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Database: UniProt
Entry: F4C6L8_SPHS2
LinkDB: F4C6L8_SPHS2
Original site: F4C6L8_SPHS2 
ID   F4C6L8_SPHS2            Unreviewed;       485 AA.
AC   F4C6L8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Glycoside hydrolase family 28 {ECO:0000313|EMBL:ADZ77054.1};
GN   OrderedLocusNames=Sph21_0472 {ECO:0000313|EMBL:ADZ77054.1};
OS   Sphingobacterium sp. (strain 21).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ77054.1};
RN   [1] {ECO:0000313|EMBL:ADZ77054.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=21 {ECO:0000313|EMBL:ADZ77054.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA   Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT   "Complete sequence of Sphingobacterium sp. 21.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family.
CC       {ECO:0000256|ARBA:ARBA00008834, ECO:0000256|RuleBase:RU361169}.
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DR   EMBL; CP002584; ADZ77054.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4C6L8; -.
DR   STRING; 743722.Sph21_0472; -.
DR   KEGG; shg:Sph21_0472; -.
DR   PATRIC; fig|743722.3.peg.513; -.
DR   eggNOG; COG5434; Bacteria.
DR   HOGENOM; CLU_016031_8_3_10; -.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR000743; Glyco_hydro_28.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR024535; Pectate_lyase_SF_prot.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR31339; PECTIN LYASE-RELATED; 1.
DR   PANTHER; PTHR31339:SF9; PLASMIN AND FIBRONECTIN-BINDING PROTEIN A; 1.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   Pfam; PF12708; Pectate_lyase_3; 1.
DR   SMART; SM00710; PbH1; 3.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS00502; POLYGALACTURONASE; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361169};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361169};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..485
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003307485"
FT   DOMAIN          70..122
FT                   /note="Pectate lyase superfamily protein"
FT                   /evidence="ECO:0000259|Pfam:PF12708"
SQ   SEQUENCE   485 AA;  54988 MW;  5363D7EBA943CECA CRC64;
     MYNKLNKRYS FLSKRSFQFR FLSFIFMSAW SINSYAQEKA WTSAKQPEQE MEMLKRQIKA
     PVFPERDFLI TDFGAVGDGL TKNTEAFKKA IEACHNNGGG RVVVPYGKFL TGGIYLKSNV
     NLHLADSATI VFSRDSSDYP IVFTRWEGME CMNYASFIYA YGEENIAVTG NGILDGNANN
     DYWWWWCGAK KYGWREELGK QTPARNALHE MMHEEVDPKK RIFGDGHYLR PNFIQPYQCK
     NVWIADVKLI NSPMWNLNPV LCENVLIEKV KVISHGPNND GCDPEACKNV WIRDCYFDTG
     DDCIAIKSGR DEDGRNIGRP AENHIIENCV MKDGHGGVVI GSEIAGGAKN IYAINCEMDS
     PNLDRVLRIK TSSSRGGIIE NVFMKNVQVG TFKEAAVKCN MFYEKPGNHI PTIRNIWVEN
     LNVEKGGQYA LMVAAYQQSP VTNLRMINCN LKGIKEPFKV DHVKNLVFED VKINGRVMEA
     PKGIN
//
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