PGLK_CAMJE
ID PGLK_CAMJE Reviewed; 564 AA.
AC Q0P9C4;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Protein glycosylation K;
DE EC=7.5.2.5 {ECO:0000269|PubMed:16498400, ECO:0000269|PubMed:26266984};
GN Name=pglK; Synonyms=wlaB; OrderedLocusNames=Cj1130c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP IDENTIFICATION.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=9720026; DOI=10.1099/00221287-144-8-2049;
RA Fry B.N., Korolik V., ten Brinke J.A., Pennings M.T.T., Zalm R.,
RA Teunis B.J.J., Coloe P.J., van der Zeijst B.A.M.;
RT "The lipopolysaccharide biosynthesis locus of Campylobacter jejuni 81116.";
RL Microbiology 144:2049-2061(1998).
RN [3]
RP FUNCTION, PATHWAY, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-388; SER-389;
RP GLY-488; ARG-492 AND LEU-506, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=16498400; DOI=10.1038/sj.emboj.7601024;
RA Alaimo C., Catrein I., Morf L., Marolda C.L., Callewaert N., Valvano M.A.,
RA Feldman M.F., Aebi M.;
RT "Two distinct but interchangeable mechanisms for flipping of lipid-linked
RT oligosaccharides.";
RL EMBO J. 25:967-976(2006).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=16547029; DOI=10.1128/jb.188.7.2427-2434.2006;
RA Kelly J., Jarrell H., Millar L., Tessier L., Fiori L.M., Lau P.C.,
RA Allan B., Szymanski C.M.;
RT "Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition
RT onto protein through block transfer.";
RL J. Bacteriol. 188:2427-2434(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION,
RP TOPOLOGY, PATHWAY, DOMAIN, CATALYTIC ACTIVITY, SUBUNIT, REGION, AND
RP MUTAGENESIS OF 46-SER--PRO-67; TYR-50; 53-ARG--LYS-55; TYR-56; TYR-63;
RP ARG-86; ARG-260; ARG-302; ARG-309 AND GLU-510.
RX PubMed=26266984; DOI=10.1038/nature14953;
RA Perez C., Gerber S., Boilevin J., Bucher M., Darbre T., Aebi M.,
RA Reymond J.L., Locher K.P.;
RT "Structure and mechanism of an active lipid-linked oligosaccharide
RT flippase.";
RL Nature 524:433-438(2015).
CC -!- FUNCTION: Mediates the ATP-dependent translocation of the
CC undecaprenylpyrophosphate-linked heptasaccharide intermediate across
CC the cell membrane; this is an essential step during the N-linked
CC protein glycosylation pathway. Transport across the membrane is
CC effected via ATP-driven conformation changes. Most likely, only the
CC polar and charged part of the glycolipid enter the substrate-binding
CC cavity, and the lipid tail remains exposed to the membrane lipids
CC during the transmembrane flipping process.
CC {ECO:0000269|PubMed:16498400, ECO:0000269|PubMed:16547029,
CC ECO:0000269|PubMed:26266984}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + lipopolysaccharideSide 1 = ADP + phosphate +
CC lipopolysaccharideSide 2.; EC=7.5.2.5;
CC Evidence={ECO:0000269|PubMed:16498400, ECO:0000269|PubMed:26266984};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:16498400, ECO:0000269|PubMed:26266984}.
CC -!- SUBUNIT: Homodimer; domain-swapped. Helices that arise in transmembrane
CC regions 4 and 5 from one subunit cross over and contact the nucleotide-
CC binding domain from the other subunit. {ECO:0000269|PubMed:26266984}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:26266984}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:26266984, ECO:0000305}.
CC -!- DOMAIN: In the absence of ligand, the homodimer has a V-shaped
CC structure with a large cavity that is accessible from the cytoplasmic
CC side. {ECO:0000269|PubMed:26266984}.
CC -!- DISRUPTION PHENOTYPE: Hypoglycosylation phenotype.
CC {ECO:0000269|PubMed:16498400}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; AL111168; CAL35247.1; -; Genomic_DNA.
DR PIR; E81317; E81317.
DR RefSeq; WP_002858308.1; NC_002163.1.
DR RefSeq; YP_002344523.1; NC_002163.1.
DR PDB; 5C73; X-ray; 5.90 A; A/B/C/F/G/K=1-564.
DR PDB; 5C76; X-ray; 3.94 A; A/B/C/D=1-564.
DR PDB; 5C78; X-ray; 2.90 A; A/B/C/D=1-564.
DR PDB; 5NBD; X-ray; 3.90 A; A/B=1-564.
DR PDBsum; 5C73; -.
DR PDBsum; 5C76; -.
DR PDBsum; 5C78; -.
DR PDBsum; 5NBD; -.
DR AlphaFoldDB; Q0P9C4; -.
DR SMR; Q0P9C4; -.
DR STRING; 192222.Cj1130c; -.
DR TCDB; 3.A.1.106.15; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q0P9C4; -.
DR PRIDE; Q0P9C4; -.
DR ABCD; Q0P9C4; 1 sequenced antibody.
DR EnsemblBacteria; CAL35247; CAL35247; Cj1130c.
