ID C0ZCY1_BREBN Unreviewed; 599 AA.
AC C0ZCY1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN OrderedLocusNames=BBR47_26630 {ECO:0000313|EMBL:BAH43640.1};
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH43640.1, ECO:0000313|Proteomes:UP000001877};
RN [1] {ECO:0000313|EMBL:BAH43640.1, ECO:0000313|Proteomes:UP000001877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599
RC {ECO:0000313|Proteomes:UP000001877};
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) 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; AP008955; BAH43640.1; -; Genomic_DNA.
DR RefSeq; WP_015890960.1; NC_012491.1.
DR AlphaFoldDB; C0ZCY1; -.
DR STRING; 358681.BBR47_26630; -.
DR KEGG; bbe:BBR47_26630; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_1_1_9; -.
DR Proteomes; UP000001877; 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; 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:UP000001877};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 114..183
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 208..585
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 599 AA; 67291 MW; 854A4E3A58693824 CRC64;
MKTRQTRDQV AVEYTWNLND LFESQEAWEQ ELAEIIQGLP VVTAFKGQLH KSGETLLACL
EANEAINVRA SVAATYARLR ASEDGTNPQN QANSARVGDV VSQLNAALSF IPSEILALPE
GKIESFLEEE PGLETFRKSL KDLLETKPYR LSAETEEAFA AMGEVFGAPY NIYLRGKLSD
MSFAPVHDGE GNERPVSFAL FETDYEMSSD TTLRRASYES FSKTLASYQN SFAAVYASEV
KRQTVMSRLR GYETVTDMLL KPQQVTLDMY HNILDIIGNE LAPHMRRYAK LKAKELGLEK
LAFCDLKTPL DPEFSPPITI EEAGKKILAS LQVMGPEYTA IMEKALNERW IDYVDNVGKS
TGAFCSTTYS KHSYILITWS GNMRSAFTLA HELGHCGHFM LATREQSFTN SRPSLYFIEA
PSTLNELLLA QHIVEQSDDP RLKRWVILQL MNTYYHNFVT HLLEARMQRK VYEAAQNDVP
LTAKQLSEWK GQVLADFWGD AVDLDDAASL TWMRQPHYYM GLYPYTYAAG LTASTAMAAS
IKQEGQPAVD RWIEVLKAGG TLTPLELMKK AGVDMSDPQP IREAVAYVGS LVDELERLF
//