DJLA_VIBVU
ID DJLA_VIBVU Reviewed; 287 AA.
AC Q8DED6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, 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=VV1_0659;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016795; AAO09171.1; -; Genomic_DNA.
DR RefSeq; WP_011078738.1; NC_004459.3.
DR AlphaFoldDB; Q8DED6; -.
DR SMR; Q8DED6; -.
DR EnsemblBacteria; AAO09171; AAO09171; VV1_0659.
DR GeneID; 66963813; -.
DR KEGG; vvu:VV1_0659; -.
DR HOGENOM; CLU_066221_1_0_6; -.
DR OMA; MQYWGKL; -.
DR Proteomes; UP000002275; 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; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..287
FT /note="Co-chaperone protein DjlA"
FT /id="PRO_0000209443"
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..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT DOMAIN 221..287
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT REGION 192..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 287 AA; 32229 MW; C5ED755E93421E15 CRC64;
MQIFGKILGA FFGFLFGGVF GALFGLFIGH QFDKARRLSQ AGFKTAGFGQ GPSQAQRQEE
FFKSAFAVMG HVAKAKGQVT KEEIQLASAM MDRMSLHGEQ RRAAQDAFRE GKERDFPLEQ
VLERVKIATS GRFDLLQFFL ELQISAAFAD GDVHPSERNV LHKIARGLGF SSEQLERRLQ
MQEAAFRFQR QGGFGGQQHQ SHHSSSHGGW QQASQTDRLA DAYKILGIDA NADGKEVKRA
YRKLMNEHHP DKLMAKGLPP EMMNMAKEKS QEIQSAYDLI KKEKGFK