ID A0A432ZS46_9GAMM Unreviewed; 273 AA.
AC A0A432ZS46;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=Co-chaperone protein DjlA {ECO:0000256|HAMAP-Rule:MF_01153};
GN Name=djlA {ECO:0000256|HAMAP-Rule:MF_01153};
GN ORFNames=CWI84_03665 {ECO:0000313|EMBL:RUO80693.1};
OS Idiomarina tyrosinivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=1445662 {ECO:0000313|EMBL:RUO80693.1, ECO:0000313|Proteomes:UP000287996};
RN [1] {ECO:0000313|EMBL:RUO80693.1, ECO:0000313|Proteomes:UP000287996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-PW-9 {ECO:0000313|EMBL:RUO80693.1,
RC ECO:0000313|Proteomes:UP000287996};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUO80693.1}.
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DR EMBL; PIQH01000003; RUO80693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432ZS46; -.
DR OrthoDB; 9782583at2; -.
DR Proteomes; UP000287996; Unassembled WGS sequence.
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:SF58; LD30543P; 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:UP000287996};
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 TOPO_DOM 30..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01153"
FT DOMAIN 207..273
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 273 AA; 30972 MW; 879EE31715908256 CRC64;
MFWGKVLGAV AGFLFARIPG AIIGVLIGHW FDRGVAQDFS QRGAFGRYLF GTDRAVGDAS
FIYTLFAVLG HLAKAKGRVT EQDIAHASAL MDRFYLQNDA RREAQSAFRE GKQPTFPLEQ
TLCDFKAAFY GNIEVLELFI EQLIRMALVD GKLDKTEYQV LLAAAKALGF NKFQLDQALM
MQKAGFRFRR SQQQRYQQKS QHNDLDDAYQ ILGAHASDSD AEIKKTYRKL MSRHHPDKLA
GQGVPEKVMK EAQQRTQEIQ AAYETIKKHR GMR
//
