ID A0A1T4TZT4_9BACT Unreviewed; 565 AA.
AC A0A1T4TZT4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Subtilase family protein {ECO:0000313|EMBL:SKA45933.1};
GN ORFNames=SAMN04488128_107148 {ECO:0000313|EMBL:SKA45933.1};
OS Chitinophaga eiseniae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=634771 {ECO:0000313|EMBL:SKA45933.1, ECO:0000313|Proteomes:UP000190367};
RN [1] {ECO:0000313|EMBL:SKA45933.1, ECO:0000313|Proteomes:UP000190367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22224 {ECO:0000313|EMBL:SKA45933.1,
RC ECO:0000313|Proteomes:UP000190367};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; FUWZ01000007; SKA45933.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4TZT4; -.
DR STRING; 634771.SAMN04488128_107148; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000190367; 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; cd07483; Peptidases_S8_Subtilisin_Novo-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034080; Protease_P7-like_dom.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 68..504
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 74
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 297
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 468
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 565 AA; 61902 MW; 31AFED9489174F0C CRC64;
MKLFSREVAV LACVALTTAA FTTKSSAQSK TPVPKNWQLL NYETDSVYGT NTEKAYKEIL
KGKKSTPVIV AVIDSGIDTL HEDLKGILWT NPREIPGNGK DDDGNGYIDD IHGWNFLGAK
DGGSLKEDSD EATREYYRYK NKYGDPDSTL GKDSKEYTTW QNLKQKIEKP SSQTKLQYKT
MAKLQENVSK CENILKTYLN KDDFTVAQLD SIQTTNQDVL LARNFMTRLL KSTGDEPLPF
GEFKMEFEGY MGELKRKAES TEVPPNQNRE QIVGDKYDDI TDTNYGNNDV MGKFGFHGTH
VSGIIGAMRN NGVGIDGVAD NVRIMAVKAV PDGDERDKDV ALAIRYAVDN GAQIINMSFG
KPYSPHKEWV DEAVKYAQKK GVLLVHAAGN DGANNDSVPN YPNPDFADGS PRADNYITVG
ASSHGLAADK VASFSNYGKK NVDLFAPGVQ IYSTIPGGNK YGSASGTSMA APVVTGVAAL
VLSYYPELSA RQLKYILEKS ATPLPDGSKE VNKPGSQDEK IDFTDLSING GIVNTYEALK
LAATIKGENV KKKQHKAKMR PVKKN
//
