ID A0A1H5JVQ4_9FLAO Unreviewed; 1452 AA.
AC A0A1H5JVQ4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Por secretion system C-terminal sorting domain-containing protein {ECO:0000313|EMBL:SEE56514.1};
GN ORFNames=SAMN04487765_3142 {ECO:0000313|EMBL:SEE56514.1};
OS Tenacibaculum sp. MAR_2010_89.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1250198 {ECO:0000313|EMBL:SEE56514.1, ECO:0000313|Proteomes:UP000198792};
RN [1] {ECO:0000313|EMBL:SEE56514.1, ECO:0000313|Proteomes:UP000198792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2010_89 {ECO:0000313|EMBL:SEE56514.1,
RC ECO:0000313|Proteomes:UP000198792};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR EMBL; FNUB01000005; SEE56514.1; -; Genomic_DNA.
DR STRING; 1250198.SAMN04487765_3142; -.
DR Proteomes; UP000198792; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd02871; GH18_chitinase_D-like; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF17957; Big_7; 4.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00704; Glyco_hydro_18; 2.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SMART; SM00495; ChtBD3; 2.
DR SMART; SM00636; Glyco_18; 2.
DR SMART; SM00409; IG; 4.
DR SMART; SM00089; PKD; 4.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR PROSITE; PS01095; GH18_1; 2.
DR PROSITE; PS51910; GH18_2; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023024};
KW Reference proteome {ECO:0000313|Proteomes:UP000198792};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1452
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011519326"
FT DOMAIN 39..509
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 1028..1356
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 1452 AA; 157186 MW; 513DCA96012E1B8C CRC64;
MKPFSFVREK LSIVFLLMTT FLFSQVNTGG TATTSNHQKQ VIGYITNWDA WKTTTAGIPG
QGALTHLNID YSKYTILNYS FFGVANDGSL HSGDHRNKQI YQSGATQAPN DIFMKDIYSS
WDMHILFGEI DPLQHINADA KRRAEAQGFQ VELEGTTWTH PTWGLSGPLP LPLHKESGAP
GLLELAHQKG VKVMASIGGW SMCKHFPEMA ADPVKRARFI EDCKKLIATG FDGIDLDWEY
PGPYSGMNFT GTQADFANFE NLVEEIRVAI GPDKLITSAM SADPRKLDGF NWNKLSNSMD
YFNMMTYDMN GGWSNKAGHN APVYPYANAE VSFFNWQATL QKLVDNGVPK NKICFGAPFY
GRGVVTEGAA DLNAKTVKKA VTIQPDGPIQ TASDYTNWKL EVYDGTPNYF FIKQKALSPN
SGWTRKWDDE AKVPYLVKGN FFLSYDDEES IGIKAQFIND NELAGTIVWT VYGDLEISGS
ATSFGTKLKR WSNVKSPLVN KMNEVFANGG TGGNTSPSVS ITSPSNNATY AEGDTVTIKA
NASDSDGTIS KVEFFNGSTK LGEDTTLPYE FTLENIVAGN YTLTAKATDN DNAVSTSSIV
TIVANGAGEN LPPIVSITSP TDDAIFNEGE TIEVKVDATD SDGTISKVEF FNGSTKLGED
VTSPYSYNIV NSLVGTYTLT AKATDDKNLS ATSSVITVKV NGGTVDNCSG IADWSATITY
NGGENVKYKN VNYQAKWWTK NQTPDTHTGD GQPWKKIKDC TGTGGGDNVS PTVNITSPST
NATFKEGATV EITASASDSD GTVNKVVFFN GTTKLGEDTT SPYSYTITNA LEGTYTLTAK
ATDDKNASTT SIVVQVKIEK DNTGGTGCDG VTQYAAGTSY NQNQEVQNGG DKFKCNVAGW
CSSAAAWAYA PGTGAHWQDA WAKVGSCSSG SSPEVSITSP VSGAVYTVGG SITINASATD
DGSISKVEFF NGTTKLGEDT SSPYSYTVAN AQAGKYILTA KATDNENNST TSSSVVISDG
TQTPISGKIL VGYWHNFDNG STIPKLRDVS SNWDVVCVAF AEPKTGSKSD MKFSPFSIYG
GNINEFKNDV AILQGRGQKV LISIGGANAH VELNNETDKN EFVASMTSII NTYGFDGLDI
DLEGNSLSLN SGDTDFRNPT TPKIVNLIQG TKEVINNVGA SKFTLSMAPE TAYVQGAYGN
YSGIFGAYLP VIHALRDQMD YIHVQHYNTG SMFGRDGKIY QPATADFHVA MAEMLITGFK
VAQTGLNFPG LRSNQVAIGL PAEPRAAGSG YTSEAIVQQA LDYLIKGTSY PNRTYTTSTT
YPEFRGLMTW SINWDLANNS TFSTSHKAYF DSLGQQLRKS LTTKQVLSEE EVKVFSNPVI
NNLIIVDLNM REANINSEIE VFDINGAVVF REKTNLNTSK KVFNVSSLKS GLYFYSYKRN
NKKHIGKFIK TN
//
