ID   DJLA_PASMU              Reviewed;         287 AA.
AC   Q9CJW3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Co-chaperone protein DjlA {ECO:0000255|HAMAP-Rule:MF_01153};
GN   Name=djlA {ECO:0000255|HAMAP-Rule:MF_01153}; OrderedLocusNames=PM1878;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03962.1; -; Genomic_DNA.
DR   RefSeq; WP_005755501.1; NC_002663.1.
DR   AlphaFoldDB; Q9CJW3; -.
DR   STRING; 747.DR93_57; -.
DR   PRIDE; Q9CJW3; -.
DR   EnsemblBacteria; AAK03962; AAK03962; PM1878.
DR   KEGG; pmu:PM1878; -.
DR   HOGENOM; CLU_066221_1_0_6; -.
DR   OMA; MQYWGKL; -.
DR   Proteomes; UP000000809; 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;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..287
FT                   /note="Co-chaperone protein DjlA"
FT                   /id="PRO_0000209432"
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"
SQ   SEQUENCE   287 AA;  32760 MW;  CCB8A110F66B0A5A CRC64;
     MNFIGKFLGL IIGWKLGGFF GAICGVILGH LGDKKLYELG TVNSSFFKSK ITRQSLFMQT
     TFAVLGHLSK AKGRVTEDDI QLASHLMQQM QLDDANRRLA QEAFTRGKAA DFPLRQVIRE
     FRLGCGQRAD LLRMFLHVQV QAAFADAQLD QSEKDVLYIV GEELGLSRFQ FEQMLAMEFA
     ARQFSRAGYQ QQNRYQRDYG YQQHQQQYGG YQQQSGPTVD DAYKVLGVSA TDDQQTVKRA
     YRRLMNENHP DKLVAKGLPK EMLEMAKEKT QQIQSAYDLI CKTKGWK