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Database: UniProt
Entry: H3NI87_9LACT
LinkDB: H3NI87_9LACT
Original site: H3NI87_9LACT 
ID   H3NI87_9LACT            Unreviewed;       602 AA.
AC   H3NI87;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=HMPREF9708_00515 {ECO:0000313|EMBL:EHR37886.1};
OS   Facklamia languida CCUG 37842.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX   NCBI_TaxID=883113 {ECO:0000313|EMBL:EHR37886.1, ECO:0000313|Proteomes:UP000006190};
RN   [1] {ECO:0000313|EMBL:EHR37886.1, ECO:0000313|Proteomes:UP000006190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 37842 {ECO:0000313|EMBL:EHR37886.1,
RC   ECO:0000313|Proteomes:UP000006190};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Facklamia languida CCUG 37842.";
RL   Submitted (JAN-2012) 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:EHR37886.1}.
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DR   EMBL; AGEG01000003; EHR37886.1; -; Genomic_DNA.
DR   RefSeq; WP_006308542.1; NZ_JH601133.1.
DR   AlphaFoldDB; H3NI87; -.
DR   STRING; 883113.HMPREF9708_00515; -.
DR   PATRIC; fig|883113.3.peg.517; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_1_1_9; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000006190; 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   Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR   Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR004438; Peptidase_M3B.
DR   NCBIfam; TIGR00181; pepF; 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|RuleBase:RU368091};
KW   Metal-binding {ECO:0000256|RuleBase:RU368091};
KW   Metalloprotease {ECO:0000256|RuleBase:RU368091};
KW   Protease {ECO:0000256|RuleBase:RU368091};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006190};
KW   Zinc {ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          113..181
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          208..583
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   602 AA;  68581 MW;  A4F407126F3B1FB5 CRC64;
     MSNLPLRNEV PVDHTWDLSL LFSSQEAFEE AILNYHELLE TIQTYKGKLI NAEEIIDALS
     LYEKIITDFS KISHYGELAY EVDKLDPLKE ENNASVRNLR NKTGAATAFI RVEIAENNIE
     LLQSVMDSDE GKGYRVYIQD IIDHKDHILS EEMETFLGFV SSELFNQYQI YNTLMYQDLS
     FADFSAGGKT YSNSFAGFEG EYEVDLKAEV RHNAWKSFHA GLSKYQNTAA INYISHTQTE
     KKLSLERGYE SVFDYLLADQ GIDRSTYDKH IDLLMTEFAP VMQRYARLLK EKHGLDTMSL
     ADIKIPYSTD SGHNLSISEG EEIVKKALSV YGPDYNAYVD RAFNERWIDF PMNQTKTTGG
     FSTTVPGGPS YVLLNWTGYL SEALVLAHEL GHSSHFQLTY QNQSVLSPEV SLYFVEAPST
     CNEVITCQYL LNGDLSHEDK IGLIGEFISR TYFHNMVTHL LEADFQRKVY QAVDRFENLN
     ADKLNRFFYD TLKKFWGDAL EINEGAELTW MRQPHYFMGL YSYTYSAGLT IGTQVGLKIA
     NQDQEVIENW LTALKAGSSL NPLELTNYVG VDMSTPDALR ATIQYVSSLV DHLEEDCNMT
     NA
//
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