(data stored in ACNUC7421 zone)

SWISSPROT: DJLA_ECO57

ID   DJLA_ECO57              Reviewed;         271 AA.
AC   Q7AHS5; Q8XA12;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 90.
DE   RecName: Full=Co-chaperone protein DjlA {ECO:0000255|HAMAP-Rule:MF_01153};
GN   Name=djlA {ECO:0000255|HAMAP-Rule:MF_01153};
GN   OrderedLocusNames=Z0064, ECs0060;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Regulatory DnaK co-chaperone. Direct interaction between
CC       DnaK and DjlA is needed for the induction of the wcaABCDE operon,
CC       involved in the synthesis of a colanic acid polysaccharide
CC       capsule, possibly through activation of the RcsB/RcsC
CC       phosphotransfer signaling pathway. The colanic acid capsule may
CC       help the bacterium survive conditions outside the host.
CC       {ECO:0000255|HAMAP-Rule:MF_01153}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01153}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01153}; Single-pass type III membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01153}.
CC   -!- DOMAIN: The transmembrane domain is a dimerization domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01153}.
DR   EMBL; AE005174; AAG54360.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33483.1; -; Genomic_DNA.
DR   PIR; D85487; D85487.
DR   PIR; D90636; D90636.
DR   RefSeq; NP_308087.1; NC_002695.1.
DR   RefSeq; WP_001200573.1; NZ_MWVM01000003.1.
DR   ProteinModelPortal; Q7AHS5; -.
DR   SMR; Q7AHS5; -.
DR   STRING; 155864.Z0064; -.
DR   EnsemblBacteria; AAG54360; AAG54360; Z0064.
DR   EnsemblBacteria; BAB33483; BAB33483; BAB33483.
DR   GeneID; 913460; -.
DR   KEGG; ece:Z0064; -.
DR   KEGG; ecs:ECs0060; -.
DR   PATRIC; fig|386585.9.peg.159; -.
DR   eggNOG; ENOG41066UG; Bacteria.
DR   eggNOG; COG1076; LUCA.
DR   HOGENOM; HOG000272779; -.
DR   KO; K05801; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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:0051087; F:chaperone binding; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   Gene3D; 1.10.3680.10; -; 1.
DR   HAMAP; MF_01153; DjlA; 1.
DR   InterPro; IPR023749; DjlA.
DR   InterPro; IPR007791; DjlA_N.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR029024; TerB-like.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF05099; TerB; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7AHS5.
DR   SWISS-2DPAGE; Q7AHS5.
KW   Cell inner membrane; Cell membrane; Chaperone; Complete proteome;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    271       Co-chaperone protein DjlA.
FT                                /FTId=PRO_0000209425.
FT   TOPO_DOM      1      6       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01153}.
FT   TRANSMEM      7     31       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01153}.
FT   TOPO_DOM     32    271       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01153}.
FT   DOMAIN      205    271       J. {ECO:0000255|HAMAP-Rule:MF_01153}.
SQ   SEQUENCE   271 AA;  30565 MW;  F7A0F92DA681758F CRC64;
     MQYWGKIIGV AVALLMGGGF WGVVLGLLIG HMFDKARSRK MAWFANQRER QALFFATTFE
     VMGHLTKSKG RVTEADIHIA SQLMDRMNLH GASRTAAQNA FRVGKSDNYP LREKMRQFRS
     VCFGRFDLIR MFLEIQIQAA FADGSLHPNE RAVLYVIAEE LGISRAQFDQ FLRMMQGGAQ
     FGGGYQQQSG GGNWQQAQRG PTLEDACNVL GVKPTDDATT IKRAYRKLMS EHHPDKLVAK
     GLPPEMMEMA KQKAQEIQQA YELIKQQKGF K
//

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