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Database: UniProt
Entry: H3SCH1_9BACL
LinkDB: H3SCH1_9BACL
Original site: H3SCH1_9BACL 
ID   H3SCH1_9BACL            Unreviewed;       596 AA.
AC   H3SCH1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:EHQ63245.1};
GN   ORFNames=PDENDC454_06044 {ECO:0000313|EMBL:EHQ63245.1};
OS   Paenibacillus dendritiformis C454.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ63245.1, ECO:0000313|Proteomes:UP000003900};
RN   [1] {ECO:0000313|EMBL:EHQ63245.1, ECO:0000313|Proteomes:UP000003900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C454 {ECO:0000313|EMBL:EHQ63245.1,
RC   ECO:0000313|Proteomes:UP000003900};
RX   PubMed=22461558; DOI=10.1128/JB.00158-12;
RA   Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA   Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA   Gutnick D.L., Lancet D., Ben-Jacob E.;
RT   "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT   dendritiformis C454 Chiral Morphotype.";
RL   J. Bacteriol. 194:2127-2128(2012).
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:EHQ63245.1}.
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DR   EMBL; AHKH01000010; EHQ63245.1; -; Genomic_DNA.
DR   RefSeq; WP_006675722.1; NZ_AHKH01000010.1.
DR   AlphaFoldDB; H3SCH1; -.
DR   STRING; 1131935.PDENDC454_06044; -.
DR   MEROPS; M03.A08; -.
DR   PATRIC; fig|1131935.3.peg.1211; -.
DR   OrthoDB; 9769691at2; -.
DR   Proteomes; UP000003900; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09607; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR034006; M3B_PepF_2.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR011977; Pept_M3B_clade3.
DR   InterPro; IPR001333; Peptidase_M32_Taq.
DR   NCBIfam; TIGR02290; M3_fam_3; 1.
DR   PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR   PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 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:RU003435};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003900};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          119..181
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          204..580
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   596 AA;  67266 MW;  0CA0DCE894908CAC CRC64;
     MQHPLNPTWD LESIFPGGSD SEALQQSFAA IEQDLALLKG ELKEMSSPLS KDSIPALAKL
     TTRLQDLNRR MQEAGAFISC LTAQNLQDKK AVQLTGRKSA LSAQLVAIDA LYDELLRGMP
     DELWSRFLAL PEIEGVGFNL NERRETAKEK LGPALEALAG DLAVDGYHGW AEMYNTIVSH
     VRINYEENGV NQQLSAGQAH NKLSHPDRRV REEMFKLWEQ EWSDKADFCA DALNHIAGFR
     LKLYERRGWD DVLKEPLARN RMSQATLGAM WDTIVRNKPK FVQYLERKAK LLGVEKLSWC
     DVDAPIGGSQ TTISYDDGAD AIVEQFRKFS PRMADFAVRA FENRWIEAED RPGKRPGGFC
     TSLPVSNQTR IFMTYAGTPS NVSTLAHELG HGYHQHVMEG LPAFAQRYAM NVAETASTFA
     EMIVADSAVK GAKDEQEKLG LLEDKIQRSI AFYMNIHARF LFETRFYEKR KAGLVSSEQI
     CALMEEAQQE AYCGALGSLH PHFWASKMHF YFTHVPFYNF PYTFGYLFST GLYARALEEG
     ESFAAKYDAL LRDTAVMTVE DLASKHLGVD LTKPDFWQSA INVTLKDVEL FLQMTE
//
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