GenomeNet

Database: UniProt
Entry: C5BI20_TERTT
LinkDB: C5BI20_TERTT
Original site: C5BI20_TERTT 
ID   C5BI20_TERTT            Unreviewed;       265 AA.
AC   C5BI20;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Co-chaperone protein DjlA {ECO:0000256|HAMAP-Rule:MF_01153};
GN   Name=djlA {ECO:0000256|HAMAP-Rule:MF_01153,
GN   ECO:0000313|EMBL:ACR12307.1};
GN   OrderedLocusNames=TERTU_1913 {ECO:0000313|EMBL:ACR12307.1};
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR12307.1, ECO:0000313|Proteomes:UP000009080};
RN   [1] {ECO:0000313|EMBL:ACR12307.1, ECO:0000313|Proteomes:UP000009080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001614; ACR12307.1; -; Genomic_DNA.
DR   RefSeq; WP_015818419.1; NC_012997.1.
DR   AlphaFoldDB; C5BI20; -.
DR   STRING; 377629.TERTU_1913; -.
DR   KEGG; ttu:TERTU_1913; -.
DR   eggNOG; COG1076; Bacteria.
DR   HOGENOM; CLU_066221_1_0_6; -.
DR   OrthoDB; 9782583at2; -.
DR   Proteomes; UP000009080; 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; PTHR44743:SF10; J DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR44743; PUTATIVE, EXPRESSED-RELATED; 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:UP000009080};
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..4
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        29..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01153"
FT   DOMAIN          200..264
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
SQ   SEQUENCE   265 AA;  29497 MW;  182F19A02EBD2366 CRC64;
     MLGKIIAGLI GFLTLGPFGA ILGVLIGHFF DHGRQQFARR FDPEQRAKVE TAFFNAVFPL
     LGHLAKADGR VSEEEVSGTE QLMAKMGLGV EARKKAIALF QQGAQSDFNP HALLDDFNLV
     CGKYPDLKQM ILVYLISLAY ADNHLHEQEE KVLADIASTL GYSSFAFNHL LGMVKAQAHF
     YRNQQGRQSP PQPREDELIL AYRALGVDAS ISDAQLKSAY RKLMSEYHPD KLAGRGVPED
     MLKVATERAQ EIQAAYDLIK KHRRG
//
DBGET integrated database retrieval system