ID F7NJL5_9FIRM Unreviewed; 1001 AA.
AC F7NJL5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Chaperone protein {ECO:0000313|EMBL:EGO63769.1};
GN ORFNames=ALO_11354 {ECO:0000313|EMBL:EGO63769.1};
OS Acetonema longum DSM 6540.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Acetonema.
OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO63769.1, ECO:0000313|Proteomes:UP000003240};
RN [1] {ECO:0000313|EMBL:EGO63769.1, ECO:0000313|Proteomes:UP000003240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO63769.1,
RC ECO:0000313|Proteomes:UP000003240};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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:EGO63769.1}.
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DR EMBL; AFGF01000092; EGO63769.1; -; Genomic_DNA.
DR RefSeq; WP_004095623.1; NZ_AFGF01000092.1.
DR AlphaFoldDB; F7NJL5; -.
DR STRING; 1009370.ALO_11354; -.
DR eggNOG; COG0326; Bacteria.
DR OrthoDB; 1837345at2; -.
DR Proteomes; UP000003240; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR001404; Hsp90_fam.
DR PANTHER; PTHR11528:SF26; HEAT SHOCK PROTEIN (HSP90-FAMILY)-RELATED; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003240}.
SQ SEQUENCE 1001 AA; 116166 MW; 532A61427EF2C0BF CRC64;
MSKYHYKDKF GGEPNLVADV TKTALMIFLK RMNTQYFAKA LELREAVQKL LSYIPATFPH
YTSHSVEHSD EIISQISQLL FKNQNSIKAT VNLSPTEAYI LIASAYLHDA GMVASDREKM
EIIASERWKC WLSTEGPSKR FFEIEKLRND LFVEESIRQF LADRQLRFLI GEFIRKEHHI
RSTQILQQNQ SELGRFAFDD PDLQRAISDV CLSHGLDYNE LDTDRYPDRR TIRGELVNMR
FFAILLRVGD LLDTVNDRAC PLLINAASPL PADSFAHWSK YQRIVHRLTA PDRIEITARC
KNQDEHRFLH DWFTWLVKEL KNAAISIIRC QLHNNWKPPV AEISTSSHPG NINIFPADDA
LYIPMDWKFE FDTDLVFKRL ISDVYDSQSA FLRELIQNAL DATRCQVYID LKNCSLTLPK
YPTEISETIR NKYPINIKLY EQEFTNELSG VREIKQVLSV EDFGIGMTEE IIQKYLLQVG
KSYYTTEDFL RNYHFHPTSQ YGIGFLSVFG VSSKITLETY SPKKVGRPIS LNLAGPRSYI
LVEKSDRNKN GTKITLVLDE PFETGDLEKI VRYWCKKVEF PIVLEDLGNQ ILITSEKPED
FIYEIPEIIE PYGKYSIRCF PIQASGLEGE IYVFAHSTSE SESWADLNYA KNYIIDHPQA
QIPTLPSDLT CIHGITIRHY NQLKNNCQLS IRVDFRDNSL KPSLSREKVR IPFRDENRLD
PRIENRLVQI LSDHLQTTSL ASGNNEWIYK QRLIRNISFL EEFWNGIPRS IRMFLGGIPR
LFSLKEIKSV EKIIAIVFPY EIENLKRRKF KLPEIAIPFN SLDSSVPVIT EIDMELLSKE
HNKAIFDNRV ITNVSILPNG FLGVEWQLGI STIKLKDTIE LAFFDSSDFF GAVLHKTSDT
VYSQIVLNEN NIFIQWLLNL KSMCESEDHG LSSRQFSHII DLVEKVVRYN DYPELLNHLN
NWRNMGEISD QLDSLQVCSN EREFYISGKK MIVLNKYMLL M
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