ID A0A1Y5RPL2_9RHOB Unreviewed; 603 AA.
AC A0A1Y5RPL2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Oligoendopeptidase F, plasmid {ECO:0000313|EMBL:SLN22376.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:SLN22376.1};
GN Name=pepF1 {ECO:0000313|EMBL:SLN22376.1};
GN ORFNames=PSJ8397_00899 {ECO:0000313|EMBL:SLN22376.1};
OS Pseudooctadecabacter jejudonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooctadecabacter.
OX NCBI_TaxID=1391910 {ECO:0000313|EMBL:SLN22376.1, ECO:0000313|Proteomes:UP000193623};
RN [1] {ECO:0000313|EMBL:SLN22376.1, ECO:0000313|Proteomes:UP000193623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8397 {ECO:0000313|EMBL:SLN22376.1,
RC ECO:0000313|Proteomes:UP000193623};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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 ---------------------------------------------------------------------------
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; FWFT01000001; SLN22376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5RPL2; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000193623; 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 InterPro; IPR011977; Pept_M3B_clade3.
DR NCBIfam; TIGR02290; M3_fam_3; 1.
DR PANTHER; PTHR11804:SF5; OLIGOENDOPEPTIDASE F; 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 Reference proteome {ECO:0000313|Proteomes:UP000193623};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 125..194
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 209..589
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 603 AA; 67907 MW; 36CACDB240A47B92 CRC64;
MNDPRTFDAN ATGTTPFGDL PEWDLTDLYP APDSKEIKRD QDWLEDACRS FATDYEGKLA
GLDADGLLEA VKRYEQIDII AGRIMSYAGL RYYQHTTDPE RAKFMSDMQD KITTYTTPLV
FYGLEFNRLD DAHIEALLAA NADLARYKPV FDRMRAMKPY QLSDELEKFL HDQSVVGSAA
WNKLFDETIA GLKFTVNGDE LNIEGTLNLL SEQDRSTREA ASRELARVFG ENVGLFARVH
NTLAKEKEVE DRWRGLPTPQ TGRHLSNHVE PEVVEALRNA VVDAYPRLSH RYYALKAKWM
GLETMEVWDR NAPLPMEADR TVPWDEAQQT VMDAYAAFDP RMADLAKPFF TDGWIDAGVK
DGKAPGAFAH PTVTTVHPYV MLNYLGKPRD VMTLAHELGH GVHQVLAAEQ GELLSSTPLT
LAETASVFGE MLTFRKLLDQ AKDATERKVL LAGKVEDMIN TVVRQIAFYD FECKLHAARA
QGELTPDDIN ALWMSVQGES LGPVFNFMDG YETFWAYIPH FVHSPFYVYA YAFGDGLVNA
LYAVFEEQGE AFKDKYFDML KAGGSKHHSE LLAPFGLDAS DPAFWAKGLS MIEGMIDELE
AME
//
