ID A0A0W0TL61_9GAMM Unreviewed; 286 AA.
AC A0A0W0TL61;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Co-chaperone protein DjlA {ECO:0000256|HAMAP-Rule:MF_01153};
GN Name=djlA {ECO:0000256|HAMAP-Rule:MF_01153,
GN ECO:0000313|EMBL:SPX62571.1};
GN ORFNames=Lfee_2111 {ECO:0000313|EMBL:KTC96313.1}, NCTC12022_03333
GN {ECO:0000313|EMBL:SPX62571.1};
OS Legionella feeleii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=453 {ECO:0000313|EMBL:KTC96313.1, ECO:0000313|Proteomes:UP000054698};
RN [1] {ECO:0000313|EMBL:KTC96313.1, ECO:0000313|Proteomes:UP000054698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-44C {ECO:0000313|EMBL:KTC96313.1,
RC ECO:0000313|Proteomes:UP000054698};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SPX62571.1, ECO:0000313|Proteomes:UP000251942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12022 {ECO:0000313|EMBL:SPX62571.1,
RC ECO:0000313|Proteomes:UP000251942};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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: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; LNYB01000081; KTC96313.1; -; Genomic_DNA.
DR EMBL; UASS01000039; SPX62571.1; -; Genomic_DNA.
DR RefSeq; WP_058446593.1; NZ_UASS01000039.1.
DR AlphaFoldDB; A0A0W0TL61; -.
DR STRING; 453.Lfee_2111; -.
DR PATRIC; fig|453.4.peg.2311; -.
DR OrthoDB; 9782583at2; -.
DR Proteomes; UP000054698; Unassembled WGS sequence.
DR Proteomes; UP000251942; Unassembled WGS sequence.
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; PTHR24074; CO-CHAPERONE PROTEIN DJLA; 1.
DR PANTHER; PTHR24074:SF58; LD30543P; 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}; Chaperone {ECO:0000256|HAMAP-Rule:MF_01153};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01153};
KW Reference proteome {ECO:0000313|Proteomes:UP000054698};
KW Stress response {ECO:0000313|EMBL:KTC96313.1};
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..15
FT /note="Periplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01153"
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 40..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01153"
FT DOMAIN 221..285
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 286 AA; 33389 MW; 6FCAF92E1ACB9799 CRC64;
MNFRQFFTNH QWWGKILGAF FGYLIGGSAG ALFGILIGNF FDRGIVSHYT RPHWYYHSEK
RQAVQKIFFQ ATFSVMGHLA KADGRVSEQE IELAKTLMDE MRLNHEQKTL AKRFFNEGKA
VNFDLSRILT LLQKACRDNP ELLKLFMDIQ YRFAQTDGLS NMKLQALDVI FRQMGFAPLN
QQYRFYEDFG YQSSRQSSNQ HSSSRQYNDH YQAPPQNTLM QAYAILEINH TASKQEVKSA
YRRLISRNHP DKLIAKGLPE EMIKIANDKT QKIRKAYEQI CTSKGW
//
