ID   A0A1M7NUY7_9SPHI        Unreviewed;      1245 AA.
AC   A0A1M7NUY7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Por secretion system C-terminal sorting domain-containing protein {ECO:0000313|EMBL:SHN07525.1};
GN   ORFNames=SAMN05216524_10544 {ECO:0000313|EMBL:SHN07525.1};
OS   Mucilaginibacter sp. OK098.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1855297 {ECO:0000313|EMBL:SHN07525.1, ECO:0000313|Proteomes:UP000184158};
RN   [1] {ECO:0000313|EMBL:SHN07525.1, ECO:0000313|Proteomes:UP000184158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK098 {ECO:0000313|EMBL:SHN07525.1,
RC   ECO:0000313|Proteomes:UP000184158};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FRCM01000005; SHN07525.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M7NUY7; -.
DR   STRING; 1855297.SAMN05216524_10544; -.
DR   OrthoDB; 9792152at2; -.
DR   Proteomes; UP000184158; 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; IPR045474; GEVED.
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   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; PF20009; GEVED; 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.
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   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01240};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1245
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013360025"
FT   DOMAIN          153..438
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          655..732
FT                   /note="GEVED"
FT                   /evidence="ECO:0000259|Pfam:PF20009"
FT   DOMAIN          1167..1243
FT                   /note="Secretion system C-terminal sorting"
FT                   /evidence="ECO:0000259|Pfam:PF18962"
FT   ACT_SITE        131
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        158
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        384
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1245 AA;  131504 MW;  5CFFD0F12458AADF CRC64;
     MNKLYAAVIF SFFLLCFADK TFGQQIPVND VKKKELTDLS ARSNNTFLIN HNNALALAKK
     NEWTVKRKTK KGGLISLQGV NSLGFPIYLK TDNNTTAAAT TGTNTVQPGG SLGLNLSGSS
     TAINNKLAIW DGGSVYKAHQ EFAGKTITLH DSTGVIDHAT HVSGTMIAKG VYAPAKGMAF
     NATTLQSYDF DNDVAEMSAA ASGLLLSNHS YGDAAGWYFN DSENHWEWYG LPGDSVDYNF
     GFYGSRTQDW DKIAYNAPYY LIVESAGNSR ADTGPAVGED YYGYASITNQ TLVDKGKRPV
     GISSNDGYDI IATTGNAKNI LTVGAVNPLP NGPATSNGIS IAYFSGYGPT DDGRIKPDIV
     GDGVDVLSTG SGSKTSYITL SGTSMSAPNV TGSLYLLQEY YTEKNNGKFM RAATLKGLAC
     HTAFDAGNVG PDYIYGWGLL DMRRAAQAIT DNNGKSLIKE ASLQQAQKQT YNVIASGNGP
     LAVTISWTDP AGAATKDGTI NSRTPKLVND LDIRVSDGTT TFNPWVLDPL NPSVAAKTGD
     NILDNIEQVY IPGAVAGKTY TITVSNKGTL LAGAQDYSLI ATGVGGSTYC ASNPVSNADS
     RVNNVTLANL NYTAPAGCSS YSDHTNLTMQ LEQGKTYPLS ITLGTCGANF NKAAKVYIDW
     NGNGVFDANE LVATSGIINA TGTYTSNISV PATVVPGNFS IMRVVLTETT DTSVIKPCGT
     YAKGETQDYR VQFLQTGIDA GVIAIVSPDA TGSCSAATQI TVRLKNFGGL AISNIPVVVT
     ITAPDNSITT LNQTYTGTLQ PLEQEDFILN TSFNAIAGST YKIVAASNLA NDPVSANNQT
     SETVTISLPP VAADLVAYYC EDSKQYQVSG SGDGELLWYQ NNTDAIPVAY GSPATISQAP
     INNTYYAGLN DFTGSIGPIT KNVFTGGGYN QFSPYVSVTT KIPVIIESAR LYIGNSGKIT
     FNVADASGRT VSSSTINAVA TRTTPLPGNQ PDDANDQGAV YNLNLLLPAA GDYTINISYD
     NTATIYRNNT GVTGYPFTIG NIFSITGNNA TSGTDTAAYK SYYYYFYDVK VKSAGCPSTV
     RQAVMVSKPV ITQNGTVLSS SVAANNQWYL NGKAIAGATN ATYTPAQSGN YQVGLILDGG
     CIALSDNYVY IITTNNAGSK TDIGLVVFPV PASSQLNILF AAKNSDNVTI SLINAAGQIV
     YNTKQTIAAG NFSTIADVTR LPPGSYILKI QLGQKAYNTK VIILR
//