ID A0A1H7PRM2_9BACT Unreviewed; 1820 AA.
AC A0A1H7PRM2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Por secretion system C-terminal sorting domain-containing protein {ECO:0000313|EMBL:SEL38108.1};
GN ORFNames=SAMN04488505_102149 {ECO:0000313|EMBL:SEL38108.1};
OS Chitinophaga rupis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=573321 {ECO:0000313|EMBL:SEL38108.1, ECO:0000313|Proteomes:UP000198984};
RN [1] {ECO:0000313|EMBL:SEL38108.1, ECO:0000313|Proteomes:UP000198984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21039 {ECO:0000313|EMBL:SEL38108.1,
RC ECO:0000313|Proteomes:UP000198984};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC {ECO:0000256|ARBA:ARBA00037986}.
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DR EMBL; FOBB01000002; SEL38108.1; -; Genomic_DNA.
DR STRING; 573321.SAMN04488505_102149; -.
DR Proteomes; UP000198984; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.60.40.1080; -; 5.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR021720; Malectin_dom.
DR InterPro; IPR026444; Secre_tail.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR Pfam; PF02368; Big_2; 5.
DR Pfam; PF11721; Malectin; 2.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SMART; SM00635; BID_2; 5.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 5.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000198984};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1820
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011508436"
FT DOMAIN 769..846
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 855..931
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 1116..1193
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 1200..1277
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 1285..1362
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT REGION 338..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1820 AA; 194302 MW; 47A1FE4E0BA9D5D3 CRC64;
MKMQKIYCTL LLTIFYLTAS QGVHAQAYTW NQVRIGGSGA LPSFIAHPKV PDLYFITTDV
GTPYRWNKNL QKWEHLMLFQ KIPVNYWNWE VNQRCGSLGV DPNDATGNIL YATVENSAGP
GPGKGSSSVG TIMKSTDRGD TWTDLHVPIV VHPNSTQAYG DRIQVDPSNS NNVWVVTDQN
GALKSDNAGT SWSQVSAITT QGSCAFILFD KSSGTVAVNG QNVTKRIYIG RSAGIYASED
GGASFTLMSN SPQYPGRATI HADGTLYVSA GTDDQKKGVY KYKNGSWQDV SPVTLDPEPG
KSDRYFSKVA VNPANSNDIV VSTRGSWQKD PYYISRQGGA PGSYTQGKIT RDNSEAPHSA
NDGLAYNDPG HNAAAFTWDP FYPNRVWIND MLDVLSTDNI FDPVSNWKIR VVGLEEIVVT
GPMAAPPSGK NLLLTATADV GGAHHRSLTE PLYQGAVSST ALHYGIFSAF NMQGVTFQYT
DPNFVVRVGC DGPAAGELSA SRAGYSTDGG DTYTLFPKSP GLRGRVAVSA NRRNILWLTQ
MDVNAPGNVY WSEDLGSSWT KSTGVASGIL PSGPQWNLYP GQNHLVADKV NGDYFYIWDR
GSFYVSADGG RSFQKTTATG LTANAGSNPN GSSYATNSNV EVTPGKTGDV WIAFYDDAYP
QYAALYHTSD TGKTFSKVGG ENFKPKWIAA AMSDTTPNAH LALYATSQVL PINGISYGAY
RSDDTGRTWA TILDRLPGVV QNITADNKGR MFIAISGNGI YFGSPVAGPV QSVEIVNPAS
DTIVKGFSVK LNVKLTPAYP TNPSVTWSSS DTAIAKVDPF GKVSGINAGT ATITVTSVDG
GKTSTRQIVV IPPTISTGIT IDSVLYGTMN TPKQIAVTVI PSNTTNKTLN WSVADSTIAS
VDANGVITGL KLGATTLTIS TADGGVTKTV QLIVNTIVTA INAGSTATTG SPATPYQNTA
IGQYIPEGPA GTDKLWHAGY TWSSRNTATM DLSQVTAPAP RQVYEYMRIA KITSAQLRYY
FRNLIPNANY SLRLHFVEPS DADKANRVFS VKTSGDSLIN FNIYQAAGNK LNTVITRTLE
AKADNAGVIT VYFYPKVGTN DPYSASIAAL EASIIPLQGI SIHSDSSNLY VSYKDTLKLT
TTPANATNRN LVYRSSNNAV ATVDLNGVVT GKAAGTVTIT ATSAESGFTA AKTYTVIYVP
VTSLTLDSTA ANVFVGATLQ LNATINPAKA SNKGVVWTSS DTTVAKVSDN GTITGVKQGD
VIVKATSADN SAIAAQANIH VANVLATGLV LQPSPATIGE RDTLRVNVTF LPANTSIKKV
TWSSSNTSLA TVDSTGLITA IKQGSLTITA NTQDGSGVSA TLPVTVAPFD SCGGIPNYGF
ESGLINWIAY RESVPTVGAV YTISGKGHSG DKAATLGYTT ANTSLNIKDS IPVRGGSVIV
FTQWVKVEKD AGGYPWWSGY GVGFVDSLGA ATGNASYQKQ VDNVTAYRDN WAQIRDTINV
PDSATGLTYW VAKVGPGTVW VDDYCIEVLK TNKSAVLAIN AGTTLNPPGP YANTTFAQYV
PEGPTGTDNL WHAGYTWVQK VNAPVDLSQV TDPAPPQVYE YIRIFKDNIT QMRYYLRGLT
PNTVYAIRLH FVEAQDAEKN KRIFSIKATH GLDSLTDFNI YQAAGNKLNT AVIKTIRAKA
DNTGLIQVVF YPKKGLYDPY SGSIAAIEVR TTSPGDTLQS MTANQSMIAV ADNKLNTHGK
LDLTAELFPN PSNNVFNVRM TSSSKAPALL SIVNNAGSVI YSARINAGTY YQLGQNLKPG
IYYISIRQGA QSKTMKVVKQ
//
