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Entry: P31680
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Original site: P31680 
ID   DJLA_ECOLI              Reviewed;         271 AA.
AC   P31680; Q6IU30;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Co-chaperone protein DjlA {ECO:0000255|HAMAP-Rule:MF_01153, ECO:0000305};
DE   AltName: Full=DnaJ-like protein DjlA {ECO:0000305};
GN   Name=djlA {ECO:0000255|HAMAP-Rule:MF_01153, ECO:0000303|PubMed:8809778};
GN   Synonyms=yabH; OrderedLocusNames=b0055, JW0054;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA   Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA   Mizobuchi K., Nakata A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT   2.4 min region.";
RL   Nucleic Acids Res. 20:3305-3308(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 55-219.
RC   STRAIN=B;
RX   PubMed=12664169; DOI=10.1007/s00239-002-2423-0;
RA   Lenski R.E., Winkworth C.L., Riley M.A.;
RT   "Rates of DNA sequence evolution in experimental populations of Escherichia
RT   coli during 20,000 generations.";
RL   J. Mol. Evol. 56:498-508(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45, SUBCELLULAR LOCATION, AND
RP   TOPOLOGY.
RX   PubMed=8809778; DOI=10.1111/j.1365-2958.1996.tb02646.x;
RA   Clarke D.J., Jacq A., Holland I.B.;
RT   "A novel DnaJ-like protein in Escherichia coli inserts into the cytoplasmic
RT   membrane with a type III topology.";
RL   Mol. Microbiol. 20:1273-1286(1996).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF HIS-233.
RX   PubMed=9364917; DOI=10.1111/j.1365-2958.1997.mmi527.x;
RA   Kelley W.L., Georgopoulos C.;
RT   "Positive control of the two-component RcsC/B signal transduction network
RT   by DjIA: a member of the DnaJ family of molecular chaperones in Escherichia
RT   coli.";
RL   Mol. Microbiol. 25:913-931(1997).
RN   [7]
RP   FUNCTION IN THE REGULATION OF THE RCS SYSTEM.
RX   PubMed=11758943; DOI=10.1271/bbb.65.2364;
RA   Chen M.H., Takeda S., Yamada H., Ishii Y., Yamashino T., Mizuno T.;
RT   "Characterization of the RcsC->YojN->RcsB phosphorelay signaling pathway
RT   involved in capsular synthesis in Escherichia coli.";
RL   Biosci. Biotechnol. Biochem. 65:2364-2367(2001).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11106641; DOI=10.1074/jbc.m003855200;
RA   Genevaux P., Wawrzynow A., Zylicz M., Georgopoulos C., Kelley W.L.;
RT   "DjlA is a third DnaK co-chaperone of Escherichia coli, and DjlA-mediated
RT   induction of colanic acid capsule requires DjlA-DnaK interaction.";
RL   J. Biol. Chem. 276:7906-7912(2001).
RN   [9]
RP   TRANSMEMBRANE DOMAIN, AND SUBUNIT.
RX   PubMed=12655402; DOI=10.1007/s00438-002-0793-z;
RA   Toutain C.M., Clarke D.J., Leeds J.A., Kuhn J., Beckwith J., Holland I.B.,
RA   Jacq A.;
RT   "The transmembrane domain of the DnaJ-like protein DjlA is a dimerisation
RT   domain.";
RL   Mol. Genet. Genomics 268:761-770(2003).
RN   [10]
RP   MUTAGENESIS.
RX   PubMed=9364918; DOI=10.1111/j.1365-2958.1997.mmi528.x;
RA   Clarke D.J., Holland I.B., Jacq A.;
RT   "Point mutations in the transmembrane domain of DjlA, a membrane-linked
RT   DnaJ-like protein, abolish its function in promoting colanic acid
RT   production via the Rcs signal transduction pathway.";
RL   Mol. Microbiol. 25:933-944(1997).
CC   -!- FUNCTION: Regulatory DnaK co-chaperone. Direct interaction between DnaK
CC       and DjlA is needed for the induction of the wcaABCDE operon, involved
CC       in the synthesis of a colanic acid polysaccharide capsule, possibly
CC       through activation of the RcsB/RcsC phosphotransfer signaling pathway.
