ID Q1YSY5_9GAMM Unreviewed; 264 AA.
AC Q1YSY5;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Co-chaperone protein DjlA {ECO:0000256|HAMAP-Rule:MF_01153};
GN Name=djlA {ECO:0000256|HAMAP-Rule:MF_01153};
GN ORFNames=GB2207_10658 {ECO:0000313|EMBL:EAS47071.1};
OS gamma proteobacterium HTCC2207.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Porticoccaceae; SAR92 clade.
OX NCBI_TaxID=314287 {ECO:0000313|EMBL:EAS47071.1, ECO:0000313|Proteomes:UP000005555};
RN [1] {ECO:0000313|EMBL:EAS47071.1, ECO:0000313|Proteomes:UP000005555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2207 {ECO:0000313|EMBL:EAS47071.1,
RC ECO:0000313|Proteomes:UP000005555};
RA Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (MAR-2006) 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}.
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:EAS47071.1}.
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DR EMBL; AAPI01000003; EAS47071.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1YSY5; -.
DR STRING; 314287.GB2207_10658; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_066221_1_0_6; -.
DR Proteomes; UP000005555; 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 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}; Chaperone {ECO:0000256|HAMAP-Rule:MF_01153};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01153};
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..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 30..264
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 264 AA; 28371 MW; 7CDB76F1F7D44B07 CRC64;
MIAGKIIAGL LGLSVAGPIG VLIGVYIGHQ FDKGLGGLRP MSAEQQAEVR ESFFETVFGL
LGHLAKADGR VSEVEVAHAE ALMAKMGLNT PHRKKAIELF KGGSQGGFSI DATMDRFMAV
CGKQNNLKRA LLDYLVSLAI ADGELHQAEQ DVLRKIAGRL GFSSALFDKF MEMVKAQSQF
KQSGGSGGYR ESTSPGKLQA AYTALGVEAA QTDAQIKRAY RKLISANHPD KLIGQGMPDD
MVKLATERTQ EIQTAYELVV ASRK
//
