ID   HSCA_RICCN              Reviewed;         595 AA.
AC   Q92J07;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=RC0262;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL02800.1; -; Genomic_DNA.
DR   PIR; F97732; F97732.
DR   RefSeq; WP_010976923.1; NC_003103.1.
DR   AlphaFoldDB; Q92J07; -.
DR   SMR; Q92J07; -.
DR   EnsemblBacteria; AAL02800; AAL02800; RC0262.
DR   KEGG; rco:RC0262; -.
DR   PATRIC; fig|272944.4.peg.300; -.
DR   HOGENOM; CLU_005965_2_4_5; -.
DR   OMA; IRVEVTF; -.
DR   Proteomes; UP000000816; 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..595
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078643"
SQ   SEQUENCE   595 AA;  65991 MW;  A9C5B18D7F1DFBCD CRC64;
     MQIIEIREPE QADFKQERQI AVGIDFGTTN SLIAIAANRQ VKVIKSIDDK ELIPTTIDFT
     SNNFTIGNNK GLRSIKRLFG KTLKEILNTP ALFSLVKDYL DVNSSELKLN FANKQLRVPE
     IAAEIFIYLK NQAEEQLKTN LTKAVITVPA HFNDAARGEV MLAAKIAGFE VLRLIAEPTA
     AAYAYGLNKN QKGCYLVYDL GGGTFDVSIL NIQEGIFQVI ATNGDNMLGG NDIDVVITQY
     LCNKFDLPNS IDTLQLAKKA KETLTYKDSF NNDNVSINKQ ILEQLILPLV ERTINIAQEC
     LEQAGNPNID GVILVGGATR IPLIKDELYK AFKIDILSDI DPDKAVVWGA ALQAENLIAP
     HTNSLLIDVA PLSLGMELYG GIVEKIIMHN TPIPISVVKE FTTYVDNQTG IQFHILQGER
     EMAADCRSLA RFELKGLPPM KAGYIRAEVT FSIDADGILS VSAYEKISNT SHAIEVKPNH
     GIDKTEIDIM LENAYKNAKI DYTTRLLQEA VIEAEALIFS IERAIAELTI LSSESEISII
     NSLLDNIKEA VHARDWILIN NSIKEFKSKI KKSIDTKFNI IINDLLKGKN INQIK