Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein glycosylation K (EC 3.6.3.39)

 PGLK_CAMJE              Reviewed;         564 AA.
Q0P9C4;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
18-APR-2012, sequence version 1.
25-OCT-2017, entry version 32.
RecName: Full=Protein glycosylation K;
EC=3.6.3.39 {ECO:0000269|PubMed:16498400, ECO:0000269|PubMed:26266984};
Name=pglK; Synonyms=wlaB; OrderedLocusNames=Cj1130c;
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
NCTC 11168).
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Campylobacteraceae; Campylobacter.
NCBI_TaxID=192222;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700819 / NCTC 11168;
PubMed=10688204; DOI=10.1038/35001088;
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W.,
Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
Whitehead S., Barrell B.G.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni
reveals hypervariable sequences.";
Nature 403:665-668(2000).
[2]
IDENTIFICATION.
STRAIN=ATCC 700819 / NCTC 11168;
PubMed=9720026; DOI=10.1099/00221287-144-8-2049;
Fry B.N., Korolik V., ten Brinke J.A., Pennings M.T.T., Zalm R.,
Teunis B.J.J., Coloe P.J., van der Zeijst B.A.M.;
"The lipopolysaccharide biosynthesis locus of Campylobacter jejuni
81116.";
Microbiology 144:2049-2061(1998).
[3]
FUNCTION, PATHWAY, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-388;
SER-389; GLY-488; ARG-492 AND LEU-506, AND CATALYTIC ACTIVITY.
STRAIN=ATCC 700819 / NCTC 11168;
PubMed=16498400; DOI=10.1038/sj.emboj.7601024;
Alaimo C., Catrein I., Morf L., Marolda C.L., Callewaert N.,
Valvano M.A., Feldman M.F., Aebi M.;
"Two distinct but interchangeable mechanisms for flipping of lipid-
linked oligosaccharides.";
EMBO J. 25:967-976(2006).
[4]
FUNCTION.
STRAIN=ATCC 700819 / NCTC 11168;
PubMed=16547029; DOI=10.1128/JB.188.7.2427-2434.2006;
Kelly J., Jarrell H., Millar L., Tessier L., Fiori L.M., Lau P.C.,
Allan B., Szymanski C.M.;
"Biosynthesis of the N-linked glycan in Campylobacter jejuni and
addition onto protein through block transfer.";
J. Bacteriol. 188:2427-2434(2006).
[5]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), FUNCTION, SUBCELLULAR
LOCATION, TOPOLOGY, PATHWAY, DOMAIN, CATALYTIC ACTIVITY, SUBUNIT,
REGION, AND MUTAGENESIS OF 46-SER--PRO-67; TYR-50; 53-ARG--LYS-55;
TYR-56; TYR-63; ARG-86; ARG-260; ARG-302; ARG-309 AND GLU-510.
PubMed=26266984; DOI=10.1038/nature14953;
Perez C., Gerber S., Boilevin J., Bucher M., Darbre T., Aebi M.,
Reymond J.L., Locher K.P.;
"Structure and mechanism of an active lipid-linked oligosaccharide
flippase.";
Nature 524:433-438(2015).
-!- FUNCTION: Mediates the ATP-dependent translocation of the
undecaprenylpyrophosphate-linked heptasaccharide intermediate
across the cell membrane; this is an essential step during the N-
linked protein glycosylation pathway. Transport across the
membrane is effected via ATP-driven conformation changes. Most
likely, only the polar and charged part of the glycolipid enter
the substrate-binding cavity, and the lipid tail remains exposed
to the membrane lipids during the transmembrane flipping process.
{ECO:0000269|PubMed:16498400, ECO:0000269|PubMed:16547029,
ECO:0000269|PubMed:26266984}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + lipopolysaccharide(In) = ADP +
phosphate + lipopolysaccharide(Out). {ECO:0000269|PubMed:16498400,
ECO:0000269|PubMed:26266984}.
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000269|PubMed:16498400, ECO:0000269|PubMed:26266984}.
-!- SUBUNIT: Homodimer; domain-swapped. Helices that arise in
transmembrane regions 4 and 5 from one subunit cross over and
contact the nucleotide-binding domain from the other subunit.
