ID A0A0G0AX65_9BACT Unreviewed; 589 AA.
AC A0A0G0AX65;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=PepF/M3 family oligoendopeptidase {ECO:0000313|EMBL:KKP56036.1};
GN ORFNames=UR50_C0010G0027 {ECO:0000313|EMBL:KKP56036.1};
OS Parcubacteria group bacterium GW2011_GWC1_34_10.
OC Bacteria.
OX NCBI_TaxID=1618891 {ECO:0000313|EMBL:KKP56036.1, ECO:0000313|Proteomes:UP000034499};
RN [1] {ECO:0000313|EMBL:KKP56036.1, ECO:0000313|Proteomes:UP000034499}
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:KKP56036.1}.
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DR EMBL; LBPL01000010; KKP56036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0AX65; -.
DR STRING; 1618891.UR50_C0010G0027; -.
DR Proteomes; UP000034499; 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 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 112..169
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 204..562
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 589 AA; 68009 MW; 954D74E687A0CA1D CRC64;
MKYKTEWDLG HIYKGDIKKQ VTKDLATIKK LYLTFAKKYR KDKAHLKSSK ALAKVIEEYE
NLSNNPASER PSAYYSHRIS LNAEDNMAHA EIAKLSDFYA DLTNELEFFF LEIGKIPKDL
QTKFLKSKEL EPFKYFLKKL FENAKYNLSE PEEKIMNLKS TPAHSMWTSG FSKLLSKQMI
KFNGGQLPIA EAFAKISDLK TKERRKLHKE IMKVLENISD FSESEINAIV TNKKINDKLR
GFKVPYEATV KGYENDLKTI KDLVEAVTKN FSLAHRFYKI KAEMLDEKNL SYADRSAKVG
KTETKITFEE GTKKVIKSFN EAHPDFGNYV EEMFTKGLVD VFPKKGKHGG AFCSSGTNLP
TYILLNHVDD FRSMTTLAHE MGHGIHAKYS KTQRPIYEGH TIATAEVAST FFENLVFEEA
LKNISVKERM ILLHDKISDD ISTIFRQIAC FNFENELHLT IRKEGFLSKD KIAELLNKHM
KSYLGPIFDL KPEDGYFFVT WSHIRNFFYV YSYAFGQLIS DTLYENYKKD KTKIKDVIKF
LSAGASDSPE NIFKKIGINP NKKLFETGLL RIKANIDLLE SLWKQNKKL
//
