ID   HSCA_RICBR              Reviewed;         595 AA.
AC   Q1RJ70;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Chaperone protein HscA homolog;
GN   Name=hscA; OrderedLocusNames=RBE_0513;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; CP000087; ABE04594.1; -; Genomic_DNA.
DR   RefSeq; WP_011477185.1; NC_007940.1.
DR   AlphaFoldDB; Q1RJ70; -.
DR   SMR; Q1RJ70; -.
DR   STRING; 336407.RBE_0513; -.
DR   EnsemblBacteria; ABE04594; ABE04594; RBE_0513.
DR   KEGG; rbe:RBE_0513; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_5; -.
DR   OMA; IRVEVTF; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001951; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 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   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_0000288744"
SQ   SEQUENCE   595 AA;  65673 MW;  FF6AA721AF072980 CRC64;
     MQIIEIREPG QAESKQEVKI AVGIDFGTTN SLIAISVGRK VKIIQTEDNK ELIPTTIEFT
     NNNITVGSNK GLRSIKRLFG KTLNEILNTP ALFSLVKDYI DLQSQEVKLN FANKQMRIAE
     IAAEVFIYLK QQAEKELTTE VTQAVITVPA HFNDAARGQV MLAARLAGLE VLRLIAEPTA
     AAYAYGLNKN QTGCYLVYDL GGGTFDVSIL NITEGVFQVI ATSGDNMLGG DDIDKIIADY
     FCNKFSLLDN LDTLRLAKKA KEALLNQDNF EFNNISLDKQ TFEQLITPII GRTINIAKEC
     LEIAGNPNID GIILVGGVTH ITLIKEELYK AFKVNILSDI DPDKAIVYGA ALQAENLTTP
     NIDSLLIDVV PLSLGMELYG GIVEKIIMRN TPIPISVVKE FTTYADNQTG IQFHILQGER
     EMVADCRTLA RFELKGLPPM KAGSIRAEVT FSIDADGILS VSAYEKISNT SHIVEVKPDY
     GIDTSEVDKV LENAYKNAKL DHAARLLQET VIEAESLIFN IEHAIKELVD LLSENEKHII
     SSLLNNIKHA IDARDRALIN NAVKDFKSKT KKSLNTKINI VISDLLKGKN INQIK