ID Q2SPE3_HAHCH Unreviewed; 268 AA.
AC Q2SPE3;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Co-chaperone protein DjlA {ECO:0000256|HAMAP-Rule:MF_01153};
GN Name=djlA {ECO:0000256|HAMAP-Rule:MF_01153};
GN OrderedLocusNames=HCH_00578 {ECO:0000313|EMBL:ABC27481.1};
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC27481.1, ECO:0000313|Proteomes:UP000000238};
RN [1] {ECO:0000313|EMBL:ABC27481.1, ECO:0000313|Proteomes:UP000000238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC27481.1,
RC ECO:0000313|Proteomes:UP000000238};
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
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:0000256|HAMAP-Rule:MF_01153}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01153}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01153}; Single-pass type III membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_01153}.
CC -!- DOMAIN: The transmembrane domain is a dimerization domain.
CC {ECO:0000256|HAMAP-Rule:MF_01153}.
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DR EMBL; CP000155; ABC27481.1; -; Genomic_DNA.
DR RefSeq; WP_011394558.1; NC_007645.1.
DR AlphaFoldDB; Q2SPE3; -.
DR STRING; 349521.HCH_00578; -.
DR KEGG; hch:HCH_00578; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_066221_1_0_6; -.
DR OrthoDB; 9782583at2; -.
DR Proteomes; UP000000238; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd07316; terB_like_DjlA; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.10.3680.10; TerB-like; 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 PANTHER; PTHR43096:SF48; CHAPERONE PROTEIN DNAJ; 1.
DR PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF05099; TerB; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF158682; TerB-like; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_01153};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01153};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01153};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01153};
KW Reference proteome {ECO:0000313|Proteomes:UP000000238};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01153};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01153}.
FT TOPO_DOM 1..6
FT /note="Periplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01153"
FT TOPO_DOM 31..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01153"
FT DOMAIN 203..268
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 268 AA; 29748 MW; 2E2992A8B0ADB9E8 CRC64;
MGWWGKVIGG AFGYALGGPL GGLLGAAIGH SFDVGVQRIE LAPPNWGAGD QERVQTAFFT
AVFSVMGHVA KADGRVSEVE IQAARHIMAG MQLNPEQEKL AIELFNRGKQ PEFDLQAVLL
QFRDECHRRA NLLQMFLEIL LATALADQDL HANEQRILRE VAETLGFSRH QFEGLLAMAI
ARQRYAQEGF HAGAKEKTPS LSDAYAALGV NENSTDDEIK KAYRRLMSQH HPDKLVSKGL
PEEMVKIATE KTQEIRTAYE QIKRARGR
//
