ID A0A1I3I606_9FLAO Unreviewed; 644 AA.
AC A0A1I3I606;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Por secretion system C-terminal sorting domain-containing protein {ECO:0000313|EMBL:SFI43362.1};
GN ORFNames=SAMN05443292_2579 {ECO:0000313|EMBL:SFI43362.1};
OS Halpernia frigidisoli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Halpernia.
OX NCBI_TaxID=1125876 {ECO:0000313|EMBL:SFI43362.1, ECO:0000313|Proteomes:UP000198931};
RN [1] {ECO:0000313|EMBL:SFI43362.1, ECO:0000313|Proteomes:UP000198931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26000 {ECO:0000313|EMBL:SFI43362.1,
RC ECO:0000313|Proteomes:UP000198931};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; FOQT01000004; SFI43362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3I606; -.
DR STRING; 1125876.SAMN05443292_2579; -.
DR OrthoDB; 9792152at2; -.
DR Proteomes; UP000198931; 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; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
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 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|PROSITE-ProRule:PRU01240};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Reference proteome {ECO:0000313|Proteomes:UP000198931};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..644
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011578143"
FT DOMAIN 119..395
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 126
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 157
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 342
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 644 AA; 69339 MW; 91CA7EC828305F3E CRC64;
MKKSILIASF FIGTFAFAQT AEQRAEIQKS IDKNELTRLE QKFQLDYEFQ QQKISSYLSA
NPNAKKTFVK DGNVFMLHHI DAEGNPIYIN TKDANQVSNA KINALYGGGS VNVNITGTNM
VAGVWDGGQI NANHELLAGN VTMQPSQTVN SAGGNNHMQA VSGIMVGKII TTSTNPNAAT
ARGLAPNATA RNYDWDNDLT EMASFAGSGF LISNHSYGYS NTTTNNIWNY GAYDETSKDW
DALLKTTPLY LPFVAGGNEQ QTTGNASATG FDNMTGSSAS KNVMTVGAIN ADNSMSDYSN
WGPTDDGRVK PDIVTLGTSI NVPLYTGNNT YTGVDINSSG TSYAAPAAAA AGLLLQQYYF
SLFNKYMTAA SLKALMLHTA DDAGNAGPDA KFGWGILNVE NAAKTIKQMQ TGGSAKLVEF
TTNPTNNSSA EVSTSGTAGG ISAKASICWT DDEGTEQTAT NGINNTTSRL VYNFDILFRQ
QGTPFIDRRT FAPLSVTSPN NVATVSSTWF VNNVDNYRQA NITTSNLGNN LIVYVRKNTT
SPAAVKPFSV LLTGLNITNA TLAVNENVIN SATVFYNKVD GQIKMISNNT KDGFGAYKIY
DMSGKILKAG TERGNTISFQ NDNNGVYILI YQNNNKEETF KFRK
//
