DJLA_YERPS
ID DJLA_YERPS Reviewed; 277 AA.
AC Q66EQ5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Co-chaperone protein DjlA {ECO:0000255|HAMAP-Rule:MF_01153};
GN Name=djlA {ECO:0000255|HAMAP-Rule:MF_01153}; OrderedLocusNames=YPTB0637;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19877.1; -; Genomic_DNA.
DR RefSeq; WP_011191713.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66EQ5; -.
DR SMR; Q66EQ5; -.
DR EnsemblBacteria; CAH19877; CAH19877; YPTB0637.
DR GeneID; 66842942; -.
DR KEGG; ypo:BZ17_1920; -.
DR KEGG; yps:YPTB0637; -.
DR PATRIC; fig|273123.14.peg.2040; -.
DR OMA; MQYWGKL; -.
DR Proteomes; UP000001011; Chromosome.
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; 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..277
FT /note="Co-chaperone protein DjlA"
FT /id="PRO_0000209446"
FT TOPO_DOM 1..6
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT TRANSMEM 7..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT TOPO_DOM 32..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT DOMAIN 211..277
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
SQ SEQUENCE 277 AA; 31105 MW; B0CE87EF7708C8B9 CRC64;
MRYWGKLLGL VLGVMYAPGV VGALLGLLVG HMVDRALGAK RRGFFADQQT RQSLFFRTTF
QVMGHLTKAK GRVTEVDIQL ASQLMDRMQL HGAARTAAQQ AFREGKESHF PLRKTLQEFR
RVCFGRFDLI RIFLEIQLQA AFADGSLHPN ERQVLYVIAE ELGISRGQFD QFLRMFDGGR
QFGGHGGWQG QQGGYSQSGY QRAPQGPTLE DACKVLGVNS SDDSVAIKRA YRKLMGEHHP
DKLVAKGLPP EMMEMAKQKA QEIQAAYDLI KREKGFK