CBF2_CAMJJ
ID CBF2_CAMJJ Reviewed; 273 AA.
AC A1VYV6; Q46105;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Putative peptidyl-prolyl cis-trans isomerase Cbf2;
DE Short=PPIase Cbf2;
DE EC=5.2.1.8;
DE AltName: Full=Cell-binding factor 2;
DE AltName: Full=Major antigen peb4A;
DE AltName: Full=Rotamase Cbf2;
DE Flags: Precursor;
GN Name=cbf2; Synonyms=peb4A; OrderedLocusNames=CJJ81176_0624;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8525063; DOI=10.1016/0923-2508(96)80292-0;
RA Burucoa C., Fremaux C., Pei Z., Tummuru M., Blaser M.J., Cenatiempo Y.,
RA Fauchere J.L.;
RT "Nucleotide sequence and characterization of peb4A encoding an antigenic
RT protein in Campylobacter jejuni.";
RL Res. Microbiol. 146:467-476(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
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DR EMBL; X84703; CAA59175.1; -; Genomic_DNA.
DR EMBL; CP000538; EAQ73401.1; -; Genomic_DNA.
DR PIR; S52412; S52412.
DR RefSeq; WP_002856774.1; NC_008787.1.
DR AlphaFoldDB; A1VYV6; -.
DR SMR; A1VYV6; -.
DR STRING; 354242.CJJ81176_0624; -.
DR EnsemblBacteria; EAQ73401; EAQ73401; CJJ81176_0624.
DR KEGG; cjj:CJJ81176_0624; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_1_1_7; -.
DR OMA; YEQAKPT; -.
DR Proteomes; UP000000646; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase; Rotamase; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..273
FT /note="Putative peptidyl-prolyl cis-trans isomerase Cbf2"
FT /id="PRO_0000281896"
FT DOMAIN 131..228
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT CONFLICT 10
FT /note="A -> T (in Ref. 1; CAA59175)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="A -> V (in Ref. 1; CAA59175)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="A -> T (in Ref. 1; CAA59175)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 30430 MW; 46E94403BB70D12F CRC64;
MKKFSLVAAA LIAGVALNVN AATVATVNGK SISDAEVSEF FAPMLRGQDF KTLPDNQKKA
LIQQYIMQDL ILQDAKKQNL EKDPLYTKEL DRAKDAILVN VYQEKILNTI KIDAAKVKAF
YDQNKDKYVK PARVQAKHIL VATEKEAKDI INELKGLKGK ELDAKFSELA KEKSIDPGSK
NQGGELGWFD QSTMVKPFTD AAFALKNGTI TTTPVKTNFG YHVILKENSQ AKGQIKFDEV
KQGIENGLKF EEFKKVINQK GQDLLNSAKV EYK
