HSCA_RALPJ
ID HSCA_RALPJ Reviewed; 621 AA.
AC B2U8U5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Rpic_0889;
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Chaperone involved in the maturation of iron-sulfur cluster-
CC containing proteins. Has a low intrinsic ATPase activity which is
CC markedly stimulated by HscB. {ECO:0000255|HAMAP-Rule:MF_00679}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00679}.
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DR EMBL; CP001068; ACD26039.1; -; Genomic_DNA.
DR RefSeq; WP_012435209.1; NC_010682.1.
DR AlphaFoldDB; B2U8U5; -.
DR SMR; B2U8U5; -.
DR STRING; 402626.Rpic_0889; -.
DR EnsemblBacteria; ACD26039; ACD26039; Rpic_0889.
DR KEGG; rpi:Rpic_0889; -.
DR PATRIC; fig|402626.5.peg.2088; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR CDD; cd10236; HscA_like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR HAMAP; MF_00679; HscA; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR042039; HscA_NBD.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR InterPro; IPR010236; ISC_FeS_clus_asmbl_HscA.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01991; HscA; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding.
FT CHAIN 1..621
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000131685"
SQ SEQUENCE 621 AA; 66261 MW; 1F9C3E82E4D90560 CRC64;
MALLQISEPG ESPAPHQRRL AVGIDLGTTN SLVASVRSSV PEVLPDDQGR PLLPSVVRYL
PTGGAHIGYK AQAEAVRDPK NTIISVKRFM GRGLKDVAHI ENTPYDFVDA PGMVQLKTVA
GVKSPVEVSA EILATLRQRA EDTLGDELVG AVITVPAYFD DAQRQATKDA AKLAGLNVLR
LLNEPTAAAI AYGLDNGSEG IYAVYDLGGG TFDISVLKLT KGVFEVMSTG GDSALGGDDF
DQRIVCWVVE QAGLQPLSAE DTRLLLNKAR AAKEWLSTAD STEIDAMLST GETVHLVLTA
ETFAELTATL VQKTLSPVRR ALRDAGVTVE DVKGVVLVGG ATRMPIIRRA VGQLFGQTPL
TNLDPDQVVA IGAAMQANLL AGNRAPGEDW LLLDVIPLSL GVETMGGLVE KIIPRNSTIP
VARAQEFTTF KDGQTAMAIH VLQGERELAS DCRSLARFEL RGIPPMVAGA ARIRVTYQVD
ADGLLSVSAR ETVSGVEASI AVKPSYGLGD DDVARMLQEG FQSAEDDMRR RALAEERVEG
ERLLEALSQA LAADGDLLSP EERAAIDTEI AALRTTMQGE DHRAIKDAVD ALSHGTDEFA
ARRMDRGIRK ALAGKRIEEL G
