ID   HSCA_RICPU              Reviewed;         595 AA.
AC   C4K0Z7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=RPR_01965;
OS   Rickettsia peacockii (strain Rustic).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=562019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rustic;
RX   PubMed=20027221; DOI=10.1371/journal.pone.0008361;
RA   Felsheim R.F., Kurtti T.J., Munderloh U.G.;
RT   "Genome sequence of the endosymbiont Rickettsia peacockii and comparison
RT   with virulent Rickettsia rickettsii: identification of virulence factors.";
RL   PLoS ONE 4:E8361-E8361(2009).
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; CP001227; ACR47248.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4K0Z7; -.
DR   SMR; C4K0Z7; -.
DR   EnsemblBacteria; ACR47248; ACR47248; RPR_01965.
DR   KEGG; rpk:RPR_01965; -.
DR   HOGENOM; CLU_005965_2_4_5; -.
DR   OMA; IRVEVTF; -.
DR   Proteomes; UP000005015; Chromosome.
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   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; 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   PROSITE; PS00329; HSP70_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding.
FT   CHAIN           1..595
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000212533"
SQ   SEQUENCE   595 AA;  65957 MW;  B664D4C3D36605BF CRC64;
     MQIIEIREPE QADFKQEQQI AVGIDFGTTN SLIAIAANRK VKVIKSIDDK ELIPTTIDFT
     SNNFTIGNNK GLRSIKRLFG KTLKEILNTP ALFSLVKDYL DVNSSELKLN FANKQLRVPE
     IAAEIFIYLK NQAEEQLKTN LTKAVITVPA HFNDAARGEV MLAAKIAGFE VLRLIAEPTA
     AAYAYGLNNN QKGCYLVYDL GGGTFDVSIL NIQEGIFQVI ATNGDNMLGG NDIDVVITQY
     LCNKFDLPNS IDTLQLAKKA KETLTYKDSF NNDNVSINKQ TLEQLILPLV ERTINIAQEC
     LEQAGNPNID GVILVGGATR TPLIKDELYK AFKIDILSDI DPDKAVVWGA ALQAENLIAP
     HTNSLLIDVA PLSLGMELYG GIVEKIIMHN TPIPISVVKE FTTYVDNQTG IQFHILQGER
     EMAADCRSLA RFELKGLPPM KAGYIRAEVT FSIDADGILS VSAYEKISNT SHAIEVKPNH
     GIDKTEIDIM LENAYKNAKI DYTTRLLQEA VIEAEALIFS IERAIAELTT LLSESEISII
     NSLLDNIKEA VHARDWILIN NSIKEFKSKI KKSMDTKFNI IINDLLKGKN INQIK