ID R5LXD4_9FIRM Unreviewed; 665 AA.
AC R5LXD4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Chaperone protein HtpG {ECO:0000313|EMBL:CCY77672.1};
GN ORFNames=BN569_00873 {ECO:0000313|EMBL:CCY77672.1};
OS Butyrivibrio crossotus CAG:259.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1263062 {ECO:0000313|EMBL:CCY77672.1, ECO:0000313|Proteomes:UP000018300};
RN [1] {ECO:0000313|EMBL:CCY77672.1, ECO:0000313|Proteomes:UP000018300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:259 {ECO:0000313|Proteomes:UP000018300};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CCY77672.1}.
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DR EMBL; CAYU010000072; CCY77672.1; -; Genomic_DNA.
DR AlphaFoldDB; R5LXD4; -.
DR Proteomes; UP000018300; 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 CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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:UP000018300}.
SQ SEQUENCE 665 AA; 76644 MW; E351C1B4931365A4 CRC64;
MATEHGNLSI NSDNIFPIIK KWMYSDHDIF FRELISNGCD AITKLKKLAL MGEYNEPDDI
KYNINVKVSS KNKTITFTDN GLGMTAEEVN EYINQIAFSG AEAFLEKYKD KTNEDQIIGH
FGLGFYSAFM VAEKVAIDTL SYKEGSKPVH WECEGGTEYD MGDGNKDTVG TTITLYLNED
STEFANEFRA KEVIDKYCSF MPYEIYLDNE DDTEEKTQMI DKDELLDTDT IIETVKKEAK
LEEQEDEDGN KKVVEVEPAT ERYKIAKRPV SLSDTTPLWT KHPNDCTDEE YKEFYRKVFH
DYKEPLFWIH LNMDYPFNLK GILYFPKINI EFESAEGIIK LYNNQVFVAD NIKEVIPEFL
MLLKGVIDCP DLPLNVSRSA LQNDGFVKKI SEYITKKVAD KLSGMCKTDK ESYEKYWDDI
SPFIKFGCLK DDKFCDKMKD YILFKNLEGK YLTLPECLEE NKEKHENKVF YVTDEIKQGQ
YIKMFKDAGI DAVILKHSID QPFITHLEQK NENVKFLSID SDLSETFKEE TSEEDLSKAG
EELAEVFKKA LNNDKLTVKA EKLVDKNISS MITVNEESKR MADMMKMYAS SGMDMSMFGE
TGETLVLNLN NELVKYVLDN PQSDNVTMIC EQLYDLAKLS HEPLKPEQMT AFIARSNEIL
KLLAK
//