ID   DJLA_VIBPA              Reviewed;         284 AA.
AC   Q87ST2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Co-chaperone protein DjlA {ECO:0000255|HAMAP-Rule:MF_01153};
GN   Name=djlA {ECO:0000255|HAMAP-Rule:MF_01153}; OrderedLocusNames=VP0340;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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; BA000031; BAC58603.1; -; Genomic_DNA.
DR   RefSeq; NP_796719.1; NC_004603.1.
DR   RefSeq; WP_005459635.1; NC_004603.1.
DR   AlphaFoldDB; Q87ST2; -.
DR   STRING; 223926.28805323; -.
DR   EnsemblBacteria; BAC58603; BAC58603; BAC58603.
DR   GeneID; 1187807; -.
DR   KEGG; vpa:VP0340; -.
DR   PATRIC; fig|223926.6.peg.327; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_066221_1_0_6; -.
DR   OMA; MQYWGKL; -.
DR   Proteomes; UP000002493; Chromosome 1.
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..284
FT                   /note="Co-chaperone protein DjlA"
FT                   /id="PRO_0000209442"
FT   TOPO_DOM        1..6
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   TRANSMEM        7..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   TOPO_DOM        31..284
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT   DOMAIN          218..284
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
SQ   SEQUENCE   284 AA;  31731 MW;  5122572C496D6F24 CRC64;
     MHIFGKILGA FFGLLLGGPF GLLFGLFIGH QFDKARRLSQ AGFSTGGFGK GPSQAQRQEE
     FFKAAFAVMG HVAKAKGQVT KEEIQLATAM MDRMNLHGEQ RRAAQDAFRE GKESDFPLED
     VLVRVKISTA GRFDLLQFFL ELQISAAFAD GAIHPSERNV LHKIARGLGF SSEQLERRLQ
     MQEAAFRFQH QGGFHGQQQG QYQSSGWQQA SQADQLADAY KILDVSPEAD GKTVKRAYRK
     LMNEHHPDKL MAKGLPPEMM NVAKEKSQEI QNAYDLIKKV KGFK