ID A0A0S7C608_9BACT Unreviewed; 835 AA.
AC A0A0S7C608;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Protein containing Por secretion system C-terminal sorting domain {ECO:0000313|EMBL:GAP44736.1};
GN ORFNames=TBC1_12547 {ECO:0000313|EMBL:GAP44736.1};
OS Lentimicrobium saccharophilum.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC Lentimicrobium.
OX NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP44736.1};
RN [1] {ECO:0000313|EMBL:GAP44736.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBC1 {ECO:0000313|EMBL:GAP44736.1};
RA Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA Cruz R., Yamaguchi T., Sekiguchi Y.;
RT "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate from a
RT Methanogenic Wastewater Treatment System.";
RL Genome Announc. 3:e01168-15(2015).
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DR EMBL; DF968183; GAP44736.1; -; Genomic_DNA.
DR RefSeq; WP_062044542.1; NZ_DF968183.1.
DR AlphaFoldDB; A0A0S7C608; -.
DR STRING; 1678841.TBC1_12547; -.
DR PATRIC; fig|1678841.3.peg.3269; -.
DR OrthoDB; 6281169at2; -.
DR Proteomes; UP000053091; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProt.
DR GO; GO:0016715; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.120.230; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR InterPro; IPR015197; PngaseF_C.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR39319:SF1; PEPTIDE-N-GLYCOSIDASE F N-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR39319; SI:DKEY-256H2.1; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF09113; N-glycanase_C; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49742; PHM/PNGase F; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000053091};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..835
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006633643"
FT DOMAIN 54..186
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
SQ SEQUENCE 835 AA; 92406 MW; B79B363380AEC8E4 CRC64;
MKNNYLKLTL MTMALLFTAL SGLRAQTNQY LHYDCANLDY VVLENGSQYI ANKPGITIAG
WFYDDQLGYG QGLMGFRGTQ GFYMIQLADG KVECRFQNSA GTLFEYVAPA NTVIPQVWQH
FAWIYDGSAI KLYVNGILKG SKAASGTFTA TNIAFSIGRS ILAGLDFYWC GRTDEVSVWS
KALTQEEIQD MMDNELTGQE PGLEMYYKFN QGVPGGDNTS ITKLTSQVDS PIRDADLINF
RMTGETSNFN GTLDPTYQAI SFPPIPNKLN NEPPFAIEAT ATSGLPVTFN ILSGPATVEG
NIITLTGAPG LVEVEATQPG GGQYNPAEPV IQRFHVLDPQ THVPDIDIRN PLAGNVYVPV
LSPIQLAAIS TIEFPELFSV AWVKFRINGQ TVDAQNFWNG HFTGWWTPPG YGNHTIEVLS
ANNFGAVKTE TMSISIQPAA TNASVQAFKD IWLNPTQITQ TVEANLPSFL GAYDQIIATL
NVHCPTGGCG AWDRVAYFEA QDKEGNWVEI IRYITPYGVA CSHSIDLTDY MSILQGKTAF
RATCPTLDNG FLYDLTLDYR SGAPAYLYSR VKEVWREIFP FGDYANLQPV TDFQYEYPEN
TVASRFKLVS TGHGWGDLNT SNAAEFYNAT HDIYVNGAKK YSQINWNTCN PNPDGCQPQN
GTWYHNRAGW CPGSIAPWFN FSLDEYVNAG NVTLGYKFFE NYVDYCHPNH PDCQTGVTCS
DCNDGFNPVL DVASYVISYA TSPMIVVKSE PKPVAENALL VFPNPSNGIF EISLEKTINL
KNGEIIIYDN MSRPIRFIPW NGDTFTLDLS AHGSGMYFLQ VVSPGFSEVK KIVIE
//
