ID   A5USQ7_ROSS1            Unreviewed;       600 AA.
AC   A5USQ7;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   OrderedLocusNames=RoseRS_1255 {ECO:0000313|EMBL:ABQ89660.1};
OS   Roseiflexus sp. (strain RS-1).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ89660.1, ECO:0000313|Proteomes:UP000006554};
RN   [1] {ECO:0000313|Proteomes:UP000006554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Roseiflexus sp. RS-1.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has oligopeptidase activity and degrades a variety of small
CC       bioactive peptides. {ECO:0000256|RuleBase:RU368091}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU368091};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU368091};
CC   -!- SIMILARITY: Belongs to the peptidase M3B family.
CC       {ECO:0000256|RuleBase:RU368091}.
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DR   EMBL; CP000686; ABQ89660.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5USQ7; -.
DR   STRING; 357808.RoseRS_1255; -.
DR   KEGG; rrs:RoseRS_1255; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_0; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000006554; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09608; 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   Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 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; IPR004438; Peptidase_M3B.
DR   NCBIfam; TIGR00181; pepF; 1.
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:RU368091};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368091};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU368091};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU368091};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          117..186
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          208..587
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   600 AA;  68529 MW;  3B9778664BA5DA53 CRC64;
     MTETQKVPRR DEIPEHYRWD LTTIYVDDAA WEQDVATIEQ MLSDVAAVQG RVAGSPDDLL
     AALRLRDQVS MRLWQIYVYA NRRFDSDTTD PVGQALAERA GTLAAKVGAA LAFIEPEILA
     APEDQIRAWI REYPDLAVYE YALDQLLRQR AHVRSAEVEA ILAQFSDITR APGEIFEVLT
     NADLHFPSIE DEQGQPVQLS HGRFLRFLRS PDRRVRRDAF VGYYSAFQGI RNTLGASLAA
     QVRTHVLNAK VRNYASSLEA ALTPNDIPVE VYHNLIATVN ASLPRLHRYF QARRKIMGLD
     ELHFYDLYAP LVPEADVAVP YEEAERMVRA AFEPLGDEYG AAVAQAFRSR WIDVYENIGK
     RSGAYSDGSY TTAPFMLLNY QERLNDVFTL AHELGHAMHS YFTRKTQPYI YGDYTIFVAE
     VASTLNEALL TDHLLRTRDD PILRRYLIVE QLEDIRTTLF RQTMFAEFEL EIHRRAETGE
     PLTTELFSTI YRDLVARYHG SEVALDEQIA LEWARIPHFY YNFYVYQYAT GLSAALALHK
     RIVQEGSPAI ERYLHFLRSG SSRPSIELLR DAGVDMLSPA PIQAAMDHFS ALLDELERMT
//