ID S9U8C2_PAEAL Unreviewed; 801 AA.
AC S9U8C2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Protease {ECO:0000313|EMBL:EPY06775.1};
GN ORFNames=PAALTS15_12867 {ECO:0000313|EMBL:EPY06775.1};
OS Paenibacillus alvei TS-15.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1117108 {ECO:0000313|EMBL:EPY06775.1, ECO:0000313|Proteomes:UP000015344};
RN [1] {ECO:0000313|EMBL:EPY06775.1, ECO:0000313|Proteomes:UP000015344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TS-15 {ECO:0000313|EMBL:EPY06775.1,
RC ECO:0000313|Proteomes:UP000015344};
RA Strain E.A., Brown E., Allard M.W., Luo Y.L.;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC 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:EPY06775.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ATMT01000052; EPY06775.1; -; Genomic_DNA.
DR RefSeq; WP_021259915.1; NZ_ATMT01000052.1.
DR AlphaFoldDB; S9U8C2; -.
DR PATRIC; fig|1117108.3.peg.2667; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG4733; Bacteria.
DR Proteomes; UP000015344; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd12214; ChiA1_BD; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
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; IPR034058; TagA/B/C/D_pept_dom.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00495; ChtBD3; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023024};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
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..801
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004558268"
FT DOMAIN 664..749
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 455
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 801 AA; 85952 MW; 91F5972C8F940731 CRC64;
MANKNNKKVL SMIMSIAMAI SLMSPAVSAY EDPANSSTEK LLYLRTGTVD LQNENEHYGL
QHDEESTQRQ LYVVQFNDVI TDSSKQLLQQ AGAELGDYLP DYAYLVRMNS QQAGTLAAND
QIYRVTLFQP EWKNGNLSTS ENTSPSNYVI SVFRGSEAEV AQSLKQQAIP VTDVQEGYIE
AVLSNESLPL VLNQPDVTFV ESKPNEELLN DFVTNQVGAA TSNGVWSKGL TGKGQVVTVA
DSGLDSGNLS TLHKDFEGQL HKTPVPNPEG TWKDTIGHGT HVAGTVLGTG AMSNGKYKGV
AYGAKLFVQT IGCGGTSICP GDLRDLFGSA KQQGSFIHTN SWGASSYSYN SNSARADEYT
FNNKDFTVLF AAGNDGSGNN TINSPGNAKN TITVGNLQKT NSNQIAPTSS RGYATDGRVK
PDLVVTGTSI ISARSSASTR PANPNQYYTN MTGTSMATPA VAGSAAIVRQ FYTENKHVTP
SSALIKATLI NGAEDVGYGW MSRETGWGRV NLVNSLTPTD GRTNNFIDNT TGIKTNDSIS
YRVKAEAGKP LKISLVWSDY QGAVQAGKQL VNDLDLEVKT PTGELYKGNC FAQNTASTSC
ANYDHINNVE NAYLSTPTTG EYTVTIKGYN VPQGPQPFAL VVSGNHSSIL GQGPEQPEPI
VLKAPEQLAV TAVTYNSVNL NWSDPNTGIQ GLTYEIYQQQ QKIGTSNQTN YVVTGLSPGN
TYTFTVRIID GKGNVSPNSQ SVTAKLPNSE GNTDPWQAGK AYKAGDLVSY NGVTYKCVQP
HTSLTGWEPS NVPALWSPVQ K
//