ID A0A368VVG0_9ACTN Unreviewed; 386 AA.
AC A0A368VVG0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Streptogrisin C {ECO:0000313|EMBL:RCW45276.1};
GN ORFNames=DFQ14_103244 {ECO:0000313|EMBL:RCW45276.1};
OS Halopolyspora algeriensis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetes incertae sedis;
OC Halopolyspora.
OX NCBI_TaxID=1500506 {ECO:0000313|EMBL:RCW45276.1, ECO:0000313|Proteomes:UP000253495};
RN [1] {ECO:0000313|EMBL:RCW45276.1, ECO:0000313|Proteomes:UP000253495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8575 {ECO:0000313|EMBL:RCW45276.1,
RC ECO:0000313|Proteomes:UP000253495};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-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:RCW45276.1}.
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DR EMBL; QPJC01000003; RCW45276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368VVG0; -.
DR OrthoDB; 8781117at2; -.
DR Proteomes; UP000253495; 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; -; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000253495};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..386
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039340252"
FT DOMAIN 124..180
FT /note="Peptidase S1A alpha-lytic prodomain"
FT /evidence="ECO:0000259|Pfam:PF02983"
FT ACT_SITE 231
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 259
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT ACT_SITE 340
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-1"
FT DISULFID 215..232
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 298..308
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
FT DISULFID 334..361
FT /evidence="ECO:0000256|PIRSR:PIRSR001134-2"
SQ SEQUENCE 386 AA; 40279 MW; 005087A411FFDB47 CRC64;
MSRKRTIRLA GAVLLATGTA TALATPSVAN PQTAEADSPK PVASAAMAEA MQRDLGLTAE
QAQTRLAQET KARNAEDTLR QSLGNSFGGA FFDAERGKLV VGTTDASEKS AVRSAGAVAK
VVPNSKQELN AAKAELDRME GSAPDSITGW YVDTRSNSVV VNVNKTKRDA ETNKFLARAR
SVDESVRVEQ VKRSPRTLYN LIGGDAYYMG SGGRCSVGFP LQGGGMVTAG HCGDTGTSAS
GHNQVHMGYF QGSSFPGNDY AWVSANSSWT SKPWVNMYNG YARTVAGSQE APVGSSICRS
GSTTGWHCGT VEAKNQTVRY SQGAVYGLTR TDVCAEPGDS GGSFISGNQA QGMTSGGSGN
CTLGGTTFFQ PVNEALNAYG LQLATN
//
