ID   Q2BBF8_9BACI            Unreviewed;       582 AA.
AC   Q2BBF8;
DT   04-APR-2006, integrated into UniProtKB/TrEMBL.
DT   04-APR-2006, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Oligoendopeptidase F, peptidase M3 family protein {ECO:0000313|EMBL:EAR67165.1};
GN   ORFNames=B14911_16670 {ECO:0000313|EMBL:EAR67165.1};
OS   Bacillus sp. NRRL B-14911.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=313627 {ECO:0000313|EMBL:EAR67165.1, ECO:0000313|Proteomes:UP000004554};
RN   [1] {ECO:0000313|EMBL:EAR67165.1, ECO:0000313|Proteomes:UP000004554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-14911 {ECO:0000313|EMBL:EAR67165.1,
RC   ECO:0000313|Proteomes:UP000004554};
RA   Siefert J., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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:EAR67165.1}.
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DR   EMBL; AAOX01000005; EAR67165.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2BBF8; -.
DR   HOGENOM; CLU_030403_3_0_9; -.
DR   Proteomes; UP000004554; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09606; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR011976; Pept_M3B_oligopep-rel.
DR   NCBIfam; TIGR02289; M3_not_pepF; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF48; PUTATIVE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          189..547
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   582 AA;  67799 MW;  F2208BCD068A21CB CRC64;
     MIIETIKIIQ RGKGSYFMTQ EVKSNYYKEL IDLQDAEGVE AQLQALLEVP IDSVSDLENW
     LKDEKELGIK IDEAMTGHQV DFYRNTEDAD IKSTYLHDQQ VIQPLLMKYE AKMNEKFCES
     PYAAQLDDKR YGLMRRVRES KVKLFREENI PLMVKEQELS TKYSEIIAGL TVEWDGEEKP
     YPFIQSQLDN LDRSVREKAY YAMLEAHRQI KPDMDSIMDE LVQLRHQIAL NAGFENYRDY
     MFVVKNREYT IQDCYDFHEN VEKHIIPAWN RLAEVFKSKL GVDAYRPWDN TAKLMKNPPY
     TEVSDLMDGV SEMLGKTDPY FADRFDYMRE NGLLDLGDRK GKSPGGFCTT LSVSGDTFVF
     ANFSPSFFSL IALIHEMGHA VNGYLEFAEH GPLEEHQHRM EVAELYSHGM ELLLLDKLDR
     FYPEEEDFKS AQREELRRAF TMLYGPLSGD LFQHWMYTNP NHTAKERDEK YFEIAKRYGL
     SPVDTSGLED VMGILWADTL HYFQVPFYNI EYSISMLGSL QILENYHNNP EQAVELFKKG
     ASADYNQSIA DIYKETGVSF DFSESAVKRM GEFLEKVIQD IH
//