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
//