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Database: UniProt
Entry: S9U8C2_PAEAL
LinkDB: S9U8C2_PAEAL
Original site: S9U8C2_PAEAL 
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}.
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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
//
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