DJLA_SALPA
ID DJLA_SALPA Reviewed; 270 AA.
AC Q5PDE4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Co-chaperone protein DjlA {ECO:0000255|HAMAP-Rule:MF_01153};
GN Name=djlA {ECO:0000255|HAMAP-Rule:MF_01153}; OrderedLocusNames=SPA0095;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(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; CP000026; AAV76128.1; -; Genomic_DNA.
DR RefSeq; WP_001200595.1; NC_006511.1.
DR AlphaFoldDB; Q5PDE4; -.
DR SMR; Q5PDE4; -.
DR EnsemblBacteria; AAV76128; AAV76128; SPA0095.
DR KEGG; spt:SPA0095; -.
DR HOGENOM; CLU_066221_1_0_6; -.
DR OMA; MQYWGKL; -.
DR Proteomes; UP000008185; 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..270
FT /note="Co-chaperone protein DjlA"
FT /id="PRO_0000209435"
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..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT DOMAIN 204..270
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
SQ SEQUENCE 270 AA; 30583 MW; F8D51E70BFF9F2AF CRC64;
MQYWGKIIGV AVALMMGGGF WGVVLGLLVG HMFDKARSRK MAWFANQRER QALFFATTFE
VMGHLTKSKG RVTEADIHIA SQLMDRMNLH GDSRTAAQNA FRVGKADNYP LREKMRQFRS
VCFGRFDLIR MFLEIQIQAA FADGSLHPNE REVLYVIAEE LGISRVQFDQ FLRMMQGGAQ
FGGGYHQQSG GGWQQAQRGP TLEDACNVLG VKTTDDATTI KRAYRKLMSE HHPDKLVAKG
LPPEMMEMAK QKAQEIQKAY ELIKEQKGFK