ID E0I9F9_9BACL Unreviewed; 546 AA.
AC E0I9F9;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN ORFNames=PaecuDRAFT_2296 {ECO:0000313|EMBL:EFM11043.1};
OS Paenibacillus curdlanolyticus YK9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM11043.1, ECO:0000313|Proteomes:UP000005387};
RN [1] {ECO:0000313|EMBL:EFM11043.1, ECO:0000313|Proteomes:UP000005387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK9 {ECO:0000313|EMBL:EFM11043.1,
RC ECO:0000313|Proteomes:UP000005387};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1B family.
CC {ECO:0000256|ARBA:ARBA00008764, ECO:0000256|RuleBase:RU004296}.
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DR EMBL; AEDD01000005; EFM11043.1; -; Genomic_DNA.
DR AlphaFoldDB; E0I9F9; -.
DR STRING; 717606.PaecuDRAFT_2296; -.
DR eggNOG; COG1864; Bacteria.
DR eggNOG; COG3591; Bacteria.
DR Proteomes; UP000005387; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00091; NUC; 1.
DR Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR040255; Non-specific_endonuclease.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR008256; Peptidase_S1B.
DR PANTHER; PTHR13966:SF5; ENDONUCLEASE G, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13966; ENDONUCLEASE RELATED; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00839; V8PROTEASE.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SUPFAM; SSF54060; His-Me finger endonucleases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:EFM11043.1};
KW Hydrolase {ECO:0000256|RuleBase:RU004296};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR640255-2};
KW Nuclease {ECO:0000313|EMBL:EFM11043.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004296};
KW Reference proteome {ECO:0000313|Proteomes:UP000005387};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004296}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 318..524
FT /note="DNA/RNA non-specific endonuclease"
FT /evidence="ECO:0000259|SMART:SM00892"
FT DOMAIN 319..526
FT /note="Extracellular Endonuclease subunit A"
FT /evidence="ECO:0000259|SMART:SM00477"
FT ACT_SITE 66
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT ACT_SITE 112
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR640255-1"
FT BINDING 414
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR640255-2"
SQ SEQUENCE 546 AA; 61954 MW; F9B5684A404AE34A CRC64;
MLDTHDNLAL ERVLGLSDIF PIHYLEKGLQ VAKSICRIVI KDDSGRSIGY GTGFLVAPTL
LLTNNHVFPN TETALRSSAQ FNYELDLQFN ARVVQEFRFQ PNELFITNQD LDFTLVAVQP
ISISGARIQE FGYLPLIKQT GKALLGEYVS IIQHPKGDYK AVVIRENKIT DMLDHFIHYS
ADTEPGSSGS TVFNDQWQVI ALHHSGVPDP NHDGQFIANE GVRISSILND IEQKKPTLST
KQQTLLQGLG EEIAFATQPI DNDESVVAED FDIERFEAMT GYDPQFLGER NTIAHPTLRS
DLKADVAELN NGNGSILNYT HFSIVMSKSR RLAFYTVVNI DGKQLKDVGR SDNWRYDPRI
DRKYQVGNEL YQQNPFDRGH LVRRRDPIWG PDAATANDDT FHFTNCSPQH ERFNQNPELW
LGLEDYILHH TDNNKMKATV FNGPVFREND IVYRGIKIPE EYWKVAVMVK DNGETSATAY
LVSQKELIRN LEAEPFGAFR TFQVKVSLIE SMTGLNFGEL SKFDPLERTE ATTLGHLLER
VEDIQL
//
