ID F1SWG1_CAMRE Unreviewed; 257 AA.
AC F1SWG1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Chaperone protein dnaJ {ECO:0000313|EMBL:BAK09218.1};
DE Flags: Fragment;
GN Name=dnaJ {ECO:0000313|EMBL:BAK09218.1};
OS Campylobacter rectus (Wolinella recta).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=203 {ECO:0000313|EMBL:BAK09218.1};
RN [1] {ECO:0000313|EMBL:BAK09218.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 6301 {ECO:0000313|EMBL:BAK09218.1};
RA Hung P.V., Zhang J., Hayashi M., Yoshoda S., Ohkusu K., Ezaki T.;
RT "Phylogenetic Analysis of Genus Campylobacter Based on hose keeping genes
RT for species Identification.";
RL Diagn. Microbiol. Infect. Dis. 0:0-0(2010).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB542735; BAK09218.1; -; Genomic_DNA.
DR AlphaFoldDB; F1SWG1; -.
DR GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10747; DnaJ_C; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR43096:SF48; CHAPERONE PROTEIN DNAJ; 1.
DR PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 4: Predicted;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00546};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00546}.
FT DOMAIN 1..38
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 103..180
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 103..180
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAK09218.1"
FT NON_TER 257
FT /evidence="ECO:0000313|EMBL:BAK09218.1"
SQ SEQUENCE 257 AA; 28268 MW; 36227A0D66D3E2BE CRC64;
HPDRNQGDKE AEEKFKLVNE AYQVLSDEEK RAIYDRYGKA GLESRGGFSS GGFSADFDLG
DIFNSFFGGG FGPGASSRKK STGKYPLDIE IALRIKFNEA VFGAEKELEF TIKKPCQTCK
GSGSKDGKTH VCPHCEGRGR ISQQRGFMSF VQECPYCNGT GETIKDRCSG CGGSGYKEER
QSVKVNIPEG IDDGMRMRVS EKGNVSSTGA RGDLYVHIEV EADEHFVRHE NDVYIEIPVF
FTQAVLGETI TIPTLKG
//