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Database: UniProt
Entry: D3QC25_STANL
LinkDB: D3QC25_STANL
Original site: D3QC25_STANL 
ID   D3QC25_STANL            Unreviewed;       565 AA.
AC   D3QC25;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=Heat shock protein 70 {ECO:0000313|EMBL:ADD44914.1};
GN   OrderedLocusNames=Snas_5280 {ECO:0000313|EMBL:ADD44914.1};
OS   Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS   NBRC 102104 / LLR-40K-21).
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Stackebrandtia.
OX   NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD44914.1, ECO:0000313|Proteomes:UP000000844};
RN   [1] {ECO:0000313|EMBL:ADD44914.1, ECO:0000313|Proteomes:UP000000844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC   LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX   PubMed=21304662; DOI=10.4056/sigs.47643;
RA   Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA   Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA   Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA   Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT   40K-21).";
RL   Stand. Genomic Sci. 1:292-299(2009).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; CP001778; ADD44914.1; -; Genomic_DNA.
DR   RefSeq; WP_013020485.1; NC_013947.1.
DR   AlphaFoldDB; D3QC25; -.
DR   STRING; 446470.Snas_5280; -.
DR   KEGG; sna:Snas_5280; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_038461_0_0_11; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000000844; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 3.30.420.40; -; 3.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF513; SLR0086 PROTEIN; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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:UP000000844};
KW   Stress response {ECO:0000313|EMBL:ADD44914.1}.
FT   REGION          197..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   565 AA;  60015 MW;  AC0029F8AAF4FBE3 CRC64;
     MTDRLGIDFG TANTVVARWN DATGTGEAIP LSGVEVVRDV GNLQRVVPSL IAYSAVDERR
     WVGAQVTPAL RASDGVRVFR STKTSVAGRV VDLPRQVGQR RITAARAAAD FLGDVMTLAR
     LETGTEAELV LTAPVESFDP YRDWLVREVG ADLDRLRIVD EATAAAAGYG AKLKPGDVFG
     VFDFGAGTLD ISVVSVVDPD GPPPSPDARP GADRGSAGGG PPLAAGPADG RRQPTRLSGC
     GVRVISKVGI DLGGDHIDAL LADEVARLTG LAEADASVHN RVFAELLTAA EAAKVALTTA
     ESAVVAAVDP LTGREWRADV SRDRFTSLLR DNDILGRIGR AFRKTLDAAA AKGHPADSLR
     HLFLVGGSSL LPPVRELLSF QIDPGLLRLD RPLEAVAAGA AAIASGHDPV DFVQHDYAIR
     HVSQTTGGYE FEPVVPAGTD YPSTEPVASL TIKGVHEGQT RLGLAIYETA HASTRDTAAG
     LEIMFDTSGG ARTVAVSPQR RTELSQVWLN EEQLTFLKAE PPARAGIDRF RLEFHVDAQK
     RLTVSAFDLE RRIWVLDRQP VVGLA
//
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