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PEB1A_CAMJE
ID   PEB1A_CAMJE             Reviewed;         259 AA.
AC   Q0P9X8; P45678;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Major cell-binding factor;
DE   AltName: Full=CBF1;
DE   AltName: Full=PEB1;
DE   Flags: Precursor;
GN   Name=peb1A; OrderedLocusNames=Cj0921c;
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   PROTEIN SEQUENCE OF 27-53.
RX   PubMed=1885571; DOI=10.1016/s0021-9258(18)55306-0;
RA   Pei Z., Ellison R.T. III, Blaser M.J.;
RT   "Identification, purification, and characterization of major antigenic
RT   proteins of Campylobacter jejuni.";
RL   J. Biol. Chem. 266:16363-16369(1991).
CC   -!- FUNCTION: Common antigen and a major cell adherence molecule. Most
CC       probably involved, with PEB1C, in a binding-protein-dependent transport
CC       system for an amino acid. May be involved in binding to intestinal
CC       cells.
CC   -!- SUBCELLULAR LOCATION: Cell surface.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC       {ECO:0000305}.
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DR   EMBL; AL111168; CAL35041.1; -; Genomic_DNA.
DR   PIR; A48518; A48518.
DR   RefSeq; WP_002853252.1; NC_002163.1.
DR   RefSeq; YP_002344319.1; NC_002163.1.
DR   PDB; 2V25; X-ray; 1.49 A; A/B=1-259.
DR   PDBsum; 2V25; -.
DR   AlphaFoldDB; Q0P9X8; -.
DR   SMR; Q0P9X8; -.
DR   IntAct; Q0P9X8; 90.
DR   STRING; 192222.Cj0921c; -.
DR   TCDB; 3.A.1.3.16; the atp-binding cassette (abc) superfamily.
DR   PaxDb; Q0P9X8; -.
DR   PRIDE; Q0P9X8; -.
DR   EnsemblBacteria; CAL35041; CAL35041; Cj0921c.
DR   GeneID; 906008; -.
DR   KEGG; cje:Cj0921c; -.
DR   PATRIC; fig|192222.6.peg.905; -.
DR   eggNOG; COG0834; Bacteria.
DR   HOGENOM; CLU_019602_18_4_7; -.
DR   OMA; YIAGIRM; -.
DR   EvolutionaryTrace; Q0P9X8; -.
DR   PRO; PR:Q0P9X8; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   InterPro; IPR018313; SBP_3_CS.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   SMART; SM00062; PBPb; 1.
DR   PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Reference proteome; Signal;
KW   Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:1885571"
FT   CHAIN           27..259
FT                   /note="Major cell-binding factor"
FT                   /id="PRO_0000031772"
FT   HELIX           30..37
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          40..44
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   TURN            56..58
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   HELIX           64..77
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          82..87
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   HELIX           93..98
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   HELIX           113..116
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          125..135
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   HELIX           136..138
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          150..154
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   HELIX           159..169
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          175..181
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   HELIX           182..190
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          193..200
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   HELIX           201..204
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   TURN            205..207
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          212..214
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          220..224
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   HELIX           233..245
FT                   /evidence="ECO:0007829|PDB:2V25"
FT   HELIX           247..256
FT                   /evidence="ECO:0007829|PDB:2V25"
SQ   SEQUENCE   259 AA;  28178 MW;  DA132ECE87BBCBD5 CRC64;
     MVFRKSLLKL AVFALGACVA FSNANAAEGK LESIKSKGQL IVGVKNDVPH YALLDQATGE
     IKGFEVDVAK LLAKSILGDD KKIKLVAVNA KTRGPLLDNG SVDAVIATFT ITPERKRIYN
     FSEPYYQDAI GLLVLKEKKY KSLADMKGAN IGVAQAATTK KAIGEAAKKI GIDVKFSEFP
     DYPSIKAALD AKRVDAFSVD KSILLGYVDD KSEILPDSFE PQSYGIVTKK DDPAFAKYVD
     DFVKEHKNEI DALAKKWGL
 
 
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