ID D5SW49_PLAL2 Unreviewed; 529 AA.
AC D5SW49;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Heat shock protein 70 {ECO:0000313|EMBL:ADG67334.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:ADG67334.1};
GN OrderedLocusNames=Plim_1501 {ECO:0000313|EMBL:ADG67334.1};
OS Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS (Planctomyces limnophilus).
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Planctopirus.
OX NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG67334.1, ECO:0000313|Proteomes:UP000002220};
RN [1] {ECO:0000313|EMBL:ADG67334.1, ECO:0000313|Proteomes:UP000002220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290
RC {ECO:0000313|Proteomes:UP000002220};
RX PubMed=21304691; DOI=10.4056/sigs.1052813;
RA Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT 290).";
RL Stand. Genomic Sci. 3:47-56(2010).
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; CP001744; ADG67334.1; -; Genomic_DNA.
DR RefSeq; WP_013109765.1; NC_014148.1.
DR AlphaFoldDB; D5SW49; -.
DR STRING; 521674.Plim_1501; -.
DR KEGG; plm:Plim_1501; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_0_0_0; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000002220; Chromosome.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
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; IPR029047; HSP70_peptide-bd_sf.
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; 2.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
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 Oxidoreductase {ECO:0000313|EMBL:ADG67334.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002220};
KW Stress response {ECO:0000313|EMBL:ADG67334.1}.
SQ SEQUENCE 529 AA; 57624 MW; 2F309EC72036B7EB CRC64;
MTQFVDGLTV GIDLGTSSSG IATLAADGQP VVIPNSDGQM ITPSVVVIND NGEVVIGPHG
DWIRTVNPDR VIVGIKRQMG NPDYSKIIDG NPLNAEFFSA LILMKLKQDA EARLGGPVTN
AVITVPYYFN DPCRRATMNA GQIAGLNVID LLNEPTAATL AYAWQKGDLG KLQSGVPEKE
KTILVYDLGG GTFDVTVVRY SAMQFRVLAT DGDTFLGGLD WTRRLVNHIA EQFRLNYRLD
PRDDARARLA LTDECDEVKR ALSELPQAAL EFSFKEKTLK PVITRAEFER LTADLLQRTR
DTTEFVLDGV GVAPQELDEV LLIGGSTYMT GVSAMLEKLC GRVPVRVLDP QLAVAQGAAI
HAGILQARET GQVLGQTGTV VSRLKSVEAV DVNSHSLGIE ITPPGDRNRK LNHIMIPRNT
ALPCEFKQRF VTNTPNPAGI LVRLLEGETK EIDGCTFIGD FRITGLPESL PVGSPVELTY
RYDENRRITV VAKELTGGRQ ATCEIHWSSN SEAGTVDQMQ SLVNSFHVD
//
