ID A0A1I7LY27_9BURK Unreviewed; 1062 AA.
AC A0A1I7LY27;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidase inhibitor I9 {ECO:0000313|EMBL:SFV14612.1};
GN ORFNames=SAMN05216552_10438 {ECO:0000313|EMBL:SFV14612.1};
OS Pseudoduganella namucuonensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Pseudoduganella.
OX NCBI_TaxID=1035707 {ECO:0000313|EMBL:SFV14612.1, ECO:0000313|Proteomes:UP000199391};
RN [1] {ECO:0000313|Proteomes:UP000199391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11014 {ECO:0000313|Proteomes:UP000199391};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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 ECO:0000256|RuleBase:RU003355}.
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DR EMBL; FPBO01000043; SFV14612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7LY27; -.
DR STRING; 1035707.SAMN05216552_10438; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000199391; 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; cd02120; PA_subtilisin_like; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 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; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
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; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 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:UP000199391};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1062
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011694289"
FT DOMAIN 68..130
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 157..666
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 460..535
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 724..815
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 239..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 625
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1062 AA; 108946 MW; 88647B8D1397023F CRC64;
MKLRPVSIAV LALLASMAHT AQADDTRRPY IVQLAAQPIA SYNGGVAGLP ATQPSPGSRL
LMLSPAVQQY TQYLDQKRGS VQAVVANAPI QHEYKVVLNG FSAMLTDDEV RQLQANPDVA
QIEADMPRSL QTSYTTSFLG LDQPGGVWSQ LNGTAKGEDV VVGIIDSGVW PENLSYADRV
DGDGKPTFDV GGTLAYNAPA GWNGACESGE GFTASHCNNK LIGARFFNAT FEAQNPGNTH
WTEFRSPRDS AAGAAGEGSH GTHTSSTAAG NGGVATSVNG IPMPGLISGM APRARVAVYK
VCWSYTVPVT AEEPNGVKNS CFGSDSVAAI ERAIADGVHV LNYSISGGES YTDSVEQAFL
NAANAGIFVS ASAGNSGPAN MVAHVSPWLT TVGASTHGRE LKATLTLGNG GQYSGLSVSN
NALPPAGLIR AEDAALPGAS AEYKNYARLC YRDNDVKPNT TIPVGPVFDT SKTAGKIVVC
TRGTTGRVDK GSAVLAAGGA GMVLVNAAAS GAGSDLYSDF HVLPAVHVTA GTGAPILAYA
GGAGATASLS RFFADLNSAP APMMADFSSR GPNRYDPNLL KPDVTAPGVA ILAGGSAALS
QSERDAVSNG TLQPSQAYTF MQGTSMSSPH VAGLAALLRQ LHPTWSPAAI KSALMTTGTM
TKDDGLTGAQ NGRLPWSQGA GHVNPNKAMD PGLVYDLSAS DYKKYMCGGG VASQCAEGAI
PGYELNLPSI TLSNVQVSQT VTRRVTNVSG AASTYTATPS ITGYTMEVTP STLTLNPGET
KSYSVKLTRT NAPNNTWQFG ELVWSDGVHS VRSPVQAQSG KAVTAPAIVS SDRTTGNRAL
GLSVGFTGKL GALKGGLKEV TRSVQNVAQA IEGSVDDAAM AAKACKDGAQ GARGTDFTFP
AGTVAARFET FNRDTVGGAA NDLDMVLIGG AGTALAYSGR AGSTEAITLA SPPAGSYRVC
VIGYAAANGV STDYTLSSAI VTTADVGGNF KVMLPSKVIA GSSATVGASW SGLALGKRYL
GGVQFLDQNN TLSATTLFNV ETSVLIPEPA AVAREKKRDT GL
//
