ID A0A1E5Q1L4_9ACTN Unreviewed; 572 AA.
AC A0A1E5Q1L4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Protease {ECO:0000313|EMBL:OEJ35462.1};
GN ORFNames=BGK67_04105 {ECO:0000313|EMBL:OEJ35462.1};
OS Streptomyces subrutilus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36818 {ECO:0000313|EMBL:OEJ35462.1, ECO:0000313|Proteomes:UP000095705};
RN [1] {ECO:0000313|EMBL:OEJ35462.1, ECO:0000313|Proteomes:UP000095705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-1-1 {ECO:0000313|EMBL:OEJ35462.1,
RC ECO:0000313|Proteomes:UP000095705};
RA Chen X.;
RT "The complete genome of Streptomyces subrutilus 10-1-1.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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:OEJ35462.1}.
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DR EMBL; MEHK01000001; OEJ35462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5Q1L4; -.
DR STRING; 36818.BGK67_04105; -.
DR Proteomes; UP000095705; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07496; Peptidases_S8_13; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034176; Peptidases_S8_13.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000095705};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 452..572
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 397
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 572 AA; 57152 MW; 03BFD04FD461C7FB CRC64;
MAVAADVPAS SAAAAATTTA PVENLIVGYK TSASEASSNT AAADDATAKG KKAGKKAKFD
RRLGTGAALV SLGSATAPAD AAKVMAQFRA DPDVAYVEVD ARAYAMATPN DTEYTKQWDL
FEPTAGMNVP AAWDKTTGSG VTVAVIDTGY VAHSDLAANV VAGYDFISNA SYARDGGGRD
GNPADEGDWN ATDNECGLGS KAGGSSWHGT HVAGTIAAAT NNGKGIAGIA YGAKIQPVRV
LGKCGGTTSD IADAITWASG GTVSGIPANA TPAKVINMSL GGSGACSATY QNAINGAVSR
GTTVVVAAGN SNSDAAGFTP ASCNNVINVA ASNRTGDRSF YSNYGASIDV AAPGGETRRG
TDTPGTVTTP ENGILSTLNA GTTTPGAENY KPYQGTSMAA PHVAGLAALA KAAKPSLTPA
QIEAAIKNNT RPLAGVCTGG CGTGLADAAA TINAVTTTTP TGLENGADYT IGDNTTVESP
ITVTGKTGNA PATLKVAVNI AHTYIGDLKV DLIAPDGTAY NLHNRTGAGT DNINQTYTVN
ASAEVANGTW KLRVNDNAGG DTGKIDYWSL TF
//