ID   DJLA_SHIFL              Reviewed;         271 AA.
AC   Q7UDT6; Q83SP9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Co-chaperone protein DjlA {ECO:0000255|HAMAP-Rule:MF_01153};
GN   Name=djlA {ECO:0000255|HAMAP-Rule:MF_01153};
GN   OrderedLocusNames=SF0052, S0054;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN41718.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP15598.1; -; Genomic_DNA.
DR   RefSeq; NP_706011.2; NC_004337.2.
DR   RefSeq; WP_001200573.1; NZ_WPGW01000005.1.
DR   AlphaFoldDB; Q7UDT6; -.
DR   SMR; Q7UDT6; -.
DR   STRING; 198214.SF0052; -.
DR   PRIDE; Q7UDT6; -.
DR   EnsemblBacteria; AAN41718; AAN41718; SF0052.
DR   EnsemblBacteria; AAP15598; AAP15598; S0054.
DR   GeneID; 1024576; -.
DR   GeneID; 58460805; -.
DR   KEGG; sfl:SF0052; -.
DR   KEGG; sfx:S0054; -.
DR   PATRIC; fig|198214.7.peg.61; -.
DR   HOGENOM; CLU_066221_1_0_6; -.
DR   OMA; MQYWGKL; -.
DR   OrthoDB; 1528212at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; 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..271
FT                   /note="Co-chaperone protein DjlA"
FT                   /id="PRO_0000209439"
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..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   DOMAIN          205..271
FT                   /note="J"
FT                   /evidence="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