ID   HSCA_RICTY              Reviewed;         586 AA.
AC   Q68XG8;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=RT0190;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017197; AAU03674.1; -; Genomic_DNA.
DR   RefSeq; WP_011190661.1; NC_006142.1.
DR   AlphaFoldDB; Q68XG8; -.
DR   SMR; Q68XG8; -.
DR   STRING; 257363.RT0190; -.
DR   EnsemblBacteria; AAU03674; AAU03674; RT0190.
DR   KEGG; rty:RT0190; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_0_0_5; -.
DR   OMA; IRVEVTF; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000604; 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.
FT   CHAIN           1..586
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078645"
SQ   SEQUENCE   586 AA;  65323 MW;  FC099D010CDA9D71 CRC64;
     MQIIEITEPK QTDCQQKLQI AVGIDFGTTN SLIAIATNRK VNIIKSKGDK ELIPTTIDFI
     NEDLIIGNNK GLRSIKRLFG KTLKEILNTK TLFALVKDYL DINSSELKLN FANKKMRIAE
     IAAEVFIYLK NQAEKQLKNN ITKAVITIPA HFNDTARGEI MLAAKIAGFE VLRLIAEPTA
     AAYAYGLNRN QTGRYLVYDL GGGTFDVSIL NIQEGIFQVI ATNGDNMLGG DDIDVVITQY
     ICNKFDLPNS SETLQLAKKA KETLTYKESF NNDIISINKQ TLEQLIFPLV KHTINITQEC
     LEQSGNPNID GVILVGGTTR IPLIKDELYK AFKINILSDI DPDKAVVCGA ALQAENLIAP
     HTNSLLIDVV PLSLGIELYG GIVEKIIMRN TPIPIAVIKE FTTYADNQTG IQFHILQGER
     EMAADCRSLA RFELKGLPPM KAGNIRAEVT FAIDADGILS ISAYEKISNI SHTIEVKPNH
     GIDKTEIEIM LENAYKNASI DYTTRLLQEE IIETEALISN IERSIIELTT LLSESEISII
     NALFDNIKYA VQTRDQTLIK HSIKEFKSKI KNIWIQNIIN INDLRK