ID   B0TG14_HELMI            Unreviewed;       604 AA.
AC   B0TG14;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   Name=pepF {ECO:0000313|EMBL:ABZ83171.1};
GN   ORFNames=HM1_0557 {ECO:0000313|EMBL:ABZ83171.1};
OS   Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Heliobacteriaceae;
OC   Heliomicrobium.
OX   NCBI_TaxID=498761 {ECO:0000313|EMBL:ABZ83171.1, ECO:0000313|Proteomes:UP000008550};
RN   [1] {ECO:0000313|EMBL:ABZ83171.1, ECO:0000313|Proteomes:UP000008550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51547 / Ice1 {ECO:0000313|Proteomes:UP000008550};
RX   PubMed=18441057; DOI=10.1128/JB.00299-08;
RA   Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA   Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA   Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA   Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT   "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT   of the Firmicutes containing the simplest photosynthetic apparatus.";
RL   J. Bacteriol. 190:4687-4696(2008).
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; CP000930; ABZ83171.1; -; Genomic_DNA.
DR   RefSeq; WP_012281387.1; NC_010337.2.
DR   AlphaFoldDB; B0TG14; -.
DR   STRING; 498761.HM1_0557; -.
DR   KEGG; hmo:HM1_0557; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_9; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000008550; 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   Reference proteome {ECO:0000313|Proteomes:UP000008550};
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          207..586
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   604 AA;  69567 MW;  A851D52BC2F8B7DF CRC64;
     MEKEKALPKR QDISAEFKWK LEDIYPTDDA WEKDFQAVPA LLDKITALKG KLQEKSANLL
     AVLQLQDELG KGLEKIFTYA RMRRDEDNTN PTYQALTDRA VALNARAAGE TSFITPEILA
     IPDDILQRFQ KEEQGLALYR FLLDDLKRQK AHVLTADEEA ILAQASELGQ SPGQIFTMLN
     NADLTFPTIR DEEGREVEIT HGRYGQLMES KDRRVRKEAF YGLYGTYKKL ENTLAATFTS
     AIKRDVFFSR VRRYPSALEA ALFGDNVPKD VYDNLIGTVR KHNDAMHRYV RLRKKLLGVD
     QLHMYDLYVP MVADVDWKVT YKEALEMVKQ GLEPLGDDYG RVLDESFKTG WIDVYENKGK
     TSGAYSWGPY GTHPYVLLNY QDRLDDVFTL AHEMGHALHS YYSHKEQPYI YSAYTIFVAE
     VASTVNETLL IRHLLEREQD KSRRLYLINH YLEQFRGTLY RQTMFAEFEK IVHAKIEAAE
     ALTLQELKQI YHRLNVDYYG PDIIVDDDID IEWARIPHFY NNFYVYKYAT GFSAATALSA
     QILAEGQPAV ERYLTFLKSG GSDYPLELLK RAGVDMGTAE PIEKALSVFR ELLDEMEKLT
     ARAN
//