ID   HSCA_RICPR              Reviewed;         593 AA.
AC   Q9ZDW5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Chaperone protein HscA homolog;
GN   Name=hscA; OrderedLocusNames=RP200;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235270; CAA14665.1; -; Genomic_DNA.
DR   PIR; B71731; B71731.
DR   RefSeq; NP_220588.1; NC_000963.1.
DR   RefSeq; WP_010886232.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDW5; -.
DR   SMR; Q9ZDW5; -.
DR   STRING; 272947.RP200; -.
DR   EnsemblBacteria; CAA14665; CAA14665; CAA14665.
DR   KEGG; rpr:RP200; -.
DR   PATRIC; fig|272947.5.peg.209; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_5; -.
DR   OMA; IRVEVTF; -.
DR   Proteomes; UP000002480; 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.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..593
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078644"
SQ   SEQUENCE   593 AA;  66019 MW;  AACB8D666AF55D21 CRC64;
     MQIIEITEPK QTDFQQKLQI AVGIDFGTTN SLIAIATNRK VKIIKSIGDK ELIPTTIDFI
     NEDLIIGNNK GLHSIKRLFG KTLKEILNTT TLFSLVKDYL DINSSELKLN FANKKMRIAE
     IAAEVFIYLK NQAEKQLKNN ITKAVITVPA HFNDAARGEI MLAAKIAGFE VLRLIAEPTA
     AAYAYGLNKN QTGRYLVYDL GGGTFDVSIL NIQEGIFQVI ATNGDNMLGG DDIDVVITQY
     LCNKFDLPHS IETLQLAKKA KEILTYKESF NNDIISINKQ TLEQLISPLV ERTINITQEC
     LEQSGNPNID GVILVGGTTR IPLIKDELYK AFKIDILSDI DPDKAVVCGA ALQAENLITQ
     HTNSLLIDVV PLSLGIELYG GIVEKIITRN TPIPIAVIKE FTTYADNQTG IQFHILQGER
     EMAADCRSLA RFELKGLPPM KAGNIRVEVT FAIDADGILS VSAYEKISNI SHNIEIKPNH
     GINKTEIETM LKNAYKNAKI DYTTRLLQEA VIETEALMSS IERSIIKLTK LLSESEISII
     NALLDNIKDA VQTRDQILIK NSIKEFKSKI KKYLDTKLNI NDLRKCKNSN QIK