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Database: UniProt
Entry: A0A0H5CTP8_9PSEU
LinkDB: A0A0H5CTP8_9PSEU
Original site: A0A0H5CTP8_9PSEU 
ID   A0A0H5CTP8_9PSEU        Unreviewed;      1092 AA.
AC   A0A0H5CTP8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Serine protease, subtilase family {ECO:0000313|EMBL:CRK61404.1};
DE            EC=3.4.21.- {ECO:0000313|EMBL:CRK61404.1};
OS   Alloactinosynnema sp. L-07.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae.
OX   NCBI_TaxID=1653480 {ECO:0000313|EMBL:CRK61404.1, ECO:0000313|Proteomes:UP000076116};
RN   [1] {ECO:0000313|Proteomes:UP000076116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-07 {ECO:0000313|Proteomes:UP000076116};
RA   Ramaraj T.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
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DR   EMBL; LN850107; CRK61404.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H5CTP8; -.
DR   STRING; 1653480.gene:80950302; -.
DR   KEGG; alo:CRK61404; -.
DR   Proteomes; UP000076116; Chromosome i.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02120; PA_subtilisin_like; 1.
DR   CDD; cd04852; Peptidases_S8_3; 1.
DR   Gene3D; 2.60.40.2310; -; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034197; Peptidases_S8_3.
DR   InterPro; IPR045051; SBT.
DR   InterPro; IPR041469; Subtilisin-like_FN3.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   PANTHER; PTHR10795:SF468; SUBTILISIN-LIKE PROTEASE SBT3.18; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 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:UP000076116};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1092
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005217845"
FT   DOMAIN          203..636
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          449..517
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          688..765
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        211
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        286
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        600
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1092 AA;  111578 MW;  19BFBD95E0D7D722 CRC64;
     MRRSRCARAA VLAMVLPISL VTSGGEAVAA PTLGAEPLTP ADRVTADKSP TSRLAKTDAS
     LLGRTDAMLI PVVIKLDYDS LATYAGGRRG LEATSPSVTG KKLKDKTAAQ QKYEAFAAGQ
     EQAFKAELAT RAPQAAVGTS LRVVYGGVSA RVPANKISDI LAIPNVVAVQ ADDPNHLLTD
     SSPDFIGAPS SYNRLGTTAG AGTGVLYGNL DSGVWPEHPS FADLGNLAAP PGPARVCDYG
     DNPLTPANDP FACQRKLVGG AAFTQTYDLV LGDDVFAGTA RDSNGHGTHT ASTSAGNIVN
     NVSVLGRAQA PIHGIAPGAW VMEYKVCGPQ GCFPSDTTAA VGQAILDGVD VINYSISGGE
     DPFTDPTELA FLDAYAAGLF VAASAGNSGP AAGTSNHLSP WVTTVAASTQ RREFASTLTI
     TADNGDTFTA DGASITPGAG PAQIVLASAA PYSNALCTTP APAGLFTGKI VACQRGPGRV
     AKGFNVLQGG AAGMVLFNPS RADALTDTHW LPAVHLPDGT SMLAFLGSHT GETARFTAGQ
     SRSGQGDVMA AFSSRGPGGN FIKPDVTAPG VQILAGDTPI VESVASGPGG ELFQAIAGTS
     MSSPHTAGAA ILLKAINPGW TPGQIKSGLM STATTAVVKE DRSTPADPFD MGSGRIDLRQ
     AWAPGITFDE TAANMALLAN DPVNAVHLNV PSVNTNVMPG RLTTVRTAKN VSGLKQKYTV
     STTAPAGAKI TVLPKKFSLD PGQSAQLSIT IESQAPAAQF FGQIRLVPDS PQFPALHLPV
     AFKTGQSHVT LASECAPTQI AVNATSTCTV TATNTSFTDT TVDLTTRLSN QLKVVSASNA
     TVVDKRTVHK TGVTVAGALP GVPSVDAGEL FGYIPLTAFG VTPVPIGDEE IINFNVPAFV
     YNGVTYSRVG VDSNGYLVVG GGTADDNNCC SLPTGPSPAR PNNILAPFWT DLDGTGAPGV
     YAAVLTDGVN SWLVFEYRVN VFGTTSGRTF QVWIGVNGTQ DITFAYNPAA LPADPGQPFL
     VGAENEFGGG DIAAVLPTDD LRVTSTVPVP GASVSYTVTV VGTEPGAGRV TTEMTGAGLP
     GTTVVTSVVA IE
//
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