ID A9BXS1_DELAS Unreviewed; 951 AA.
AC A9BXS1;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=DnaK-related protein {ECO:0000313|EMBL:ABX38347.1};
GN OrderedLocusNames=Daci_5719 {ECO:0000313|EMBL:ABX38347.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX38347.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX38347.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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DR EMBL; CP000884; ABX38347.1; -; Genomic_DNA.
DR RefSeq; WP_012207516.1; NC_010002.1.
DR AlphaFoldDB; A9BXS1; -.
DR STRING; 398578.Daci_5719; -.
DR GeneID; 24118860; -.
DR KEGG; dac:Daci_5719; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_013948_0_0_4; -.
DR Proteomes; UP000000784; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10170; HSP70_NBD; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR021030; DUF3731.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF12531; DUF3731; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000784}.
FT REGION 464..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 951 AA; 102533 MW; 737E26A2280221B1 CRC64;
MPDTAASESS APAPASGAAH IVGIDLGTSH TVVAHVPVGG TAADIALLPV AQRVSASEVA
AQVLLPSARY QAAPGELGDA WQQPWTALGA DAQAPAVNGR WARDLGAAVP SRLVASAKSW
LSHAGVDRTG AILPWGAPEE VARLSPLQAS ASYLDHVRQA WDRAHPGAPL RDQLVVLTVP
ASFDEGARAL TLEAAQLAGL PAVQLLEEPK AAFHDWLVLQ GERLAAELAH CRLVLVVDVG
GGTTDLTLIR VQPGDAGGLP VLTRTAVGEH LMLGGDNMDL ALAHRLEPQF APPGERLPAA
RFAQLVQRCR TAKEQLLANE APESVAVTLL GGGSKLLAQT RTATLRRDEV REAVVEGFMP
LAGLQDLPTR RQGALRGLGL PYPADAAITR HLAHFLAQHA AGDLPDAVLL NGGVFHAHAL
AQRLVAQLQA WRGQPLRLLH NPHPDWAVAR GAAAHGLAMH VQSRPSEDLP ESEDARTVPA
PVPRIGGGSP RSYWLVLPEK AGAAPQGICL LPRGTEEGVR IVLSGRRFAL RLGQAVRFSL
VANSLAAAPA QAGRIAALDG EGWVELPALS TVLPAPEGRD KAQVEVQLQA CMTEVGTLEV
RCVAADDAQR QWLLPFSVRG ALAADGQDTG DRSARQGRLA DAVALIERIF GSQAQEVTAK
EVRQLRQSLE RRLGPREDWD LPLLRALFDA LLARSRRRRR TAEHERVWLN LAGWCLRPGV
GAELDGWRMQ QVWQLHGQGL GHGGEAANRT EWWVFWRRVA AGLDEARQME LLEEVAGHMQ
KAVQQSTQRS QGKSAHGSYD DMLRLFAAME AVPWQYRQEM GQWMLQRLKH PGESVQTWWA
IGRLAARMPL AANAHRVMPP EAAQEFLDAT LAQDWRRNET AMFAAVQMAR MTGDRALDLS
DAQRALVLER LRGAGAPQRW IDLVEQVQQM DAQDAKRSFG DSLPPGLVLV G
//