ID L0MAC7_ENTBF Unreviewed; 272 AA.
AC L0MAC7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Co-chaperone protein DjlA {ECO:0000256|HAMAP-Rule:MF_01153};
GN Name=djlA {ECO:0000256|HAMAP-Rule:MF_01153};
GN OrderedLocusNames=D782_3813 {ECO:0000313|EMBL:AGB79720.1};
OS Enterobacteriaceae bacterium (strain FGI 57).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB79720.1, ECO:0000313|Proteomes:UP000011002};
RN [1] {ECO:0000313|EMBL:AGB79720.1, ECO:0000313|Proteomes:UP000011002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI 57 {ECO:0000313|EMBL:AGB79720.1,
RC ECO:0000313|Proteomes:UP000011002};
RX PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA Currie C.R.;
RT "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT associated with leaf-cutter ant fungus gardens.";
RL Genome Announc. 1:E00238-12(2013).
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; CP003938; AGB79720.1; -; Genomic_DNA.
DR AlphaFoldDB; L0MAC7; -.
DR STRING; 693444.D782_3813; -.
DR KEGG; ebf:D782_3813; -.
DR PATRIC; fig|693444.3.peg.3633; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_066221_1_0_6; -.
DR OrthoDB; 9782583at2; -.
DR Proteomes; UP000011002; 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; 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 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:UP000011002};
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 TRANSMEM 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 32..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01153"
FT DOMAIN 206..272
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 272 AA; 30724 MW; DF5931E8F82ABBC7 CRC64;
MQYWGKVIGV AIALMMGGGF WGVVLGLLVG HMFDKARSRR MNWFANQQER QSLFFATTFE
VMGHLTKSKG RVTEADIHIA SMLMDRMNLH GASRTAAQQA FRVGKSDNYP LREKMRQFRS
VCFGRFDLIR MFLEIQIQAA FADGSLHPNE RDVLYVIAEE LGISRAQFDQ FLRMMQGGAQ
FGGGYQQQSQ GAGGWQQAQR GPTLEDACNV LGVKSTDDAT TIKRAYRKLM SEHHPDKLVA
KGLPPEMMEM AKQKAQEIQS AYELIKEQKG FK
//
