ID R7WTN4_9NOCA Unreviewed; 587 AA.
AC R7WTN4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Chaperone protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Rrhod_0007 {ECO:0000313|EMBL:EOM78618.1};
OS Rhodococcus rhodnii LMG 5362.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM78618.1, ECO:0000313|Proteomes:UP000013525};
RN [1] {ECO:0000313|EMBL:EOM78618.1, ECO:0000313|Proteomes:UP000013525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM78618.1,
RC ECO:0000313|Proteomes:UP000013525};
RX PubMed=23788540;
RA Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA Dyson P.J., Facey P.D.;
RT "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT Vector of Trypanosoma cruzi.";
RL Genome Announc. 1:e00329-13(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOM78618.1}.
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DR EMBL; APMY01000001; EOM78618.1; -; Genomic_DNA.
DR RefSeq; WP_010836088.1; NZ_APMY01000001.1.
DR AlphaFoldDB; R7WTN4; -.
DR PATRIC; fig|1273125.3.peg.8; -.
DR eggNOG; COG0443; Bacteria.
DR Proteomes; UP000013525; Unassembled WGS sequence.
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 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; PTHR42749; CELL SHAPE-DETERMINING PROTEIN MREB; 1.
DR PANTHER; PTHR42749:SF1; CELL SHAPE-DETERMINING PROTEIN MREB; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR PROSITE; PS01036; HSP70_3; 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:UP000013525}.
FT REGION 357..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..437
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..499
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 58413 MW; 6A0E1F7AE206946B CRC64;
MTGSFDGRTA TSLGISTGSA GVGAALVRTE RTGSDSAPDV HDVMFRYLSA EQPANDLAGL
VRSAIRLMST QLPSGPHRPE SIAVTYRTQQ QQHVLRGAVA GRRAHLVPET AATLEFLRST
GRVARFDTIA VADVGASGVG VSIVDRVDGT VLDTARENGI GGDAVDALLV DHVTQQSGTG
PRLPADSAII AARCRSAKET LSKPDSPAGG GETVRIESVG DGARPVVLDR TAFDAVVAPA
ITRIAEFVRT RLAASPRTVD AVVLVGGGSG LPALAAAIAD VTDAAVVTTP EPESASATGA
ALLAAGPEAA LYPTTGGPRQ GLGSKLKVVG TVAVAVTAAA ALFGYGTSAL PSGGRGFAPA
ATDVQQTSHH DTAPGEEQPA SEVGGAVTAT PSPDSGGYTE VGEPPTTAGL PPDEWAADPT
TPWDVPASPP LTTVPPTSPP AETTTEAAPE TGTTAPEEGS PELTMPSIPT EPQPPVFEWP
DIPTFWPTVP APPGDAPGEG PGQGVPDSGS SAGTPSPGLP GAGGPDQGSP ESGEPANGAP
ATPPAPATTQ PVPVETSPAT ETSGTPETSG PVQPTETPAP EAVHPTG
//
