GLCSF_BACTN
ID GLCSF_BACTN Reviewed; 558 AA.
AC Q89YS5;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=N-acetylglucosamine-6-O-sulfatase {ECO:0000303|PubMed:25002587};
DE EC=3.1.6.- {ECO:0000269|PubMed:25002587};
GN OrderedLocusNames=BT_4656 {ECO:0000312|EMBL:AAO79761.1};
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25002587; DOI=10.1074/jbc.m114.573303;
RA Ulmer J.E., Vilen E.M., Namburi R.B., Benjdia A., Beneteau J., Malleron A.,
RA Bonnaffe D., Driguez P.A., Descroix K., Lassalle G., Le Narvor C.,
RA Sandstroem C., Spillmann D., Berteau O.;
RT "Characterization of glycosaminoglycan (GAG) sulfatases from the human gut
RT symbiont Bacteroides thetaiotaomicron reveals the first GAG-specific
RT bacterial endosulfatase.";
RL J. Biol. Chem. 289:24289-24303(2014).
RN [4] {ECO:0007744|PDB:5G2V}
RP X-RAY CRYSTALLOGRAPHY (1.39 ANGSTROMS) OF 45-558.
RA Cartmell A., Lowe E.C., Basle A., Crouch L.I., Czjzek M., Turnbull J.,
RA Henrissat B., Terrapon N., Thomas S., Murray H., Firbank S.J., Bolam D.N.;
RT "Metabolism of host GAGs by the human gut bacterium Bacteroides
RT thetaiotaomicron.";
RL Submitted (APR-2016) to the PDB data bank.
CC -!- FUNCTION: Exosulfatase involved in the degradation of the
CC glycosaminoglycan (GAG) heparan sulfate (HS). Catalyzes the hydrolysis
CC of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units
CC (PubMed:25002587). GAG-specific sulfatases play a key role in the
CC persistence of the major human gut symbiont B.thetaiotaomicron in the
CC host gastrointestinal tract (PubMed:25002587).
CC {ECO:0000269|PubMed:25002587, ECO:0000305|PubMed:25002587}.
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity.
CC {ECO:0000250|UniProtKB:Q9X759}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; AE015928; AAO79761.1; -; Genomic_DNA.
DR RefSeq; NP_813567.1; NC_004663.1.
DR PDB; 5G2V; X-ray; 1.39 A; A=45-558.
DR PDBsum; 5G2V; -.
DR AlphaFoldDB; Q89YS5; -.
DR SMR; Q89YS5; -.
DR STRING; 226186.BT_4656; -.
DR PaxDb; Q89YS5; -.
DR PRIDE; Q89YS5; -.
DR EnsemblBacteria; AAO79761; AAO79761; BT_4656.
DR KEGG; bth:BT_4656; -.
DR PATRIC; fig|226186.12.peg.4737; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_9_3_10; -.
DR InParanoid; Q89YS5; -.
DR OMA; VHYEEAM; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR032506; DUF4976.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF16347; DUF4976; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
DR PROSITE; PS00149; SULFATASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..558
FT /note="N-acetylglucosamine-6-O-sulfatase"
FT /id="PRO_0000446231"
FT MOD_RES 101
FT /note="3-oxoalanine (Ser)"
FT /evidence="ECO:0000250|UniProtKB:Q9X759"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:5G2V"
FT TURN 233..238
FT /evidence="ECO:0007829|PDB:5G2V"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:5G2V"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:5G2V"
FT TURN 271..275
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 300..318
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 324..359
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 366..374
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:5G2V"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 421..428
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:5G2V"
FT TURN 447..450
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 475..480
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 482..492
FT /evidence="ECO:0007829|PDB:5G2V"
FT STRAND 495..500
FT /evidence="ECO:0007829|PDB:5G2V"
FT TURN 501..503
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:5G2V"
FT HELIX 518..534
FT /evidence="ECO:0007829|PDB:5G2V"
SQ SEQUENCE 558 AA; 64585 MW; 07EB36AE3D116B26 CRC64;
MPATEKASAP HWSFLSSDVI SIMKSNPSTL LLPLAALSLA SCANPQKEET KRPNIIFMMT
DDHTTQAMSC YGGNLIQTPN MDRIANEGIR FDNCYAVNAL SGPSRACILT GKFSHENGFT
DNASTFNGDQ QTFPKLLQQA GYQTAMIGKW HLISEPQGFD HWSILSGQHE QGDYYDPDFW
EDGKHIVEKG YATDIITDKA INFLENRDKN KPFCMMYHQK APHRNWMPAP RHLGIFNNTI
FPEPANLFDD YEGRGKAARE QDMSIEHTLT NDWDLKLLTR EEMLKDTTNR LYSVYKRMPS
EVQDKWDSAY AQRIAEYRKG DLKGKALISW KYQQYMRDYL ATVLAVDENI GRLLNYLEKI
GELDNTIIVY TSDQGFFLGE HGWFDKRFMY EECQRMPLII RYPKAIKAGS TSSAISMNVD
FAPTFLDFAG VEVPSDIQGA SLKPVLENEG KTPADWRKAA YYHYYEYPAE HSVKRHYGIR
TQDFKLIHFY NDIDEWEMYD MKADPREMNN IFGKAEYAKK QKELMQLLEE TQKQYKDNDP
DEKETVLFKG DRRLMENR
