ID   DJLA_LEGPH              Reviewed;         296 AA.
AC   Q9X772; Q5ZT24;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Co-chaperone protein DjlA {ECO:0000255|HAMAP-Rule:MF_01153};
GN   Name=djlA {ECO:0000255|HAMAP-Rule:MF_01153}; OrderedLocusNames=lpg2341;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10913104; DOI=10.1128/jb.182.16.4654-4657.2000;
RA   Brabetz W., Schirmer C.E., Brade H.;
RT   "3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferase of Legionella
RT   pneumophila transfers two kdo residues to a structurally different lipid A
RT   precursor of Escherichia coli.";
RL   J. Bacteriol. 182:4654-4657(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU28403.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ011775; CAB43070.1; -; Genomic_DNA.
DR   EMBL; AE017354; AAU28403.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_010948047.1; NC_002942.5.
DR   RefSeq; YP_096350.2; NC_002942.5.
DR   AlphaFoldDB; Q9X772; -.
DR   SMR; Q9X772; -.
DR   STRING; 272624.lpg2341; -.
DR   PaxDb; Q9X772; -.
DR   PRIDE; Q9X772; -.
DR   EnsemblBacteria; AAU28403; AAU28403; lpg2341.
DR   GeneID; 66491468; -.
DR   KEGG; lpn:lpg2341; -.
DR   PATRIC; fig|272624.6.peg.2459; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_066221_1_0_6; -.
DR   Proteomes; UP000000609; 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..296
FT                   /note="Co-chaperone protein DjlA"
FT                   /id="PRO_0000209430"
FT   TOPO_DOM        1..15
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   TRANSMEM        16..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   TOPO_DOM        40..296
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   DOMAIN          231..296
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   REGION          200..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   296 AA;  34130 MW;  CC0495809613415B CRC64;
     MNLRDFFVIT TWWGKILGAF FGYLTAGPVG ALFGILVGNF FDRGLVSYYS NPHWLYHAEK
     QRIVQKAFFE ATFSIMGHVA KSDGRVSEQE ISMAKSIMNE MKLSKGQKDL AKRLFNEGKQ
     ADFNVSLALI QLQRICKDNR DLLKLFVDIQ YRAAQVDGLS SQKIHALDNI FTHLGFAPLH
     KQYRFYEDFG SYFQQEQSKQ HYHNQQEYKH TSSSQGQQGY KPQSPPNTLA HAFALLEVSP
     NANKQEVRRA YRRLLSRNHP DKLIAQGLPE EMIKLANDKT HQIMKAYELI CETKGW