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Database: UniProt
Entry: D8MUH5_ERWBE
LinkDB: D8MUH5_ERWBE
Original site: D8MUH5_ERWBE 
ID   D8MUH5_ERWBE            Unreviewed;       450 AA.
AC   D8MUH5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Putative heat shock protein {ECO:0000313|EMBL:CAX60482.1};
GN   OrderedLocusNames=EbC_29510 {ECO:0000313|EMBL:CAX60482.1};
OS   Erwinia billingiae (strain Eb661).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN   [1] {ECO:0000313|EMBL:CAX60482.1, ECO:0000313|Proteomes:UP000008793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eb661 {ECO:0000313|EMBL:CAX60482.1,
RC   ECO:0000313|Proteomes:UP000008793};
RX   PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA   Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA   Knaust F., Geider K., Reinhardt R.;
RT   "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT   tasmaniensis with the pear pathogen E. pyrifoliae.";
RL   BMC Genomics 11:393-393(2010).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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DR   EMBL; FP236843; CAX60482.1; -; Genomic_DNA.
DR   RefSeq; WP_013202967.1; NC_014306.1.
DR   AlphaFoldDB; D8MUH5; -.
DR   STRING; 634500.EbC_29510; -.
DR   KEGG; ebi:EbC_29510; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_033976_0_0_6; -.
DR   Proteomes; UP000008793; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10231; YegD_like; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   InterPro; IPR042054; YegD-like.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00329; HSP70_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW   Stress response {ECO:0000313|EMBL:CAX60482.1}.
SQ   SEQUENCE   450 AA;  49103 MW;  5107EDF47666A4FB CRC64;
     MFIGFDYGTA NCSVAIMKDG VPALLPLEQG STLLPSMLCA PTRDAVSEWL FRHHQVPTPE
     ADNQAILRRA LAFNREEDIE VTPNSVQFGL ASLAQYMADP EDVWFVKSPK SFLGANGLKP
     QQVAFFEDLV CAMMLHIRQK AEQNLNQSIT QAVIGRPINF QGLGGDEANR QAQGILARAA
     SRAGFKDVEF QFEPVAAGLE FEATLKQETR VLVVDIGGGT TDCSMLLMGP EWHDKSDRSA
     SLLGHSGCRV GGNDLDIMLA FKELMPLLGL GGATEKGTAL PALPWWNAVA INDVPAQSDF
     YATASKKLLL DLIRDTREPE KVKRLLKVWQ QRLGYRLVRA AEESKIALSE QANVTTQLAF
     IEQSLETAIS VQGLEAAIAQ PLERIQEQVK MALDASGTRP DVIYLTGGSA RSPVLRQALQ
     QQLPDIPLAS GDDFGSVTAG LARWAQVMFR
//
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