ID   A0A1I1V315_9BACT        Unreviewed;      1399 AA.
AC   A0A1I1V315;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Por secretion system C-terminal sorting domain-containing protein {ECO:0000313|EMBL:SFD77441.1};
GN   ORFNames=SAMN05518672_103165 {ECO:0000313|EMBL:SFD77441.1};
OS   Chitinophaga sp. CF118.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1884367 {ECO:0000313|EMBL:SFD77441.1, ECO:0000313|Proteomes:UP000199596};
RN   [1] {ECO:0000313|EMBL:SFD77441.1, ECO:0000313|Proteomes:UP000199596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF118 {ECO:0000313|EMBL:SFD77441.1,
RC   ECO:0000313|Proteomes:UP000199596};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOMK01000003; SFD77441.1; -; Genomic_DNA.
DR   STRING; 1884367.SAMN05518672_103165; -.
DR   OrthoDB; 197688at2; -.
DR   Proteomes; UP000199596; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   CDD; cd14490; CBM6-CBM35-CBM36_like_1; 1.
DR   CDD; cd09619; CBM9_like_4; 2.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   Gene3D; 2.60.40.1190; -; 2.
DR   Gene3D; 2.60.40.2030; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR038081; CalX-like_sf.
DR   InterPro; IPR010502; Carb-bd_dom_fam9.
DR   InterPro; IPR033801; CBM6-CBM35-CBM36-like_1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   Pfam; PF13229; Beta_helix; 1.
DR   Pfam; PF02368; Big_2; 1.
DR   Pfam; PF06452; CBM9_1; 2.
DR   Pfam; PF18962; Por_Secre_tail; 1.
DR   SMART; SM00635; BID_2; 1.
DR   SMART; SM00710; PbH1; 9.
DR   SUPFAM; SSF141072; CalX-like; 1.
DR   SUPFAM; SSF49344; CBD9-like; 2.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
PE   4: Predicted;
FT   DOMAIN          628..706
FT                   /note="BIG2"
FT                   /evidence="ECO:0000259|SMART:SM00635"
SQ   SEQUENCE   1399 AA;  149431 MW;  1277F90EB96FB013 CRC64;
     MRKTLSFPSN QVHPGIPPDF PNNLRKVPGW LTTLLLLFLL SNAHAQSDGL PRGAYQLPYI
     RYESDNAILD GGAALQQSPQ FIQTDIASEA SDQKYVSLTA NGASIEWTAT QAAQGVNLRF
     TLPDDNTGAG LTGSLGLYVN GVKVKTIPLS SYWAYQYFPQ ADPVQTPGGK TFMRFDEVHF
     RLDNPINIGN TISIRKDNSD AITYGVDFIE LEPVPAALTQ PANYLSVTAY GAVANDQTDD
     FAAFNACIAA AASQGKNVYI PAGKFLLSDK LPLNVSNMKI LGAGVWYTEV YFSTDKQFYG
     GIMGRASNVE ISNFSLNTIN NDRLKYDEAN PRLPGEMYKT YKGFMGTYGA GSRIHDIWVE
     HFECGFWIAG YDPPYPIDIT TDLVISKCRI RNNYADGVNF CQGTSNSVVE QSSVRNNGDD
     GLAVWPANAA GNNQTCRNNI FRYNTIENNW RAGSIALFGG TGHEIHHNLI KDGVAGSAIR
     FTNDFPGFTF EYPGDVIKVY ENTMSGCGSS YDLWDQKRGA VEFYAGGSGI FNMQFDNNTI
     LRSQRDAIQI YGNGIHHLVF NNTTIDGTGL DPVVRNEPAD VYGGFGLYVQ AGSQTATFNN
     LTVTNAESGA YINKNNSFQL IIQNINIPVS SVSIKPANDT TLTTGQTLQL TANILPVDAT
     NKNVTWTSSN AGAATVDASG KVTAVGYGIA TITVVTASGN FTATRKVTIQ PGVNVVATTP
     AAAEGGAAGV FTFSTSSLSS TISVKYTVSG TASGSDYTPS LNGTITLTPT NPSATITITP
     VDDVVFEGPE TLRISLKKDS AYNLGGDTTA VITIADNDNP PCVAPVIALV SGTAPVIDQS
     IDAAWAIAPV KNISNVILGS LPSDYAGKWR ALYDNTNLYL LVEVNDGTKL SDSGASWWED
     DVVEIFIDGD NSKGTAYDGI NDFQLGFRWN DNTVHVGSYS VNRTTGINYN QYATATGYTL
     EVAIPWSTIG VSPSIGKSLG LDVQIDDDDN GGTRDAQIAS FATNTTAFQN PAVFGTVYLT
     TCNGVVNQPP TVNAGTDQTL AANTTSVTLQ GNGSDPEGHA VTYSWTKVSG PAVTFSSTTI
     ANPVVTGLTN GSTYVFQLTV SDGTLTSADQ VQISIGSVSN PADLTAYPGT VTVDGNLNES
     SWNLSKSIAK TTVGTPNNTA TFGVLWDNNN LYIGVKVLDA TLNNDSPDSW DNDAVEIFID
     ANNNKGSTFD GRDNQFIKAY NSSTLFSKIA VTGVQHAYAT ITGGYTVEIS IPWSQLGITP
     AAGLTIGFDA GYDDDDNGGS RDGQAVWFGT INNYQSTADY GTLVLANTAL NTLAVEHSVV
     SSSDLKIVPN PAINGQAKVL ISGNTAKGYI YVYDLHGKQV YTTKALPEVK LDLQQLPKGV
     YVVKYIIGDK SFTRKLLIQ
//