HTPG_NOCFA
ID HTPG_NOCFA Reviewed; 652 AA.
AC Q5Z3N4;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=NFA_1150;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC Rule:MF_00505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000255|HAMAP-Rule:MF_00505}.
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DR EMBL; AP006618; BAD54957.1; -; Genomic_DNA.
DR RefSeq; WP_011206644.1; NC_006361.1.
DR AlphaFoldDB; Q5Z3N4; -.
DR SMR; Q5Z3N4; -.
DR STRING; 247156.NFA_1150; -.
DR PRIDE; Q5Z3N4; -.
DR EnsemblBacteria; BAD54957; BAD54957; NFA_1150.
DR GeneID; 61130957; -.
DR KEGG; nfa:NFA_1150; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_11; -.
DR OMA; MRRMKEM; -.
DR Proteomes; UP000006820; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
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_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF00183; HSP90; 2.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..652
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000224219"
FT REGION 1..351
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 352..568
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 569..652
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 652 AA; 74542 MW; B0EBDDD93D43146C CRC64;
MTEHVEQLEF QAETHQLLEL MIHSVYSNKD TFLRELISNA SDALDKLRLE SFKDKDLHVD
TADLHIELEV DKDNRILTVR DNGIGMSRAE VVDLIGTLAK SGTAELRRKL SEAKSEAAAE
ELIGQFGIGF YSTFMVADKV TLTTRKAGET GGTRWESSAG SSTYTIEDLA EAPQGTAVSL
HLKPADEEDH LYDYTQEWKL REIVKKYSDF IAWPIRMQVE RTVTEGEGED KQEKTIVEEQ
TLNSRKALWT RPRGEVSDEE YKEFYKHVSH AWDEPLEIIP LKAEGTFEYQ ALLFLPSQAP
FDLFTREHKR GVQLYVKRVF IMDNCEELMP EYLRFVKGVV DAQDLSLNVS REILQQDRQI
QMIRKRLVKK VLATVKDLQQ AEDQSKYQTF WREFGRVLKE GLLSDFDNRE TILQVSSFAS
THSDSELTTL AQYVERMPEG QDAIYYMTGE SRQQVESSPH MEAFKAKGRE VLILTDPVDE
MWVGSVPEFD GKRFQSIAKG EVDLESEEEK KASEALREQQ DKEFADLLSW LGKTLEENIK
EVRLTNRLTT SPACLVGDVF DFTPMLERMY RASGQPVPVS KRILELNPTH PLVTGLRDAY
DQRKQDADEG KVPELTETAE LLYGTAVLAE GGELKDPARF AHILTDRLTR TL