ID   DJLA_PECAS              Reviewed;         291 AA.
AC   Q6D0E4;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Co-chaperone protein DjlA {ECO:0000255|HAMAP-Rule:MF_01153};
GN   Name=djlA {ECO:0000255|HAMAP-Rule:MF_01153}; OrderedLocusNames=ECA3855;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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   -!- 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}.
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DR   EMBL; BX950851; CAG76753.1; -; Genomic_DNA.
DR   RefSeq; WP_011095353.1; NC_004547.2.
DR   AlphaFoldDB; Q6D0E4; -.
DR   STRING; 218491.ECA3855; -.
DR   EnsemblBacteria; CAG76753; CAG76753; ECA3855.
DR   GeneID; 57210473; -.
DR   KEGG; eca:ECA3855; -.
DR   PATRIC; fig|218491.5.peg.3910; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_066221_1_0_6; -.
DR   OMA; MQYWGKL; -.
DR   OrthoDB; 1528212at2; -.
DR   Proteomes; UP000007966; 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; 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; SSF158682; SSF158682; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Chaperone; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..291
FT                   /note="Co-chaperone protein DjlA"
FT                   /id="PRO_0000209427"
FT   TOPO_DOM        1..6
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   TRANSMEM        7..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   TOPO_DOM        32..291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   DOMAIN          225..291
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   REGION          177..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   291 AA;  33156 MW;  43B162A977D493AC CRC64;
     MRYWGKLLGL ALGIVSSTGI WGMIMGLLMG HWIDRARASR RRDYFSAQST RQSLFFLTTF
     QAMGHLTKSK GRVTEADINI ATKMMDRLEL FGDARAAAQR AFREGKAGQF PLRIKLRKLR
     DACLGRFDLI KMFLEIQLQV AFVDGVLHPN ERRVLYVIAD ELGVTREQFE FFLRNMESPT
     GQQSRQNQSR QNGKSQQRRN NGYSNGHSYG GQRPPSPLRG PTVESACRTL GVRSSDDAVT
     IKRAYRKLMS EHHPDKLVAK KLSPRMMEMA KRKAQDIQAA YELLKSANQT K