ID A0A223D6N0_9BACL Unreviewed; 580 AA.
AC A0A223D6N0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN Name=pepF {ECO:0000313|EMBL:ASS77249.1};
GN ORFNames=CIG75_15550 {ECO:0000313|EMBL:ASS77249.1};
OS Tumebacillus algifaecis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Tumebacillus.
OX NCBI_TaxID=1214604 {ECO:0000313|EMBL:ASS77249.1, ECO:0000313|Proteomes:UP000214688};
RN [1] {ECO:0000313|EMBL:ASS77249.1, ECO:0000313|Proteomes:UP000214688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=THMBR28 {ECO:0000313|EMBL:ASS77249.1,
RC ECO:0000313|Proteomes:UP000214688};
RX PubMed=25858243; DOI=10.1099/ijs.0.000240;
RA Wu Y.F., Zhang B., Xing P., Wu Q.L., Liu S.J.;
RT "Tumebacillus algifaecis sp. nov., isolated from decomposing algal scum.";
RL Int. J. Syst. Evol. Microbiol. 65:2194-2198(2015).
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; CP022657; ASS77249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A223D6N0; -.
DR KEGG; tab:CIG75_15550; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000214688; 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:UP000214688};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 94..162
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 184..564
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 580 AA; 67106 MW; DDEFEBDA8001DCB5 CRC64;
MYPTAEAWEA DYKKVQELLP SIATYRGRLH EGADILLEWM RLSEKIALTF DNVFVYAHMR
YHQNTGDSFY QGLSDRASML GAEVQSEMSF VNPELLGLPD GTLERYMEEK EELRLYKLVF
ERLLREKEHV LSPEVEELLA KVSEIADAPA TIFSMFANAD LKMPSVQDSE GKEYEVNEGR
YRNLLESKDR VLRERAMKAL FGTYGKFRNT LGATYNNNVK KNVFFAKARK YNSTLEAALS
GENIPVEVYN NLIAANHDNA KHLQRYLTLR KKVLGLEELH YYDFFVPMVE SIEMKIPWEQ
AKQMSLDALQ PLGEEYVATV QRAFDERWVD VYPNEGKRTG AYSWGTYTSS PYLFLNYTET
LDDVFTTVHE LGHSLHSYYT MKEQPFTYGN YTIFVAEVAS TLNENLLLSK MLREETDKKK
RMYLLTHSLD QYRSTMFRQT MFGEFEKIVH ELVEAGHPLN ADLLSEEYLK LNIKYYGTEL
VIDDELKHEW GRIPHFYDAF YVYKYATGFA AAAALARQIE TEGAPAIERY LDFLKKGSSE
DPIDLLKGAG VDMSSPQPIH DAFKVFVERL DELEALINEQ
//
