ID A0A3E0HVN7_9PSEU Unreviewed; 385 AA.
AC A0A3E0HVN7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Streptogrisin C {ECO:0000313|EMBL:REH50340.1};
GN ORFNames=BCF44_104617 {ECO:0000313|EMBL:REH50340.1};
OS Kutzneria buriramensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1045776 {ECO:0000313|EMBL:REH50340.1, ECO:0000313|Proteomes:UP000256269};
RN [1] {ECO:0000313|EMBL:REH50340.1, ECO:0000313|Proteomes:UP000256269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45791 {ECO:0000313|EMBL:REH50340.1,
RC ECO:0000313|Proteomes:UP000256269};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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:REH50340.1}.
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DR EMBL; QUNO01000004; REH50340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E0HVN7; -.
DR OrthoDB; 8781117at2; -.
DR Proteomes; UP000256269; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd21112; alphaLP-like; 1.
DR Gene3D; 3.30.300.50; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR004236; Pept_S1_alpha_lytic.
DR InterPro; IPR001316; Pept_S1A_streptogrisin.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR035070; Streptogrisin_prodomain.
DR Pfam; PF02983; Pro_Al_protease; 1.
DR PIRSF; PIRSF001134; Streptogrisin; 1.
DR PRINTS; PR00861; ALYTICPTASE.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001134-2};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..385
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039713847"
FT DOMAIN 129..178
FT /note="Peptidase S1A alpha-lytic prodomain"
FT /evidence="ECO:0000259|Pfam:PF02983"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 258
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 339
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT DISULFID 209..230
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 297..307
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 333..360
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
SQ SEQUENCE 385 AA; 38668 MW; A783944FAF0E3C33 CRC64;
MNRTRAARIT GAALLSFGLA ATVSVPAAAT SAPVSVDTST NGVVISPDVA SALRRDLGLS
PARARDLFAR QNRADVQVAT LRTALGPIFA GSWFDAAAGE AVVAVTDVTF VPSVRAAGVE
ARVVPRTDAQ LTAVAEGLNA RPAPAGVAGW YVDLPSDQVV VQVLDHSGPT ESFVAAAGPA
VREETVAARP RPLYAVRGGD AWYGPDFRCS VGFAATDGGG GKHFVTAGHC TAGGGTAFGY
NRVSLGRSSG SHFGSGGDFG KVDITSDQWT LAGLVINGGG TVAVRGSAEA AVGAAVCRSG
STSGWHCGVI QAKNQTVVYS EGTVTGLTRT NVCAEPGDSG GAWISGNQAQ GVTSGGSGDC
THGGTTYFSP VNPALSAYGL RLVTS
//