{ECO:0000269|PubMed:26266984}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000305|PubMed:26266984}; Multi-pass membrane protein
{ECO:0000269|PubMed:26266984, ECO:0000305}.
-!- DOMAIN: In the absence of ligand, the homodimer has a V-shaped
structure with a large cavity that is accessible from the
cytoplasmic side. {ECO:0000269|PubMed:26266984}.
-!- DISRUPTION PHENOTYPE: Hypoglycosylation phenotype.
{ECO:0000269|PubMed:16498400}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL111168; CAL35247.1; -; Genomic_DNA.
PIR; E81317; E81317.
RefSeq; WP_002858308.1; NC_002163.1.
RefSeq; YP_002344523.1; NC_002163.1.
PDB; 5C73; X-ray; 5.90 A; A/B/C/F/G/K=1-564.
PDB; 5C76; X-ray; 3.94 A; A/B/C/D=1-564.
PDB; 5C78; X-ray; 2.90 A; A/B/C/D=1-564.
PDB; 5NBD; X-ray; 3.90 A; A/B=1-564.
PDBsum; 5C73; -.
PDBsum; 5C76; -.
PDBsum; 5C78; -.
PDBsum; 5NBD; -.
ProteinModelPortal; Q0P9C4; -.
SMR; Q0P9C4; -.
STRING; 192222.Cj1130c; -.
TCDB; 3.A.1.106.15; the atp-binding cassette (abc) superfamily.
PaxDb; Q0P9C4; -.
EnsemblBacteria; CAL35247; CAL35247; Cj1130c.
GeneID; 905421; -.
KEGG; cje:Cj1130c; -.
PATRIC; fig|192222.6.peg.1112; -.
eggNOG; ENOG4105BZ1; Bacteria.
eggNOG; COG1132; LUCA.
KO; K06148; -.
OMA; MSFNAFL; -.
UniPathway; UPA00378; -.
Proteomes; UP000000799; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0015437; F:lipopolysaccharide-transporting ATPase activity; IDA:UniProtKB.
GO; GO:0015772; P:oligosaccharide transport; IDA:UniProtKB.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
Gene3D; 1.20.1560.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00664; ABC_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
Complete proteome; Hydrolase; Membrane; Nucleotide-binding;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 564 Protein glycosylation K.
/FTId=PRO_0000422584.
TOPO_DOM 1 15 Cytoplasmic.
{ECO:0000305|PubMed:26266984}.
TRANSMEM 16 38 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441,
ECO:0000305|PubMed:26266984}.
TOPO_DOM 39 76 Extracellular.
{ECO:0000305|PubMed:26266984}.
TRANSMEM 77 98 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441,
ECO:0000305|PubMed:26266984}.
TOPO_DOM 99 149 Cytoplasmic.
{ECO:0000305|PubMed:26266984}.
TRANSMEM 150 170 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441,
ECO:0000305|PubMed:26266984}.
TOPO_DOM 171 173 Extracellular.
{ECO:0000305|PubMed:26266984}.
TRANSMEM 174 197 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441,
ECO:0000305|PubMed:26266984}.
TOPO_DOM 198 254 Cytoplasmic.
{ECO:0000305|PubMed:26266984}.
TRANSMEM 255 276 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441,
ECO:0000305|PubMed:26266984}.
TOPO_DOM 277 292 Extracellular.
{ECO:0000305|PubMed:26266984}.
TRANSMEM 293 314 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441,
ECO:0000305|PubMed:26266984}.
TOPO_DOM 315 564 Cytoplasmic.
{ECO:0000305|PubMed:26266984}.
DOMAIN 17 319 ABC transmembrane type-1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 349 564 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 382 389 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 46 67 Important for stimulation of ATPase
activity by lipid-linked oligosaccharides
and subsequent translocation of lipid-
linked oligosaccharides.
{ECO:0000269|PubMed:26266984}.
MUTAGEN 46 67 SDFSYFDRNKYLISLKEYLNIP->GSSGSSGS:
Abolishes stimulation of ATPase activity
by lipid-linked oligosaccharide binding.
Abolishes translocation of lipid-linked
oligosaccharide.
{ECO:0000269|PubMed:26266984}.
MUTAGEN 50 50 Y->A: Abolishes stimulation of ATPase
activity by lipid-linked oligosaccharide
binding and decreases translocation of
lipid-linked oligosaccharide; when
associated with A-56 and A-63.
