ID A0A243SCM1_9FLAO Unreviewed; 837 AA.
AC A0A243SCM1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Secretion protein {ECO:0000313|EMBL:OUD32751.1};
GN ORFNames=FPG59_14235 {ECO:0000313|EMBL:OUD32751.1};
OS Flavobacterium sp. FPG59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1929267 {ECO:0000313|EMBL:OUD32751.1, ECO:0000313|Proteomes:UP000195161};
RN [1] {ECO:0000313|EMBL:OUD32751.1, ECO:0000313|Proteomes:UP000195161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FPG59 {ECO:0000313|EMBL:OUD32751.1};
RA Wu A., Liu R., Kropinski A.M., Macinnes J.I.;
RT "The genome of Flavobacter psychrophilum strain FPG59.";
RL Submitted (DEC-2016) 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:OUD32751.1}.
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DR EMBL; MTCA01000242; OUD32751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A243SCM1; -.
DR Proteomes; UP000195161; 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; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR026444; Secre_tail.
DR InterPro; IPR034058; TagA/B/C/D_pept_dom.
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 SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Reference proteome {ECO:0000313|Proteomes:UP000195161};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 127..356
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 772..834
FT /note="Secretion system C-terminal sorting"
FT /evidence="ECO:0000259|Pfam:PF18962"
FT ACT_SITE 132
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 303
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 837 AA; 93026 MW; 26EC01B09F3C98A7 CRC64;
MISFSKKEFK NHKLSSLPLN DLWKLPTGLK YHSSKKKYTI VTDSVKNVIN KLNALKIETT
TQGNVVLVEA NYKTILNQII PLNDVLSVTL ESYNPSFESK IIDQNFSVNQ INGASKKFAD
ITGFNQIVSV KDAFFDTNDV DLLQKHIQSS TQSNQISQHA TAMATIVAGL GNSSVLGKGV
APQAKVQSSN FLSIFPDEIS SLQGATVQNH SYGTTIENFY GNLASVYDKT LYENPTISHV
FSAGNKGVEG FKSITGNFKQ SKNSIVVGSV NASEKSMSFS SKGPAYDGRI KPEIVAYSTE
GTSNATAITT GIITLMKELY EKKYTSQLQN ATAKAILINS AKDLGNKGPD FTYGFGNINA
LKCLNSIEKN RIITGTSVPG QKNNHQIIVP ENSKNVKITL VWNDPPAPAN TNISLIHDLD
LELISPTETF LPWILNPDLP QEPAKKGVDK INTVEQIELE NPQFQTYTIV VKNSLSNNAI
QDYSIVYDYE LKNTFEWYYP ILYDNFPLDG KTASPFKWNT TIENNTGDLA ISYNEGQTWE
TIATNISINT NQYLYLPSQE LFTKAKLKMK IGDEDFISDD FIISYDLNTT TSLVCNGVTE
INWTKPETVT SFNIYELVDD KLAFKELVTN SNYTYTNGKI HAVSPNFKSV EGIKSESTLR
YENNSNCYFE FVNAAITTDN KITISTNLFS LFQIKNVELL KLVNNKEVLL TSINHPLSKS
FSLVDNSPSE GFNKYRVRLT LEDNTIINSP TIDIIFLGKN DFFVYPTALK PNQDINIETK
AEEASFSLFN LNGQNIVSQS FTTKNNSITL PSLSSGIYIY KITSKTGKNK TGKISIQ
//