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Database: UniProt
Entry: S2Y1Y8_9BACL
LinkDB: S2Y1Y8_9BACL
Original site: S2Y1Y8_9BACL 
ID   S2Y1Y8_9BACL            Unreviewed;       606 AA.
AC   S2Y1Y8;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=HMPREF1210_02025 {ECO:0000313|EMBL:EPD51427.1};
OS   Paenisporosarcina sp. HGH0030.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae;
OC   Paenisporosarcina.
OX   NCBI_TaxID=1078085 {ECO:0000313|EMBL:EPD51427.1, ECO:0000313|Proteomes:UP000014412};
RN   [1] {ECO:0000313|EMBL:EPD51427.1, ECO:0000313|Proteomes:UP000014412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGH0030 {ECO:0000313|EMBL:EPD51427.1,
RC   ECO:0000313|Proteomes:UP000014412};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA   Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Paenisporosarcina sp. HGH0030.";
RL   Submitted (MAY-2013) 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:EPD51427.1}.
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DR   EMBL; AGEQ01000011; EPD51427.1; -; Genomic_DNA.
DR   RefSeq; WP_016428533.1; NZ_KE150421.1.
DR   AlphaFoldDB; S2Y1Y8; -.
DR   PATRIC; fig|1078085.3.peg.2009; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_1_1_9; -.
DR   Proteomes; UP000014412; 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   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   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:UP000014412};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          115..181
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          206..583
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   606 AA;  69297 MW;  4066DCDAD74B16D8 CRC64;
     MVQSLPARSD VKREETWNLQ DLFTSEEAYQ DALVALEKEV DAFHQQFKGQ IKDAHSAEEA
     LKGYESLYKM FVPLGTYAGL AYSTDQTDSD AQMRSARFGS VSASLSSKLS FVDSELLELP
     VEVLEEAMKN STEFGHYLKK LIRKKPHQLH PEVEKVLAAY SSSFDGPYEL YNTTKMVDLS
     FEDFEVNGKK YPLSYVLFEG DWEAETDTDV RRAAFKAFSN QLKNYQHTTA KTYDMNLQIE
     KTTSDLRGYD NIFDYLLFGQ EVDKSLFDRQ IDLIMTELAP HMRKYAKLLQ DVHGLEEMTF
     ADLKIPLDPS YEPKITIEES KKYMNDALAI LGDDYLDMVN RSFDERWIDF AQNKGKSTGA
     FCSSPYGFHP YILISWSSRM NEVFVLAHEL GHAGHFYNAH KNQNVFNSRP SLYFIEAPST
     MNEMLMANHL LENSDDPKFK RWVISSIVAR TYYHNFVTHL LEAAYQRKVY ERVDAGKNVN
     AGILNEIKRD VLEEFWGDAV EITPGAELTW MRQPHYYMGL YPYTYSAGLT ISTQVSKRIL
     EEGEPAVAQW LEVLQAGGTK SPVELAQMAG VDITTEQPLR DTIAYIGELI DELVKLTKEI
     EAVPAK
//
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