHDPSLDSVS TLAHELGHGY HNLLKAPRTP LQRETPMTLA ETASIFCETI
IQNAALERSE GEERLYVLET QLLGHAQVVV DIHSRFLFER AVFEKRAERD LTPQEISDLM
TWAQRETYGD ALASTHPYMW AVKPHYYSLS FYNYPYTFGL LFGLGLYAQY RAAKERGEAA
DFQRRYDELL SSTGLADART LAAGFGIDLH APDFWEASLD VIRGQIVAYE AALG
//