{ECO:0000269|PubMed:26266984}.
MUTAGEN 53 55 RNK->ANA: Abolishes stimulation of ATPase
activity by lipid-linked oligosaccharide
binding. Strongly decreases translocation
of lipid-linked oligosaccharide.
{ECO:0000269|PubMed:26266984}.
MUTAGEN 56 56 Y->A: Abolishes stimulation of ATPase
activity by lipid-linked oligosaccharide
binding and decreases translocation of
lipid-linked oligosaccharide; when
associated with A-50 and A-63.
{ECO:0000269|PubMed:26266984}.
MUTAGEN 63 63 Y->A: Abolishes stimulation of ATPase
activity by lipid-linked oligosaccharide
binding and decreases translocation of
lipid-linked oligosaccharide; when
associated with A-50 and A-56.
{ECO:0000269|PubMed:26266984}.
MUTAGEN 86 86 R->A: Abolishes translocation of lipid-
linked oligosaccharide; when associated
with A-260; A-302 and A-309.
{ECO:0000269|PubMed:26266984}.
MUTAGEN 260 260 R->A: Abolishes translocation of lipid-
linked oligosaccharide; when associated
with A-86; A-302 and A-309.
{ECO:0000269|PubMed:26266984}.
MUTAGEN 302 302 R->A: Abolishes translocation of lipid-
linked oligosaccharide; when associated
with A-86; A-260 and A-309.
{ECO:0000269|PubMed:26266984}.
MUTAGEN 309 309 R->A: Abolishes translocation of lipid-
linked oligosaccharide; when associated
with A-86; A-260 and A-302.
{ECO:0000269|PubMed:26266984}.
MUTAGEN 388 388 K->A: Reduced efficiency of the N-linked
protein glycosylation pathway.
{ECO:0000269|PubMed:16498400}.
MUTAGEN 389 389 S->A: Impaired N-linked protein
glycosylation pathway.
{ECO:0000269|PubMed:16498400}.
MUTAGEN 488 488 G->D: Impaired N-linked protein
glycosylation pathway.
{ECO:0000269|PubMed:16498400}.
MUTAGEN 492 492 R->C: No effect on the N-linked protein
glycosylation pathway.
{ECO:0000269|PubMed:16498400}.
MUTAGEN 506 506 L->A: Reduced efficiency of the N-linked
protein glycosylation pathway.
{ECO:0000269|PubMed:16498400}.
MUTAGEN 510 510 E->Q: Abolishes ATPase activity and
strongly reduces translocation of lipid-
linked oligosaccharide.
{ECO:0000269|PubMed:26266984}.
SEQUENCE 564 AA; 64739 MW; 00C8D00B231EACF3 CRC64;
MLKKLFFILS KEDKNFLFFL LVFSVFISFI ETFAISLVMP FITLASDFSY FDRNKYLISL
KEYLNIPVFE IIVYFGVGLI VFYVFRALLN AYYFHLLARF SKGRYHAIAY KVFSKFLNIN
YEKFTQKNQS EILKSITGEV YNLSTMISSF LLLMSEIFVV LLLYALMLLI NYKITLFLSI
FMVLNAFILV KILSPIIKKA GVRREEAMKN FFEILNTNLN NFKFIKLKTK EDGVLSLFKA
QSEAFSKANI TNESVAAVPR IYLEGIGFCV LVFIVVFLVL KNESDISGIL STISIFVLAL
YRLMPSANRI ITSYHDLLYY HSSLDIIYQN LRQEEENLGE EKLSFNQELK ICNLSFGYEG
KKYLFKNLNL NIKKGEKIAF IGESGCGKST LVDLIIGLLK PKEGQILIDE QELNANNTKN
YRQKIGYIPQ NIYLFNDSIA KNITFGDAVD EEKLNRVIKQ ANLEHFIKNL PQGVQTKVGD
GGSNLSGGQK QRIAIARALY LEPEMLVLDE ATSALDTQSE AKIMDEIYKI SKDKTMIIIA
HRLSTITQCD KVYRLEHGKL KEEK


Related products :

Catalog number Product name Quantity
U0263h CLIA Advanced glycosylation end product-specific receptor,AGER,Homo sapiens,Human,RAGE,Receptor for advanced glycosylation end products 96T
E0263h ELISA Advanced glycosylation end product-specific receptor,AGER,Homo sapiens,Human,RAGE,Receptor for advanced glycosylation end products 96T
E0263h ELISA kit Advanced glycosylation end product-specific receptor,AGER,Homo sapiens,Human,RAGE,Receptor for advanced glycosylation end products 96T
E0263m ELISA Advanced glycosylation end product-specific receptor,Ager,Mouse,Mus musculus,Rage,Receptor for advanced glycosylation end products 96T
