DJLA_ECOLI
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 03-AUG-2022, entry version 164.
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; Proteobacteria; 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; P31680; -.
DR PRIDE; P31680; -.
DR EnsemblBacteria; AAC73166; AAC73166; b0055.
DR EnsemblBacteria; BAB96623; BAB96623; BAB96623.
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 PhylomeDB; P31680; -.
DR BioCyc; EcoCyc:EG11570-MON; -.
DR PRO; PR:P31680; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0051087; F:chaperone binding; IMP:EcoCyc.
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; IPR036869; J_dom_sf.
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 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
