ID   HSCA_RICAH              Reviewed;         595 AA.
AC   A8GMI8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=A1C_01475;
OS   Rickettsia akari (strain Hartford).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=293614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hartford;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia akari.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000847; ABV74613.1; -; Genomic_DNA.
DR   RefSeq; WP_012149247.1; NC_009881.1.
DR   AlphaFoldDB; A8GMI8; -.
DR   SMR; A8GMI8; -.
DR   STRING; 293614.A1C_01475; -.
DR   PRIDE; A8GMI8; -.
DR   EnsemblBacteria; ABV74613; ABV74613; A1C_01475.
DR   KEGG; rak:A1C_01475; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_5; -.
DR   OMA; IRVEVTF; -.
DR   Proteomes; UP000006830; 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_1000044881"
SQ   SEQUENCE   595 AA;  65688 MW;  15730742AA4E2042 CRC64;
     MQIIEIREPE QTDFKQKQQI AVGIDFGTTN SLIAIATDRK VKVIKSIDDK EITPTTIDFT
     SNNFTIGNNK GLRSIKRLFG KTLKEILNTP ALFSLVKDYL DVNSNELKLN FANRRIRICE
     IAAEVFIYLK NQAEEQLKTH ITKAVITVPA HFNDAARGEV MLAAKIAGFE VLRLIAEPTA
     AAYAYGLNNN QKGCYLVYDL GGGTFDVSIL NIQEGIFQVI ATSGDNMLGG DDIDVVITQY
     LCNKFDLPNS IDTLQLAKKA KETLTYKDSF NNDNISINRQ ILEQLILPLV EYTINIAQEC
     LAQAGNPNID GVILVGGVTR IPLIKDELYK AFKVDILSDI DPDKAVVWGA ALQADNLIAP
     HTNSLLIDVV PLSLGMELYG GIVEKIIMRN TPIPIAVVKE FTTYADNQTG IQFHILQGER
     EMAVDCRSLA RFELKGLPPM KAGNIRAEVT FAIDADGILS VSAYEKISNT SHTIEVKPNH
     GIDNTEIDIM LENAYKNAQI DYTTRLLQEA IIEAEALISS IEGAMAELTT LLSESEISVI
     NSLLDNIKAA AKARDRILIN NSIKEFKSKI NKSMDTNLNI IINGVLKGKN INQIQ