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Database: UniProt
Entry: A0A1X9NGF9_9GAMM
LinkDB: A0A1X9NGF9_9GAMM
Original site: A0A1X9NGF9_9GAMM 
ID   A0A1X9NGF9_9GAMM        Unreviewed;       265 AA.
AC   A0A1X9NGF9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Co-chaperone protein DjlA {ECO:0000256|HAMAP-Rule:MF_01153};
GN   Name=djlA {ECO:0000256|HAMAP-Rule:MF_01153};
GN   ORFNames=BST96_07840 {ECO:0000313|EMBL:ARN74037.1};
OS   Oceanicoccus sagamiensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; Oceanicoccus.
OX   NCBI_TaxID=716816 {ECO:0000313|EMBL:ARN74037.1, ECO:0000313|Proteomes:UP000193450};
RN   [1] {ECO:0000313|EMBL:ARN74037.1, ECO:0000313|Proteomes:UP000193450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 107125 {ECO:0000313|EMBL:ARN74037.1,
RC   ECO:0000313|Proteomes:UP000193450};
RA   Kumagai Y.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP019343; ARN74037.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X9NGF9; -.
DR   STRING; 716816.BST96_07840; -.
DR   KEGG; osg:BST96_07840; -.
DR   OrthoDB; 9782583at2; -.
DR   Proteomes; UP000193450; 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; PTHR24074; CO-CHAPERONE PROTEIN DJLA; 1.
DR   PANTHER; PTHR24074:SF56; CO-CHAPERONE PROTEIN DJLA; 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   SUPFAM; SSF158682; TerB-like; 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};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01153};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01153};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193450};
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..5
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01153"
FT   TRANSMEM        6..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        30..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01153"
FT   DOMAIN          201..265
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
SQ   SEQUENCE   265 AA;  29384 MW;  E4EA098432326615 CRC64;
     MIFGKLIGGL IGFFSGGIFG AIIGLFAGHF FDKGIGQAMG FDYGADRAKL QRLFFETTFT
     IMGHLAKADG RISEQEIQQA EVLMERLGLT PEHRKEAINL FKQGSHSNFQ LEPIISTFIN
     EGGRRHNLPI LLLEFLFSIA MADGEMHQAE KEILAKTAGY LGIGSRQFEQ LLAMLTAQQN
     FHGGGYQQQG RQQTSANDLD NAYKALGVSS SASDKEIKKV YRKLMSQHHP DKLIAQGVPE
     DMMKVATEKA QEIQAAYDLI KEARK
//
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