ID   DJLA_COXBU              Reviewed;         270 AA.
AC   Q45885;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Co-chaperone protein DjlA {ECO:0000255|HAMAP-Rule:MF_01153};
DE   AltName: Full=Mucoidy activation protein MucZ;
GN   Name=djlA {ECO:0000255|HAMAP-Rule:MF_01153}; Synonyms=mucZ;
GN   OrderedLocusNames=CBU_1873;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Nine Mile;
RX   PubMed=7635811; DOI=10.1128/jb.177.15.4238-4244.1995;
RA   Zuber M., Hoover T.A., Court D.L.;
RT   "Analysis of a Coxiella burnetti gene product that activates capsule
RT   synthesis in Escherichia coli: requirement for the heat shock chaperone
RT   DnaK and the two-component regulator RcsC.";
RL   J. Bacteriol. 177:4238-4244(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO91364.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L42518; AAA79969.1; -; Genomic_DNA.
DR   EMBL; AE016828; AAO91364.1; ALT_INIT; Genomic_DNA.
DR   PIR; I40852; I40852.
DR   RefSeq; NP_820850.1; NC_002971.3.
DR   AlphaFoldDB; Q45885; -.
DR   SMR; Q45885; -.
DR   STRING; 227377.CBU_1873; -.
DR   EnsemblBacteria; AAO91364; AAO91364; CBU_1873.
DR   GeneID; 1209786; -.
DR   KEGG; cbu:CBU_1873; -.
DR   PATRIC; fig|227377.7.peg.1855; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_066221_1_0_6; -.
DR   OMA; MQYWGKL; -.
DR   Proteomes; UP000002671; 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..270
FT                   /note="Co-chaperone protein DjlA"
FT                   /id="PRO_0000209423"
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..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;  31291 MW;  E75DA56B15BF4810 CRC64;
     MNWIGKLIGM MLGFILAGPI GLIIGLFIGH VVFDQGRFRQ WFQTTASARS QPSKIQEVFF
     NTTFRVMGFV AKADGRVSEN EIRQARQVMQ QMNLDDSMKR EAIRLFTEGK QPNFNLDESL
     NELRQACVFQ PALLRVFLEI QIQMASADGQ GLSGQKRQVL QTICRRLEVF GFDYNQFEQR
     FRAEQNYQRY QQRATQDPRA YLNDAYKVLG LTSAATDSEI KKSYRRLMSQ HHPDKLMAKG
     LPPEMMKMAT QKTQQIKKAY EQIRKVRSMV