DJLA_PHOLL
ID DJLA_PHOLL Reviewed; 273 AA.
AC Q7N8V3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Co-chaperone protein DjlA {ECO:0000255|HAMAP-Rule:MF_01153};
GN Name=djlA {ECO:0000255|HAMAP-Rule:MF_01153}; OrderedLocusNames=plu0613;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(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; BX571860; CAE12908.1; -; Genomic_DNA.
DR RefSeq; WP_011144990.1; NC_005126.1.
DR AlphaFoldDB; Q7N8V3; -.
DR SMR; Q7N8V3; -.
DR STRING; 243265.plu0613; -.
DR EnsemblBacteria; CAE12908; CAE12908; plu0613.
DR GeneID; 24168040; -.
DR KEGG; plu:plu0613; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_066221_1_0_6; -.
DR OMA; MQYWGKL; -.
DR OrthoDB; 1528212at2; -.
DR BioCyc; PLUM243265:PLU_RS03020-MON; -.
DR Proteomes; UP000002514; 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..273
FT /note="Co-chaperone protein DjlA"
FT /id="PRO_0000209433"
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..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT DOMAIN 207..273
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
SQ SEQUENCE 273 AA; 30898 MW; B89CB030D0228791 CRC64;
MHYWGKLLGL IFGVVSGAGF WGIVIGLFIG HMLDRASVRG NQGFFANNQS RQLLFFSSTF
QVMGHITKSK GRVTETDIRL ASQLMERMQL HGQARIAAQQ AFREGKEPNF PLRETLRQLR
RACFGRSDLI RMFLEIQLQA AFSDGQLHPN ERTVLFIIAD ELGISRNQFE QFLAMMEGGR
NFGDGGEWQQ RQYGGYQKAA QGPTLADACK VLGVREKDDA TTIKRAYRRL MSEHHPDKLV
AKGLPPEMME IAKQKAQSIQ AAYDLIKKEK GFK