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Database: UniProt
Entry: C2BFD7_9FIRM
LinkDB: C2BFD7_9FIRM
Original site: C2BFD7_9FIRM 
ID   C2BFD7_9FIRM            Unreviewed;       599 AA.
AC   C2BFD7;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   Name=pepF {ECO:0000313|EMBL:EEI86423.1};
GN   ORFNames=HMPREF0072_1057 {ECO:0000313|EMBL:EEI86423.1};
OS   Anaerococcus lactolyticus ATCC 51172.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Anaerococcus.
OX   NCBI_TaxID=525254 {ECO:0000313|EMBL:EEI86423.1, ECO:0000313|Proteomes:UP000005984};
RN   [1] {ECO:0000313|EMBL:EEI86423.1, ECO:0000313|Proteomes:UP000005984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51172 {ECO:0000313|EMBL:EEI86423.1,
RC   ECO:0000313|Proteomes:UP000005984};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (OCT-2008) 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}.
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:EEI86423.1}.
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DR   EMBL; ABYO01000194; EEI86423.1; -; Genomic_DNA.
DR   RefSeq; WP_004827117.1; NZ_GG666044.1.
DR   AlphaFoldDB; C2BFD7; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_1_1_9; -.
DR   Proteomes; UP000005984; Unassembled WGS sequence.
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; cd09609; 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; IPR034009; M3B_PepF_4.
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; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF45; SIMILAR TO OLIGOENDOPEPTIDASE; 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:UP000005984};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          112..176
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          200..579
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   599 AA;  68325 MW;  76DD5CC81DB18FAD CRC64;
     MKKRCDVDPK ETWAIEDLYA SDEAFYADIE KLAGMASDFK EKYAKLETSE DVYNSLEAYS
     DIISLTDGLG TFSGISKETD ATDDAMAKRD AKFGSEAAKI FANLSFYESA LVKVDSKILD
     EVIKNHPGYA YYLQRVKDKA KYLLDEKTEA ALAALAPTFD APYTNYNDMR YGDMKFENIN
     HNGKEVVLNH NTFEEFLEGE TDTELRRKAF ADYHKVLGAY QNADASVYNN LIQNEKIMAD
     LRGYDSVFHY LLARQDVDFD IYENHIDIIM EKLAPIMRKY ATIIRNHYGL DEMTYADLKL
     SIDPDYEPQV SIEEARDYIV DGLSPLGENY IGYMKQAFAD RWIDYSQNIG KRTGAFCSSP
     YPSHPFIMTT YNHSMSQVMT LAHELGHAGQ GILSNANQNA LSCDMSMYFV EAPSTANEIT
     MERYLLKKAK DDREKLWVLS TMIGKTYYHN FVTHYLEAAF QREVYRRVEK GESLSAADFN
     QIFKEKLEKF WGDAVILNEG AELTWMRQPH YYMGLYSFTY QAGLTIGTAI SEKIVHGTEE
     DRKQWLEVLK LGGSMGPIDL AKAAGVDMTS TKPIEDAIAF IGQIVDQIDE LLKKLNMYK
//
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