ID A9BXS2_DELAS Unreviewed; 621 AA.
AC A9BXS2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Putative heat-shock chaperone protein {ECO:0000313|EMBL:ABX38348.1};
GN OrderedLocusNames=Daci_5720 {ECO:0000313|EMBL:ABX38348.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX38348.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX38348.1, 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, ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CP000884; ABX38348.1; -; Genomic_DNA.
DR RefSeq; WP_012207517.1; NC_010002.1.
DR AlphaFoldDB; A9BXS2; -.
DR STRING; 398578.Daci_5720; -.
DR GeneID; 24119387; -.
DR KEGG; dac:Daci_5720; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_030332_0_0_4; -.
DR Proteomes; UP000000784; 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; cd10170; HSP70_NBD; 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 PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000000784}.
SQ SEQUENCE 621 AA; 66486 MW; 840B60855106860D CRC64;
MDQSRQSSQA RFSIGIDLGT THCALSYVDR QASDGEKVEQ GVLDIPQLTG PSSVEARPLL
PSFLYLPHES ELTAADMALP WGASQDFVVG EFARSRGAAT PIRLVSSAKS WLCHPGVDRR
SPLLPADAPE EVHRVSPLTA SIRYLSHLRW AWEQAHPEAP FDAQDVTVTI PASFDPAARE
LTAEACRAAG FQKLTLLEEP QAALYSWIQA SGGQWRKQVQ SGEIILVVDV GGGTTDLSLI
AVLEKDGGLE LQRVAVGEHI LLGGDNMDLA LAYGVARKLA QEGKQLDAWQ TRALAHGCRQ
AKEQLLADAS LQSVPVVVPS RGSKLIGGSI RTEVTRDEVL QMLVEGFFPR AAVSDKPQTR
ARAALTQLGL PYAQDAAVTR HLAAFLSRQA GATEQIEGLK GTQPEGASFL HPSAILFNGG
VLKAPQIEQR ILEVVNGWLA GEGAQPARLL DGANLDLAVA RGAAYFGHVA AAGRGVRIRG
GTAQSYYVGV ESNMPAIPGM EPPISALCLA PFGMEEGTEV ALDTQEFGLV VGEPVRLRFF
GSSVRRADQV GTVLDFWGPE ELVELQEIEA HLPAEGRAPG EIVPVTLHAR VTDIGTLELN
AVPVGGEERW KVEFDVRADV A
//
