ID   HSCA_HAEIG              Reviewed;         619 AA.
AC   A5UGH6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN   OrderedLocusNames=CGSHiGG_04675;
OS   Haemophilus influenzae (strain PittGG).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittGG;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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; CP000672; ABQ99881.1; -; Genomic_DNA.
DR   RefSeq; WP_005691750.1; NC_009567.1.
DR   AlphaFoldDB; A5UGH6; -.
DR   SMR; A5UGH6; -.
DR   EnsemblBacteria; ABQ99881; ABQ99881; CGSHiGG_04675.
DR   KEGG; hiq:CGSHiGG_04675; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000001990; 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   CDD; cd10236; HscA_like_NBD; 1.
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; IPR042039; HscA_NBD.
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   TIGRFAMs; TIGR01991; HscA; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
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..619
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044860"
SQ   SEQUENCE   619 AA;  66948 MW;  3743667CC1DF5BA3 CRC64;
     MALLQIAEPG QAAAPHQHRL AVGIDLGTTN SLVASVRSGQ SVILNDEQER SLVPSVVHYG
     VEEKKVGLEA FEQASLDPKN TVISVKRLIG RSLSDVQSRY SSLPYEFVAS ENGLPLIITA
     QGSKSPIEVS SDILSRLNHI AEQRLGGELS GVVITVPAYF DDAQRQSTKD AARLAGLNVL
     RLLNEPTAAA LAYGLDSGQE GIIAVYDLGG GTFDISILRL SKGIFEVLAT GGDTALGGDD
     FDHLIADWII EQTKLKPQTA NQQRELITLA NQAKITLTNE KSAVISWQDF SVEISREQFN
     ELIYPLVKRS LLTCRRALKD ANVESEEVQA VVMVGGSTRV PYVREQVGEF FGKTPLTSID
     PDKVVALGAA IQADILVGNK TDSDMLLLDV VPLSLGIETM GGLVEKIIPR NTTIPVARAQ
     EFTTFKDGQT AMTVHVLQGE RELVDDCRSL GRFTLRGIPP MAAGAAHIRV TYQVDADGLL
     SVTAMEKSTK VQSSIQIKPS YGLTDEEVTA MIKSSFDNAQ EDLQARELAE QRVEADRVIE
     SVIVALQADG AELLSTDEFH HIETVLKQLM DVKLGSDRDA IAQGIKALDT ATQEFAARRM
     NASINKALTG KNLSDIENP