ID Q0PBL7_CAMJE Unreviewed; 250 AA.
AC Q0PBL7;
DT 19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 19-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Major antigenic peptide PEB3 {ECO:0000313|EMBL:CAL34442.1};
GN Name=peb3 {ECO:0000313|EMBL:CAL34442.1};
GN OrderedLocusNames=Cj0289c {ECO:0000313|EMBL:CAL34442.1};
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222 {ECO:0000313|EMBL:CAL34442.1, ECO:0000313|Proteomes:UP000000799};
RN [1] {ECO:0000313|EMBL:CAL34442.1, ECO:0000313|Proteomes:UP000000799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000313|Proteomes:UP000000799};
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K., Ketley J.M., Churcher C., Basham D.,
RA Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K.,
RA Karlyshev A., Moule S., Pallen M.J., Penn C.W., Quail M., Rajandream M.A.,
RA Rutherford K.M., VanVliet A., Whitehead S., 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] {ECO:0007829|PDB:2HXW}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 21-250.
RX PubMed=17456748; DOI=10.1110/ps.062737507;
RA Rangarajan E.S., Bhatia S., Watson D.C., Munger C., Cygler M., Matte A.,
RA Young N.M.;
RT "Structural context for protein N-glycosylation in bacteria: The structure
RT of PEB3, an adhesin from Campylobacter jejuni.";
RL Protein Sci. 16:990-995(2007).
RN [3] {ECO:0007829|PDB:3FIR, ECO:0007829|PDB:3FJ7}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH
RP (2R)-3-PHOSPHOGLYCERATE.
RX PubMed=19236052; DOI=10.1021/bi802195d;
RA Min T., Vedadi M., Watson D.C., Wasney G.A., Munger C., Cygler M.,
RA Matte A., Young N.M.;
RT "Specificity of Campylobacter jejuni adhesin PEB3 for phosphates and
RT structural differences among its ligand complexes.";
RL Biochemistry 48:3057-3067(2009).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic sulfate-binding protein family.
CC {ECO:0000256|ARBA:ARBA00006099}.
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DR EMBL; AL111168; CAL34442.1; -; Genomic_DNA.
DR PIR; G81447; G81447.
DR RefSeq; WP_002857286.1; NZ_SZUC01000004.1.
DR RefSeq; YP_002343730.1; NC_002163.1.
DR PDB; 2HXW; X-ray; 1.60 A; A/B=21-250.
DR PDB; 3FIR; X-ray; 2.00 A; A/B=1-250.
DR PDB; 3FJ7; X-ray; 1.70 A; A/B=21-250.
DR PDB; 3FJG; X-ray; 2.20 A; A/B/C/D=1-250.
DR PDB; 3FJM; X-ray; 1.60 A; A/B=1-250.
DR PDBsum; 2HXW; -.
DR PDBsum; 3FIR; -.
DR PDBsum; 3FJ7; -.
DR PDBsum; 3FJG; -.
DR PDBsum; 3FJM; -.
DR AlphaFoldDB; Q0PBL7; -.
DR SMR; Q0PBL7; -.
DR IntAct; Q0PBL7; 24.
DR STRING; 192222.Cj0289c; -.
DR PaxDb; 192222-Cj0289c; -.
DR EnsemblBacteria; CAL34442; CAL34442; Cj0289c.
DR GeneID; 904613; -.
DR KEGG; cje:Cj0289c; -.
DR PATRIC; fig|192222.6.peg.282; -.
DR eggNOG; COG4588; Bacteria.
DR HOGENOM; CLU_084206_0_0_7; -.
DR OrthoDB; 9802127at2; -.
DR EvolutionaryTrace; Q0PBL7; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:1902358; P:sulfate transmembrane transport; IEA:InterPro.
DR CDD; cd13519; PBP2_PEB3_AcfC; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR005669; Thiosulph/SO4-bd.
DR PANTHER; PTHR30368; SULFATE-BINDING PROTEIN; 1.
DR PANTHER; PTHR30368:SF1; THIOSULFATE-BINDING PROTEIN; 1.
DR Pfam; PF13531; SBP_bac_11; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2HXW, ECO:0007829|PDB:3FIR};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000000799};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..250
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004175477"
FT BINDING 28
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0007829|PDB:3FJG"
FT BINDING 138
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0007829|PDB:3FJG"
FT BINDING 139
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0007829|PDB:3FJG"
FT BINDING 171
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0007829|PDB:3FJG"
FT BINDING 172
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0007829|PDB:3FJG"
SQ SEQUENCE 250 AA; 27537 MW; B2A9AF0630A04065 CRC64;
MKKIITLFGA CALAFSMANA DVNLYGPGGP HTALKDIANK YSEKTGVKVN VNFGPQATWF
EKAKKDADIL FGASDQSALA IASDFGKDFN VSKIKPLYFR EAIILTQKGN PLKIKGLKDL
ANKKVRIVVP EGAGKSNTSG TGVWEDMIGR TQDIKTIQNF RNNIVAFVPN SGSARKLFAQ
DQADAWITWI DWSKSNPDIG TAVAIEKDLV VYRTFNVIAK EGASKETQDF IAYLSSKEAK
EIFKKYGWRE
//
