ID   HSCA_HAEDU              Reviewed;         617 AA.
AC   Q7VMA4;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=HD_1087;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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; AE017143; AAP95953.1; -; Genomic_DNA.
DR   RefSeq; WP_010945002.1; NC_002940.2.
DR   AlphaFoldDB; Q7VMA4; -.
DR   SMR; Q7VMA4; -.
DR   STRING; 233412.HD_1087; -.
DR   EnsemblBacteria; AAP95953; AAP95953; HD_1087.
DR   KEGG; hdu:HD_1087; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000001022; 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; Reference proteome.
FT   CHAIN           1..617
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078629"
SQ   SEQUENCE   617 AA;  66569 MW;  20512A41BAC1E599 CRC64;
     MALLQIAEPG QTAAPHQLRL AVGIDLGTTN SLVASVRSRQ VQVLLDDKES ALIPSVVHYT
     ETSKMVGVTA FEQASYDPQN TIISAKRLIG RSLMDVQTRY PNLPYQFQAS ENGLPLIHTR
     QGYKSPIEVS ADILSHLNHL AEQRLAGELS GVVITVPAYF DDAQRQSTKD AARLVGLNVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SKGVFEVLAT GGDTALGGDD
     FDHLLADWIA TQAAVQPKNA TEQRQLLTLA TQTKIALSQA DETPLHFANW TGNITQAQFN
     QLIQPLVKRS LVACRRALKD ASVDIEEVCQ VVMVGGSTRV PFVREAVGEF FAKKPLTSID
     PDKVVALGAA IQADILVGNK PDNEMLLLDV VPLSLGIETM GGLVEKIIPR NTTIPVARAQ
     EFTTAKDGQT AMSVHVLQGE RELVDDCRSL ARFTLRGIPP MVAGAATIRV TYQVDADGLL
     SVTAMEKSTK VQASIQIKPS YGLTDEEVTQ MIKSSMSNAK ADMEARQLAE QRVEADRAIE
     MVMAALQKDG KAVLSVAEFN AIEVEMQKLI ELKAGTDRIA IQQSIKDLDL ATQAFAAKRM
     NLSIQKALAG KAVDEII