DR GeneID; 905421; -.
DR KEGG; cje:Cj1130c; -.
DR PATRIC; fig|192222.6.peg.1112; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_7; -.
DR OMA; MSFNAFL; -.
DR BioCyc; MetaCyc:MON-21510; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015437; F:lipopolysaccharide floppase activity; IDA:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..564
FT /note="Protein glycosylation K"
FT /id="PRO_0000422584"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26266984"
FT TRANSMEM 16..38
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441,
FT ECO:0000305|PubMed:26266984"
FT TOPO_DOM 39..76
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:26266984"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441,
FT ECO:0000305|PubMed:26266984"
FT TOPO_DOM 99..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26266984"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441,
FT ECO:0000305|PubMed:26266984"
FT TOPO_DOM 171..173
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:26266984"
FT TRANSMEM 174..197
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441,
FT ECO:0000305|PubMed:26266984"
FT TOPO_DOM 198..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26266984"
FT TRANSMEM 255..276
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441,
FT ECO:0000305|PubMed:26266984"
FT TOPO_DOM 277..292
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:26266984"
FT TRANSMEM 293..314
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441,
FT ECO:0000305|PubMed:26266984"
FT TOPO_DOM 315..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26266984"
FT DOMAIN 17..319
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 349..564
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 46..67
FT /note="Important for stimulation of ATPase activity by
FT lipid-linked oligosaccharides and subsequent translocation
FT of lipid-linked oligosaccharides"
FT /evidence="ECO:0000269|PubMed:26266984"
FT BINDING 382..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 46..67
FT /note="SDFSYFDRNKYLISLKEYLNIP->GSSGSSGS: Abolishes
FT stimulation of ATPase activity by lipid-linked
FT oligosaccharide binding. Abolishes translocation of lipid-
FT linked oligosaccharide."
FT /evidence="ECO:0000269|PubMed:26266984"
FT MUTAGEN 50
FT /note="Y->A: Abolishes stimulation of ATPase activity by
FT lipid-linked oligosaccharide binding and decreases
FT translocation of lipid-linked oligosaccharide; when
FT associated with A-56 and A-63."
FT /evidence="ECO:0000269|PubMed:26266984"
FT MUTAGEN 53..55
FT /note="RNK->ANA: Abolishes stimulation of ATPase activity
FT by lipid-linked oligosaccharide binding. Strongly decreases
FT translocation of lipid-linked oligosaccharide."
FT /evidence="ECO:0000269|PubMed:26266984"
FT MUTAGEN 56
FT /note="Y->A: Abolishes stimulation of ATPase activity by
FT lipid-linked oligosaccharide binding and decreases
FT translocation of lipid-linked oligosaccharide; when
FT associated with A-50 and A-63."
FT /evidence="ECO:0000269|PubMed:26266984"
FT MUTAGEN 63
FT /note="Y->A: Abolishes stimulation of ATPase activity by
FT lipid-linked oligosaccharide binding and decreases
FT translocation of lipid-linked oligosaccharide; when
FT associated with A-50 and A-56."
FT /evidence="ECO:0000269|PubMed:26266984"
FT MUTAGEN 86
FT /note="R->A: Abolishes translocation of lipid-linked
FT oligosaccharide; when associated with A-260; A-302 and A-
FT 309."
FT /evidence="ECO:0000269|PubMed:26266984"
FT MUTAGEN 260
FT /note="R->A: Abolishes translocation of lipid-linked
FT oligosaccharide; when associated with A-86; A-302 and A-
FT 309."
FT /evidence="ECO:0000269|PubMed:26266984"
FT MUTAGEN 302
FT /note="R->A: Abolishes translocation of lipid-linked
FT oligosaccharide; when associated with A-86; A-260 and A-
FT 309."
FT /evidence="ECO:0000269|PubMed:26266984"
FT MUTAGEN 309
FT /note="R->A: Abolishes translocation of lipid-linked
FT oligosaccharide; when associated with A-86; A-260 and A-
FT 302."
FT /evidence="ECO:0000269|PubMed:26266984"
FT MUTAGEN 388
FT /note="K->A: Reduced efficiency of the N-linked protein
FT glycosylation pathway."
FT /evidence="ECO:0000269|PubMed:16498400"
FT MUTAGEN 389
FT /note="S->A: Impaired N-linked protein glycosylation
FT pathway."
FT /evidence="ECO:0000269|PubMed:16498400"
FT MUTAGEN 488
FT /note="G->D: Impaired N-linked protein glycosylation
FT pathway."
FT /evidence="ECO:0000269|PubMed:16498400"
FT MUTAGEN 492
FT /note="R->C: No effect on the N-linked protein
FT glycosylation pathway."
FT /evidence="ECO:0000269|PubMed:16498400"
FT MUTAGEN 506
FT /note="L->A: Reduced efficiency of the N-linked protein
FT glycosylation pathway."
FT /evidence="ECO:0000269|PubMed:16498400"
FT MUTAGEN 510
FT /note="E->Q: Abolishes ATPase activity and strongly reduces
FT translocation of lipid-linked oligosaccharide."
FT /evidence="ECO:0000269|PubMed:26266984"
SQ 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
