ID A0A285IB59_9ACTN Unreviewed; 888 AA.
AC A0A285IB59;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=WD40-like Beta Propeller Repeat {ECO:0000313|EMBL:SNY44296.1};
GN ORFNames=SAMN05421748_10754 {ECO:0000313|EMBL:SNY44296.1};
OS Actinoplanes atraurantiacus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1036182 {ECO:0000313|EMBL:SNY44296.1, ECO:0000313|Proteomes:UP000219612};
RN [1] {ECO:0000313|EMBL:SNY44296.1, ECO:0000313|Proteomes:UP000219612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6857 {ECO:0000313|EMBL:SNY44296.1,
RC ECO:0000313|Proteomes:UP000219612};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; OBDY01000007; SNY44296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285IB59; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000219612; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR Gene3D; 2.120.10.60; Tricorn protease N-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR InterPro; IPR011659; PD40.
DR PANTHER; PTHR45639:SF4; HSC70CB, ISOFORM G; 1.
DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR Pfam; PF00012; HSP70; 2.
DR Pfam; PF07676; PD40; 3.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000219612};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 570..592
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 367..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..516
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..558
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 92978 MW; 5A039A4B4C027C6F CRC64;
MARFWKHRGV ASEYSLGVDL GTTQTAAAVR ESDGRIDVVR LGTRRAEIPS LVFVTASGEL
LIGEAAERRG QAEPDRLARE FKRRVGDPVP ILAGGVPFSA HALTGKLLRH VLDTVVRLRG
GPPTTITLTH PANWGPYKRD QFDQAVRLAD VGPVLFRTEP EAAALRHATA RRVGPGETVA
VYDLGGGTFD VAVLRREGDD FVLLGEAEGI EQLGGADFDE AVFGHVLEVL GDAAGDLDGD
DPEVVTALAR LRRDCVEAKE ALSFDTETMI PVALPGLHRQ VRLNRSELES MIAPALADTI
DATRRALRGA GVTPDDLSAI LLAGGSSRIP LVAQILTDEL SRPVAADPHP EHSVALGAAL
AGATTPIPAR FSGRGGAAPI PTPSTGRGGA APIPTPSTGR GGAAPISAPS ARRGSATPAS
ARPASEPSTL ASPAPTSSPA SSSSAAPRQA ATAAAGVQYA RGAASVPGSS DLPDTSEMSV
TSGRSETATS PSVAPAPPAR TQIFSPPTPS PQTGYSPGPE SPGTYPAGSP VGYSAVADPH
AAYPAPPVQT PAGPRAPGEP EPGRRRNGRI LAITGAFVAV LVAAGTAAYI ALNRDDEPEK
PDDALPANSA AAVPYPTDKK ILVRVDTGAD SGPERISKIY AFQPGTDTPR TPLAGTEPGD
VLPKWSHDRK QIALTHNTGT ASEIYVMNAD GSERRKIIDD APGRVAWSSD DSKLAFVKKV
DGVTQLFTMP VAGGPHKQLT FSKDPKDDPF WSADGKAIAY WVQRGGIKQI YELDMADIKE
PGRQITTAAM GQANDPALSP DGSQVLFTRE GDNGDSDIWI VGRDGENPRQ LTDDPSREQD
PSWSPDGTWF AFARGPYERP RIVLLKPDGT GEAVVTKSGQ REAHPCWF
//