ID A0A0U5IIP5_9GAMM Unreviewed; 620 AA.
AC A0A0U5IIP5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Putative Subtilisin {ECO:0000313|EMBL:CRI64489.1};
DE EC=3.4.21.62 {ECO:0000313|EMBL:CRI64489.1};
GN ORFNames=THIOKS11970001 {ECO:0000313|EMBL:CRI64489.1};
OS Thiocapsa sp. KS1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=610332 {ECO:0000313|EMBL:CRI64489.1, ECO:0000313|Proteomes:UP000198608};
RN [1] {ECO:0000313|Proteomes:UP000198608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KS1 {ECO:0000313|Proteomes:UP000198608};
RA Luecker S.;
RL Submitted (MAY-2015) 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; CVPF01000109; CRI64489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5IIP5; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000198608; 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; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
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 PANTHER; PTHR43806:SF59; EXTRACELLULAR PROTEASE; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50853; FN3; 2.
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 433..525
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 526..620
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 366
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 620 AA; 63550 MW; D633FFEA6513257C CRC64;
MTRAEQQTAL LERAMTEGSV PVIVRLRTPD TPQMRADSVQ RRAAVSAAQQ GILQRLGIGN
GRDRFGAPVK RFSEVSGLAM QADAIDLMDL ADDPAVLDVL EDVAYPPALL TSVPLVGALG
GSFAGYSGLG QVVAILDTGV DKSHPFLGGK VVSEACYSSD YPLSEITSLC PGRVTASTAD
GSARNCDTSV SGCMHGTHVA GIAAGQGSSF SGVARDARII AIQVFSLFPS SACGTAPCVM
AYTSDIIRGL ERVNALRTTY AIAAANLSLG GRGSTTACDS DLAKPAIDTL YAAGIATVIA
SGNNGYVNAI SSPGCISTAV TVGSTTKSDS VSSFSNSASF LDLLAPGSAI NSSIPGGNYA
TWSGTSMAAP HVTGAWAVLK SVKPSAGVDE VLGALRSTGR TVLDTRNNLS KPRIEVASAV
AVLKGATSPA PVAPNALAAS QITVSGFTAN WGSVSGAAGY RLDVSSSSIF ANYVNGYRDR
DVGNVRSLAV TGLNPGTTYY YRVRAYNTGG AGPSSNTRNA TTQIAVPKAP TLNPALNLSR
TSFLANWSPV GGAAGYRIDV ATNSTFRTYV SGYKNLNVGN VASRSVTGLK AGTTYYVRLR
AYNATGTSAN SAVQLIVTPR
//