ID   HSCA_HISS2              Reviewed;         616 AA.
AC   B0UVL9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, 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}; OrderedLocusNames=HSM_0158;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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; CP000947; ACA31340.1; -; Genomic_DNA.
DR   RefSeq; WP_012340717.1; NC_010519.1.
DR   AlphaFoldDB; B0UVL9; -.
DR   SMR; B0UVL9; -.
DR   STRING; 228400.HSM_0158; -.
DR   EnsemblBacteria; ACA31340; ACA31340; HSM_0158.
DR   KEGG; hsm:HSM_0158; -.
DR   HOGENOM; CLU_005965_2_3_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
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_1000082982"
SQ   SEQUENCE   616 AA;  67071 MW;  033005C61ED0A34E CRC64;
     MALLQIAEPG QSAAPHQHKL AVGIDLGTTN SLVAAVRSGS SEVLRDEQDR LLIPSIVHLT
     EDQAIVGYEA GQLASQDPQN TIISVKRLIG RSCTDVQQRY PNLPYQFNAT ENGLPLLKTR
     RGLLSPVEIS AEILKKLTAL AEQRLGGELT GAVITVPAYF DDAQRQSTKD AAKLAGLKVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDVSILRL SKGVFEVLAT GGDTALGGDD
     FDHLLAEWIV KKSTVAPQND REKRQLIEVA NQVKVALTTN DKIRISYAEQ NLEIMRDEFN
     FLISGLVKRS 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