DJLA_MANSM
ID DJLA_MANSM Reviewed; 288 AA.
AC Q65RA1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Co-chaperone protein DjlA {ECO:0000255|HAMAP-Rule:MF_01153};
GN Name=djlA {ECO:0000255|HAMAP-Rule:MF_01153}; OrderedLocusNames=MS1902;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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=AAU38509.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016827; AAU38509.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011201062.1; NC_006300.1.
DR AlphaFoldDB; Q65RA1; -.
DR STRING; 221988.MS1902; -.
DR EnsemblBacteria; AAU38509; AAU38509; MS1902.
DR KEGG; msu:MS1902; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_066221_1_0_6; -.
DR OrthoDB; 1528212at2; -.
DR Proteomes; UP000000607; 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; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..288
FT /note="Co-chaperone protein DjlA"
FT /id="PRO_0000209431"
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..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
FT DOMAIN 222..288
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01153"
SQ SEQUENCE 288 AA; 32878 MW; C67A02CFE83CA996 CRC64;
MNFIGKILGF IIGYRFGGLF GGIAGLILGH IADKKLYELG SVNSSFFSKK ITRQSLFMQT
TFAVLGHLSK AKGRVTEEDI QLANNLMSQM QLDVANRQLA QNAFNRGKEA DFPVREVIRE
FRIGCGQRAD LLRMFLHIQV QAAFADSNLH NNEKELLFVI AEELGLSRFQ FDQMLAMEMA
ARQFTQGGFY RQQQYQQQSH QQYNQENYQN SYRTSSGPTV EDAYKVLGVN AGDNQQTVKR
AYRRLMNEHH PDKLVAKGLP KEMMEMAKEK AQQIQAAYDL ICKVKGWK
