ID A0A1Z5SDD2_9BACT Unreviewed; 1512 AA.
AC A0A1Z5SDD2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CAP35_08895 {ECO:0000313|EMBL:OSZ78361.1};
OS Chitinophagaceae bacterium IBVUCB1.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae.
OX NCBI_TaxID=1985173 {ECO:0000313|EMBL:OSZ78361.1, ECO:0000313|Proteomes:UP000194327};
RN [1] {ECO:0000313|EMBL:OSZ78361.1, ECO:0000313|Proteomes:UP000194327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBVUCB1 {ECO:0000313|EMBL:OSZ78361.1,
RC ECO:0000313|Proteomes:UP000194327};
RA Orr R.J.;
RT "Draft genome sequences of novel bacteria, isolated from environmental
RT samples.";
RL Submitted (MAY-2017) 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:OSZ78361.1}.
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DR EMBL; NFUW01000002; OSZ78361.1; -; Genomic_DNA.
DR STRING; 1985173.CAP35_08895; -.
DR OrthoDB; 9792152at2; -.
DR Proteomes; UP000194327; 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 Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
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:UP000194327};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1512
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011967015"
FT DOMAIN 240..501
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 1434..1510
FT /note="Secretion system C-terminal sorting"
FT /evidence="ECO:0000259|Pfam:PF18962"
FT ACT_SITE 249
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 275
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 447
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1512 AA; 166885 MW; 36956F4EE2C86B56 CRC64;
MHNCMLFVNL RMKRIAKLLL VIFTIHLIGD NSVNAQALQT DNKLDTRFGY LQINPNMLSW
FIDSCGNTTD NSKRQVIVHL KRVPDIYDKL QLMSYGVQLI HHIDGFSYTA LVDCAKIDVN
QIDLVYGVSE YDFQWKISDD IKVNKNKNVS ICIALISSEV ESEFLVFINS LGQKVIKSFG
SSYFLHGVSK NQLGIIASHY TVSSISLYAD PSILNYEAKC VTKSNIANLS ILYGGYNLKG
KGVTVGIGDN MSGTGNIDIN NRVVANFNPQ PYTNHGVHIN GIVGGAGIGD VRGEGVAPEA
FFVNHFFSQI LEGTTDFYNQ YNMTITNNSY AAVIRDCNYA GIYNTYSEAT DVLALKHKDV
LHIFAAGNDG LMTCNPYPNG FGTVVGAYQT AKNCLVVTSI DKRYNNALDG GRGPIRDGRL
KPEITAVGVD VMSTNRVDSY YVSGGTSMAS PGVAGGAALL TERFKQINGS TNPRADVLKA
LLMNGATDIG NPGPDYRYGF GFMNLPRSLA MLDNNRIITS TATNGSLQTY SISVPPNTAQ
MKVMLYWHDA VASTLATRQL VNDLDVSITT PAAATHRPLI LDPASDKILN NAVEGVDRLN
NVEQIIVNNP VAGNYVVAIN GFNIPSAQQD YVLVYDFIPQ GIKLTYPTTG ATVKTEDSLR
IYWDASEDGN TQKIELSTDG GSNWVLIADN IPAAQRHFAW LVPQGISSGK CRMRIIRNNT
SEQYTTGNFA INPIPVVSLD ANQCPGYIKI NWNVISNASA YEVMKKEGAA MKVVGIVSGT
TYTFAGLSVD SMYYIAVRPI IDGLQGYRSL AAKRKPNDGD CAGNISDGDI VAAKVLRPLN
GRLLTSTALN NKSILELSVR NLDDNPVNNF RVSYTLNGSV WKSRDYSTAI HALGFSSVIV
DTLDLSAAGI YQFVVAVQNL SMTDVVNVND TIRYAVKQLN NFPVDLTTVM LNDFEDWQAI
TLHQASAGLS PDERWDYTNA NDTCRLRSFV KQDITIKGNR SISMDATINT FKGQRNELAA
TLNLVNYNVN NEEIRLEFDY KLHGYSGEED SNKVYVRGSD TQPWVPLYAY DRKFAATGKI
ANSGSLSLTD AMLASKQNFS TSTQLNFVQS DVSLIGTNSF GRGFTMDNLK LYTVQNDVQL
ISVVSPITSE CGLSGMQPLT IKVRNGVNQT LNNIQLYYKY DNNAVVVETL ASLSGKQTIN
YTFNNKIDLT PKGKHTLSIW LAVNGDTYLL NDSILNYVFY NQPLIASYPY FEDFEDDNGG
WFAEGKDNSW AYGSPNSSLI NMAASGKHAW KTNLSGNYNL SELSYLYSPC FDITAVKNPY
YRFKAAMDIE NCGQVLCDGA NMEYSLDGIN WQKLGKYGEG TNWYNDSLHN VWSIQNSVNW
QSSSVKLPSN AKALRLRYRF EADLGVEREG MAVDDAEVYN EQPEVVTNNL LNIVPNPVTD
GKLLIDWTAK AGTRLIIKIH SISGALVYNE EIGTTKEGRN KYEFRTPQFQ RGVYIVQVLV
GDRKFTRKLV YL
//
