ID A0A285F046_9ACTN Unreviewed; 983 AA.
AC A0A285F046;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=PQQ-like domain-containing protein {ECO:0000313|EMBL:SNY04652.1};
GN ORFNames=SAMN05421748_101284 {ECO:0000313|EMBL:SNY04652.1};
OS Actinoplanes atraurantiacus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1036182 {ECO:0000313|EMBL:SNY04652.1, ECO:0000313|Proteomes:UP000219612};
RN [1] {ECO:0000313|EMBL:SNY04652.1, ECO:0000313|Proteomes:UP000219612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6857 {ECO:0000313|EMBL:SNY04652.1,
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; OBDY01000001; SNY04652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285F046; -.
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; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR45639:SF4; HSC70CB, ISOFORM G; 1.
DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-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 314..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 541..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 383..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..529
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 983 AA; 101754 MW; B71CB82D5FF087DC CRC64;
MTDGFVLGVD LGTSHTVAML RRPDGRTRPL LFDGRPLLPS AVFLDPTGRL HVGADALRLG
QADPGRLEPH PKRHVDEESV MLGDGATVPV ADLLAALLDA VAREAVATAG FLPPAVVTYP
ASWGARRRAV LTRALSQAGW PSDTLGQPAE TTLVTEPVAA ARYFADVLRR PLPEKSSLAV
FDFGGGTLDV AVVRRDGGSY AATASGGASY SVTASGGADD LGGLDIDAAL VDHLGKSLSG
AEPAAWQALT EPVTLAQWRA RRQFWEDVRG AKEMLSRSSF APVPVPGVEE AVHLTRDELE
AAADPLIRRG VSEAAAVIAA AGLSPIELAG LFLVGGSSRV PLVARLLHSE LGIAPTVLEQ
PELAAAEGAT LAAALRYAAG VSTAATPTPT PTTAPDFPPP ITDTQAASTP VDPISPAAGP
PAATASAGPP NAAASAGLPD VASRSAGPAA SPATGPPTSP AARPFNPDSD PPYSTDKTDE
RESIEAVDPW ATAEAAAIAA GHVTPTSATP SSAAPWQPPA PPPTYSPEAP PAAKSAKRRT
WIIAGAATLA VVLAAGTALA WTLWPRYPAL DYHPLADLQH LPAAVPIGSS WSDAAVIGDR
VYFASTDYDT GDLGVVAFDD GAKSAAWSQK QTGIAKRWRQ MVALPSGVAL FSDTDLDKDT
REVVVLDAGK GAKRWQRTVG RDDLVYFAGD HAIVADRAGR RLVGLKLEDG SEDWTRPDPG
DSTSATAVHV VTTPGDLDGP AGLTGRPFDA DLGDDPRLVQ ITPDREARLI DAGTGKVIAS
RQSVAGPDDE VVAHNGRLFV REDEDADRIV TYQLDKLGEP DVTYTAGSAT ARLTGLIPCG
DDRVCAIEGT GYGDDNATVV ALDAAEGGKV WERKVAKAET LVPVGEAVLA RSTAPETTLI
DATGKQIWTG KSDAVRLDAA NILEFSKPLV GYVDDPAVAG RHLGDDPVQL GPLQGVRTSS
CAWNTTLLAC VADKDFVVTS FAG
//