ID   HSCA_RICRO              Reviewed;         595 AA.
AC   B0BWJ7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=RrIowa_0319;
OS   Rickettsia rickettsii (strain Iowa).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=452659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Iowa;
RX   PubMed=18025092; DOI=10.1128/iai.00952-07;
RA   Ellison D.W., Clark T.R., Sturdevant D.E., Virtaneva K., Porcella S.F.,
RA   Hackstadt T.;
RT   "Genomic comparison of virulent Rickettsia rickettsii Sheila Smith and
RT   avirulent Rickettsia rickettsii Iowa.";
RL   Infect. Immun. 76:542-550(2008).
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; CP000766; ABY72223.1; -; Genomic_DNA.
DR   RefSeq; WP_012150479.1; NC_010263.3.
DR   AlphaFoldDB; B0BWJ7; -.
DR   SMR; B0BWJ7; -.
DR   STRING; 452659.RrIowa_0319; -.
DR   EnsemblBacteria; ABY72223; ABY72223; RrIowa_0319.
DR   GeneID; 45538856; -.
DR   KEGG; rrj:RrIowa_0319; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_5; -.
DR   OMA; IRVEVTF; -.
DR   Proteomes; UP000000796; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding.
FT   CHAIN           1..595
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000082984"
SQ   SEQUENCE   595 AA;  65994 MW;  EEE885F4149199D9 CRC64;
     MQIIEIREPE QADFKPEQQI AVGIDFGTTN SLIAIAANRK VKVIKSIDDK ELIPTTIDFT
     SNNFTIGNNK GLRSIKRLFG KTLKEILNTP ALFSLVKDYL DVNSSELKLN FANKQLRVPE
     IAAEIFIYLK NQAEEQLKTN LTKAVITVPA HFNDAARGEV MLAAKIAGFE VLRLIAEPTA
     AAYAYGLNKN QKGCYLVYDL GGGTFDVSIL NIQEGIFQVI ATNGDNMLGG NDIDVVITQY
     LCNKFDLPNS IDTLQLAKKA KETLTYKDSF NNDNVSINKQ TLEQLILPLV ERTINIAQEC
     LEQAGNPNID GVILVGGATR TPLIKDELYK AFKIDILSDI DPDKAVVWGA ALQAENLIAP
     HTNSLLIDVA PLSLGMELYG GIVEKIIMHN TPIPISVVKE FTTYVDNQTG IQFHILQGER
     EMAADCRSLA RFELKGLPPM KAGYIRAEVT FSIDADGILS VSAYEKISNT SHAIEVKPNH
     GIDKTEIDIM LENAYKNAKI DYTTRLLQEA VIEAEAFIFS IERAIAEFTT LLSESEISII
     NSLLDNIKEA VHARDWILIN NSIKEFKSKI KKSMDTKFNV IINDLLKGKN INQIK