E0263m ELISA kit Advanced glycosylation end product-specific receptor,Ager,Mouse,Mus musculus,Rage,Receptor for advanced glycosylation end products 96T
E0263r ELISA kit Advanced glycosylation end product-specific receptor,Ager,Rage,Rat,Rattus norvegicus,Receptor for advanced glycosylation end products 96T
E0263r ELISA Advanced glycosylation end product-specific receptor,Ager,Rage,Rat,Rattus norvegicus,Receptor for advanced glycosylation end products 96T
U0263b CLIA Advanced glycosylation end product-specific receptor,AGER,Bos taurus,Bovine,RAGE,Receptor for advanced glycosylation end products 96T
U0263m CLIA Advanced glycosylation end product-specific receptor,Ager,Mouse,Mus musculus,Rage,Receptor for advanced glycosylation end products 96T
E0263b ELISA kit Advanced glycosylation end product-specific receptor,AGER,Bos taurus,Bovine,RAGE,Receptor for advanced glycosylation end products 96T
U0263r CLIA Advanced glycosylation end product-specific receptor,Ager,Rage,Rat,Rattus norvegicus,Receptor for advanced glycosylation end products 96T
E0263b ELISA Advanced glycosylation end product-specific receptor,AGER,Bos taurus,Bovine,RAGE,Receptor for advanced glycosylation end products 96T
orb81387 Human Advanced Glycosylation End Product-Specific Receptor protein Proteins 2
orb81388 Human Advanced Glycosylation End Product-Specific Receptor HEK protein Proteins 2
bs-1158P Proteins: AGEs (advanced glycosylation end products) Protein Length: 12-25 amino acids. 200ug lyophilized
bs-0177P Peptides: AGER(Advanced glycosylation end product-specific receptor) Protein Length:12-25 amino acids. 200ug lyophilized
30-591 The GALNT13 protein is a member of the UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase (GalNAcT; EC 2.4.1.41) family, which initiate O-linked glycosylation of mucins b 0.05 mg
26-493 The GALNT13 protein is a member of the UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase (GalNAcT; EC 2.4.1.41) family, which initiate O-linked glycosylation of mucins b 0.05 mg
29-576 MUC1 is a membrane bound, glycosylated phosphoprotein. The protein is anchored to the apical surface of many epithelia by a transmembrane domain, with the degree of glycosylation varying with cell typ 0.05 mg
29-577 MUC1 is a membrane bound, glycosylated phosphoprotein. The protein is anchored to the apical surface of many epithelia by a transmembrane domain, with the degree of glycosylation varying with cell typ 0.1 mg
EIAAB25336 Homo sapiens,Human,Mannose-P-dolichol utilization defect 1 protein,MPDU1,SL15,Suppressor of Lec15 and Lec35 glycosylation mutation homolog
EIAAB25335 Mannose-P-dolichol utilization defect 1 protein,Mouse,Mpdu1,Mus musculus,SL15,Supl15h,Suppressor of Lec15 and Lec35 glycosylation mutation homolog
26-016 SIL1 is a resident endoplasmic reticulum (ER), N-linked glycoprotein with an N-terminal ER targeting sequence, 2 putative N-glycosylation sites, and a C-terminal ER retention signal. This protein func 0.05 mg
31-363 SIL1 is a resident endoplasmic reticulum (ER), N-linked glycoprotein with an N-terminal ER targeting sequence, 2 putative N-glycosylation sites, and a C-terminal ER retention signal. This protein func 0.05 mg
orb80645 Rat VEGF-C (152) protein VEGF -C 152 Rat Recombinant contains 152 amino acids residues and was fused to His-tag (6x His) at the C-terminal end. As result of glycosylation VEGF-C migrates as an 18-24 k 2


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur