ID   HSCA_HAES1              Reviewed;         616 AA.
AC   Q0I1K8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=HS_0285;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(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; CP000436; ABI24563.1; -; Genomic_DNA.
DR   RefSeq; WP_011608439.1; NC_008309.1.
DR   AlphaFoldDB; Q0I1K8; -.
DR   SMR; Q0I1K8; -.
DR   STRING; 205914.HS_0285; -.
DR   EnsemblBacteria; ABI24563; ABI24563; HS_0285.
DR   KEGG; hso:HS_0285; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
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..616
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044861"
SQ   SEQUENCE   616 AA;  66982 MW;  43160EF0B2DB29BE CRC64;
     MALLQIAEPG QSAAPHQHKL AVGIDLGTTN SLVAAVRSGS SEVLRDEQDR LLIPSIVHLT
     EDQVIVGYEA GKLASQDPQN TIISVKRLIG RSCTDVQQRY PNLPYQFSAT ENGLPLLKTR
     RGLLSPVEIS AEILKKLTAL AEQRLGGELT GAVITVPAYF DDAQRQSTKD AAKLAGLKVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDVSILRL SKGVFEVLAT GGDTALGGDD
     FDHLLAEWIV KKSTVAPQND REKRQLIEVA NQVKVALTTN DKIRISYAEQ NLEITRDEFN
     SLISGLVKRS LLACRRTLKD ANLTPSDILE VVMVGGSTRI PYVREQVGEF FQCTPLTSID
     PDKVVALGAA IQADILVGNK PDSEMLLLDV IPLSLGIETM GGLVEKIIPR NTTIPVARAQ
     EFTTFKDGQT AMSVHVLQGE REMVTDCRSL ARFTLRGIPA MVAGAARIRV TYQVDADGLL
     SVTAVEKSTG VQASTQVKPS YGLTDDEIAN MLKSSMEHAK EDIQTRLLTE QRVDATRVIE
     SVYSALQQDE DLLDDNELSA VKNALVSLQK LIQEEDSLAI KQGIKMLDQA TQEFASRRMD
     KSIRRALSGQ HIEHIK