ID   A0A238VWJ3_9FLAO        Unreviewed;      1276 AA.
AC   A0A238VWJ3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Por secretion system C-terminal sorting domain-containing protein {ECO:0000313|EMBL:SNR37849.1};
GN   ORFNames=SAMN06265371_102100 {ECO:0000313|EMBL:SNR37849.1};
OS   Lutibacter agarilyticus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=1109740 {ECO:0000313|EMBL:SNR37849.1, ECO:0000313|Proteomes:UP000198384};
RN   [1] {ECO:0000313|EMBL:SNR37849.1, ECO:0000313|Proteomes:UP000198384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29150 {ECO:0000313|EMBL:SNR37849.1,
RC   ECO:0000313|Proteomes:UP000198384};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FZNT01000002; SNR37849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238VWJ3; -.
DR   OrthoDB; 9792152at2; -.
DR   Proteomes; UP000198384; Unassembled WGS sequence.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF18962; Por_Secre_tail; 1.
DR   Pfam; PF13583; Reprolysin_4; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198384};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1276
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013189794"
FT   DOMAIN          773..868
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          864..1014
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          548..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1276 AA;  138539 MW;  37BB820D7D5ABE89 CRC64;
     MKLIHHKLLF STLLFFGLVV NISAQTPDKL WFKSTDFQNN SKTKVERRST PNNYKVYNLD
     LESLTDKLKN TPQRKDKKAT SNLIIDFPSA SGEIENYEIF EASVLDEVLQ KKYPSIKSYV
     GKNTTNSAET IRFSVSKIGL HAMILQNKEG AVFIDPFTTD HKSYMVYSKK EVPSINPFVC
     MFDDVNDKTT TAKTVLSSKS LNANDSQMRS YRLAIATTGE YSQFQLTYHG ISSTATETEK
     KEAILSAINV TMTRVNAIFE RDVSLTMKLV TDTDKVIFLD PNTDNLTNDD GSVLINESQT
     VIDANIGFNN YDIGHTFSTG GGGLAQLNSP CTSSKARGIT GSSFPIGDTY DIDFVAHEMG
     HQFGANHTFN SNEGSCSGNK NDITSIEPGS GSTIMAYAGL CAPDNVQSQS DDYFHLVSIQ
     EMWANISAGN SSSCATLTNT GNSAPVVNAL NTYTIPISTP FALTAEASDP DSDTLTYTWE
     QLDPENAVAP PVATSIEGPS FRSITPSTSP TRYFPNQNTV IAGKLFDTWE VLPSVSRTMK
     FSVNVRDNNL SGGQSSSQET TITFDGTTGP FNVTSQTSSE SWNSNESQTI TWNIANTNNA
     PVNCSTVNIL LSTDGGYTFP FELATNIPNN GTYTFSVPNI TTNLGRIKVE SVGNIFYAIN
     KANLSIQAKE FQLDFSNSTA KVCKPSSAVY NFTYTTFLGF NEETTFSATG NPAGSTVTFS
     PTTATSNNTN IEVTVSGISN LTIGTYEINL KGVSATSAME KSELVTLTVF DSTITTPTLT
     SPENNTVDLL NPFVFEWSAD ENAESYQIQL ATDASFNSIV EENNTLTTNT FTANSLDFNT
     TYYWRVKSSN NCGESAFSEV FNFSTANVIC NTYNSTDKSL EIPDNDPNGV NSIITVINNQ
     TITDINVTVN ITHPYVEDLT LTLTSPNGIA ILLSVSNGGA GDNYTNTVFD DDATIKISDG
     FAPFTGSFIP QLPLANLNNI ESKGDWTLNV ADNGEADTGT ILNWSLEICG LNIEVINDDD
     NDGITNDIDQ CPNSTPGSKV NSVGCFTVAE GNFNIEGTGE TCLGKANGQI VISTTETHNY
     TATINGTDYS FTNFQTINDL PAGTYDFCIS INEENYEQCF TVVIETGATI AAKATISSNK
     AAIIISEGTA PFNILVNGKQ VFKTSNTSFE IDVTHGDLVE VKTAIECEGV FSKNIDLIEG
     VLAYPNPSKG RFQITVPYSK KDITVKVYNV QSQLISTKNY SVYNGKILLN IEAVPTGVYF
     AKIMLDEPVS LKLIKQ
//