ID A0A0G0RNY3_9BACT Unreviewed; 589 AA.
AC A0A0G0RNY3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=PepF/M3 family oligoendopeptidase {ECO:0000313|EMBL:KKR54143.1};
GN ORFNames=UT90_C0001G0011 {ECO:0000313|EMBL:KKR54143.1};
OS Parcubacteria group bacterium GW2011_GWA1_40_21.
OC Bacteria.
OX NCBI_TaxID=1618784 {ECO:0000313|EMBL:KKR54143.1, ECO:0000313|Proteomes:UP000034712};
RN [1] {ECO:0000313|EMBL:KKR54143.1, ECO:0000313|Proteomes:UP000034712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKR54143.1}.
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DR EMBL; LBYO01000001; KKR54143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0RNY3; -.
DR STRING; 1618784.UT90_C0001G0011; -.
DR Proteomes; UP000034712; Unassembled WGS sequence.
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; cd09610; 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; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF08439; Peptidase_M3_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 105..159
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 193..569
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT COILED 202..229
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 589 AA; 68090 MW; 4DCAAEE4D10C6AA7 CRC64;
MNLLFSGSDS DLEKDKKIVS EKSSGFIDKW KDRNDYLKDP SVLKKALDEY EYLNRNFGTS
GNAGFYFELK SSLDQNDPKI KAKFKNIHDF SVKIGNDLQF FEHNIAKISP NNQTQFLNYK
GLREYRHFLE RLFKQSRYIL SDVEEKILNL KQATSHSNWI RMVSGFLSKE ERMVVTEKGK
KENKNFSEIM KLINSSNKKV RASAAEALND ILDKNKDVAE NEINSVLANK KINDDLRKME
RPDLARHLDD DIESEVVDTL ISVVSSSFNI SRKYYALKAK LMGVKRLEYH ERNVEYGKLS
AKYPHDKSVD LIRRVFSYLD KNFSDIFDNW VSQGQVDFFP KKSKRDGAFC ASDLISQPGY
VLLNYAETLD DVLTFAHEMG HAINSELQKR AQNSLNFGTP KSTAEVASTF MEDFILKELE
KESDDEMKLA LMVHKLNSDI STIFRQIACY MLEQELHKQF REKGYLSKEE IGKLFQKHMS
AYMGHAVIQS QGSENWWIHW GHIRNFFYNY SYASGLLISK AMQARYAEDH SFISKVKEFL
SAGTSDSPKN IFKKMSIDIT DKKFWESGLG KIEEDLKAAE KLAKKLGKI
//
