ID A0A0A8EYY9_9ACTN Unreviewed; 354 AA.
AC A0A0A8EYY9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Peptidase alpha-lytic pro domain protein {ECO:0000313|EMBL:AJC59356.1};
GN ORFNames=GZL_06789 {ECO:0000313|EMBL:AJC59356.1};
OS Streptomyces sp. 769.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1262452 {ECO:0000313|EMBL:AJC59356.1, ECO:0000313|Proteomes:UP000031113};
RN [1] {ECO:0000313|EMBL:AJC59356.1, ECO:0000313|Proteomes:UP000031113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=769 {ECO:0000313|EMBL:AJC59356.1,
RC ECO:0000313|Proteomes:UP000031113};
RA Du Q., Wang Q., Li Q., Wang L., Zhang Z., Ren J., Wang J., Wang M.;
RT "Complete Genome Sequence of Streptomyces gongzhulingensis.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; CP003987; AJC59356.1; -; Genomic_DNA.
DR RefSeq; WP_039637710.1; NZ_CP003987.1.
DR AlphaFoldDB; A0A0A8EYY9; -.
DR KEGG; stre:GZL_06789; -.
DR HOGENOM; CLU_030648_0_1_11; -.
DR Proteomes; UP000031113; Chromosome.
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; 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; IPR006311; TAT_signal.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF02983; Pro_Al_protease; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001134; Streptogrisin; 1.
DR PRINTS; PR00861; ALYTICPTASE.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001134-2};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..354
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002051124"
FT DOMAIN 96..151
FT /note="Peptidase S1A alpha-lytic prodomain"
FT /evidence="ECO:0000259|Pfam:PF02983"
FT DOMAIN 192..345
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT ACT_SITE 200
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 310
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT DISULFID 181..201
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 304..331
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
SQ SEQUENCE 354 AA; 36160 MW; CBFF48EF35193FE6 CRC64;
MKHRRIPHRR TVLASAGALA LAATATVTLA NAHAAPAPSV ATLSPAAATT LASQLKTGTA
GAFYDAKAQK LVVNVVDEAS AAAVRAKGAE ARIVKHSMAQ LDAARQTLKT GATIPGTAWA
MDPKANKVVV TADRTVTGAK LDRLTKVAKG LGDTVEIRHS QGEFKPLIAG GDAIWGSSAR
CSLGFNVTKG GQPYILTAGH CGNAVQEWSD QQGGQTIATT EDSKFPGNDY SIAKYTGNTD
HPSEVDLYNG STQKITKAAE ATVGEKVQRS GSTTQVHDGT VKGLNATVNY QEGTVNGLID
TDVCAEPGDS GGALFDGESA LGLTSGGSGD CTNGGETFFQ PVPAALQATG TQIG
//