CC       The colanic acid capsule may help the bacterium survive conditions
CC       outside the host. {ECO:0000255|HAMAP-Rule:MF_01153,
CC       ECO:0000269|PubMed:11106641, ECO:0000269|PubMed:11758943,
CC       ECO:0000269|PubMed:9364917}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01153,
CC       ECO:0000269|PubMed:12655402}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01153, ECO:0000269|PubMed:11106641, ECO:0000269|PubMed:8809778,
CC       ECO:0000269|PubMed:9364917}; Single-pass type III membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01153, ECO:0000269|PubMed:11106641,
CC       ECO:0000269|PubMed:8809778, ECO:0000269|PubMed:9364917}.
CC   -!- DOMAIN: The transmembrane domain is a dimerization domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01153, ECO:0000269|PubMed:12655402}.
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DR   EMBL; U00096; AAC73166.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAB96623.1; -; Genomic_DNA.
DR   EMBL; AY625119; AAT42473.1; -; Genomic_DNA.
DR   PIR; G64726; G64726.
DR   RefSeq; NP_414597.1; NC_000913.3.
DR   RefSeq; WP_001200579.1; NZ_STEB01000010.1.
DR   AlphaFoldDB; P31680; -.
DR   SMR; P31680; -.
DR   BioGRID; 4261616; 19.
DR   IntAct; P31680; 7.
DR   STRING; 511145.b0055; -.
DR   jPOST; P31680; -.
DR   PaxDb; 511145-b0055; -.
DR   EnsemblBacteria; AAC73166; AAC73166; b0055.
DR   GeneID; 66671655; -.
DR   GeneID; 948992; -.
DR   KEGG; ecj:JW0054; -.
DR   KEGG; eco:b0055; -.
DR   PATRIC; fig|1411691.4.peg.2228; -.
DR   EchoBASE; EB1530; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_066221_1_0_6; -.
DR   InParanoid; P31680; -.
DR   OMA; MQYWGKL; -.
DR   OrthoDB; 9782583at2; -.
DR   PhylomeDB; P31680; -.
DR   BioCyc; EcoCyc:EG11570-MONOMER; -.
DR   PRO; PR:P31680; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IMP:EcoCyc.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd07316; terB_like_DjlA; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 1.10.3680.10; TerB-like; 1.
DR   HAMAP; MF_01153; DjlA; 1.
DR   InterPro; IPR023749; DjlA.
DR   InterPro; IPR007791; DjlA_N.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR029024; TerB-like.
DR   PANTHER; PTHR24074; CO-CHAPERONE PROTEIN DJLA; 1.
DR   PANTHER; PTHR24074:SF58; LD30543P; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF05099; TerB; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Chaperone; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..271
FT                   /note="Co-chaperone protein DjlA"
FT                   /id="PRO_0000209424"
FT   TOPO_DOM        1..6
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153,
FT                   ECO:0000305|PubMed:8809778, ECO:0000305|PubMed:9364917"
FT   TRANSMEM        7..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   TOPO_DOM        32..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153,
FT                   ECO:0000305|PubMed:8809778, ECO:0000305|PubMed:9364917"
FT   DOMAIN          205..271
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   MUTAGEN         15
FT                   /note="L->R: Loss of activation of rcs."
FT                   /evidence="ECO:0000269|PubMed:9364918"
FT   MUTAGEN         16
FT                   /note="M->R: Only partial activation of rcs."
FT                   /evidence="ECO:0000269|PubMed:9364918"
FT   MUTAGEN         233
FT                   /note="H->Q: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:9364917"
FT   CONFLICT        195
FT                   /note="Q -> L (in Ref. 4; AAT42473)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   271 AA;  30579 MW;  80A0FC28F6D470DF CRC64;
     MQYWGKIIGV AVALLMGGGF WGVVLGLLIG HMFDKARSRK MAWFANQRER QALFFATTFE
     VMGHLTKSKG RVTEADIHIA SQLMDRMNLH GASRTAAQNA FRVGKSDNYP LREKMRQFRS
     VCFGRFDLIR MFLEIQIQAA FADGSLHPNE RAVLYVIAEE LGISRAQFDQ FLRMMQGGAQ
     FGGGYQQQTG GGNWQQAQRG PTLEDACNVL GVKPTDDATT IKRAYRKLMS EHHPDKLVAK
     GLPPEMMEMA KQKAQEIQQA YELIKQQKGF K
//
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