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Database: UniProt
Entry: F7XCY7_SINMM
LinkDB: F7XCY7_SINMM
Original site: F7XCY7_SINMM 
ID   F7XCY7_SINMM            Unreviewed;       305 AA.
AC   F7XCY7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=DnaJ/CbpA-type protein {ECO:0000313|EMBL:AEH82762.1};
GN   OrderedLocusNames=SM11_pC1689 {ECO:0000313|EMBL:AEH82762.1};
OS   Sinorhizobium meliloti (strain SM11).
OG   Plasmid pSmeSM11c {ECO:0000313|EMBL:AEH82762.1,
OG   ECO:0000313|Proteomes:UP000009045}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH82762.1, ECO:0000313|Proteomes:UP000009045};
RN   [1] {ECO:0000313|EMBL:AEH82762.1, ECO:0000313|Proteomes:UP000009045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM11 {ECO:0000313|EMBL:AEH82762.1,
RC   ECO:0000313|Proteomes:UP000009045};
RC   PLASMID=pSmeSM11c {ECO:0000313|Proteomes:UP000009045};
RX   PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA   Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA   Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT   "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT   isolate SM11 extends the S. meliloti pan-genome.";
RL   J. Biotechnol. 155:20-33(2011).
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DR   EMBL; CP001831; AEH82762.1; -; Genomic_DNA.
DR   RefSeq; WP_014532106.1; NZ_JAJJBH010000005.1.
DR   AlphaFoldDB; F7XCY7; -.
DR   KEGG; smx:SM11_pC1689; -.
DR   PATRIC; fig|707241.3.peg.5600; -.
DR   HOGENOM; CLU_017633_0_0_5; -.
DR   Proteomes; UP000009045; Plasmid pSmeSM11c.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10747; DnaJ_C; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43096:SF52; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   4: Predicted;
KW   Plasmid {ECO:0000313|EMBL:AEH82762.1}.
FT   DOMAIN          4..69
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
SQ   SEQUENCE   305 AA;  33662 MW;  4D8651DC3DD64493 CRC64;
     MTDDPYQILG VPRTGKPDEI RKAYRKRAKE LHPDLHPGDK EVETKFKALS AAYHLLSDPE
     QRARFDRGEI DASGAERPQQ HFYRHYADAD HARRYGSAGG TGEFEDVSDI FADLFGQGGA
     GGRFKARGQD RHYHLELEFL DAVNGARRRI TFPDGNTLDL AIPAGTRDGS TLRLRGKGTP
     GIAGGEPGDA LIEISVRSHS VFRREGNDIE IDLPITLYEA VLGAKIEVPT ISGRVSMTIP
     KGSNTGDILR LRGKGVKSQH GPAGDQRVTL KVVLPTATDP DLERFMETWR RSHAYDPREA
     LGRTT
//
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