ID A0A0H3DXU2_BACA1 Unreviewed; 670 AA.
AC A0A0H3DXU2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN OrderedLocusNames=BATR1942_03410 {ECO:0000313|EMBL:ADP31636.1};
OS Bacillus atrophaeus (strain 1942).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=720555 {ECO:0000313|EMBL:ADP31636.1, ECO:0000313|Proteomes:UP000006867};
RN [1] {ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|Proteomes:UP000006867};
RA Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., Bruce D.,
RA Karavis M., McGregor P., Hong C., Park K.H., Akmal A., Feldman A.,
RA Lin J.S., Chang W.E., Higgs B.W., Demirev P., Lindquist J., Liem A.,
RA Fochler E., Tapia R., Bishop-Lilly K., Detter C., Han C., Sozhamannan S.,
RA Rosenzweig C.N., Skowronski E.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADP31636.1, ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|EMBL:ADP31636.1,
RC ECO:0000313|Proteomes:UP000006867};
RX PubMed=21464989; DOI=10.1371/journal.pone.0017836;
RA Gibbons H.S., Broomall S.M., McNew L.A., Daligault H., Chapman C.,
RA Bruce D., Karavis M., Krepps M., McGregor P.A., Hong C., Park K.H.,
RA Akmal A., Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA Lindquist J., Liem A., Fochler E., Read T.D., Tapia R., Johnson S.,
RA Bishop-Lilly K.A., Detter C., Han C., Sozhamannan S., Rosenzweig C.N.,
RA Skowronski E.W.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus var. globigii, a historical biowarfare simulant.";
RL PLoS ONE 6:E17836-E17836(2011).
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; CP002207; ADP31636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H3DXU2; -.
DR KEGG; bae:BATR1942_03410; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_2_0_9; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000006867; 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 Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..670
FT /note="Oligoendopeptidase F"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038762279"
FT DOMAIN 181..250
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 271..651
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 670 AA; 77492 MW; E9CC3AB38E44C18A CRC64;
MKGKKRSVFR FFTVFLACVV FFTAYDLTNG SEKPEDNHNT SLLRNSRFFN WLELKKTRGI
TMTEEKKANQ LPDRSEAKAE DTWKLEDIFP SDEAWNKEFQ AVKELIPNLS EFKGTLDHSA
DNLYEALTYQ DKVMERLGKL YTYAHMRSDQ DTGNSFYQGL NDKAANLYTQ AASATAYMVP
EILSIQEEKL QQFLLEKEEL KLYSHAIEEI TKERPHVLSE KEEALLAEAS EALSSSSNTF
SVLNNADITF PSIKDENGQE KQITHGNFIN FLESENREVR KNAFEAVYKT YGQYKNTMAT
TLSGTVKKDN FYARVKKYKS AREAALSNNS IPEEVYDNLI KTINKHLPLL HRYIELRKKV
LELDEVHIYD LYTPLVKDAG MKVTYDEAKE YMLKGLAPLG DEYASILKEG LENRWVDVYE
NKGKRSGAYS SGTYGTNPYI LMNWHDNVNN LFTLVHEFGH SVHSYYTRKH QPYQYGNYSI
FVAEVASTTN EALLGEYMLN NLKDEKQRLY LLNHMLEGFR GTVFRQTMFA EFEHQIHMKA
QEGEPLTPEL LSSMYYDLNK KYFGDNMVID KEIGLEWSRI PHFYYNYYVY QYATGYSAAQ
ALSSQILKEG KPAVDRYVDF LKAGSSEYPI DILKKAGVDM TSPEPIEAAC KMFEEKLDEM
EELLLKVKHS
//
