ID   HSCA_AZOVI              Reviewed;         619 AA.
AC   O69221;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, 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};
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=9582371; DOI=10.1074/jbc.273.21.13264;
RA   Zheng L., Cash V.L., Flint D.H., Dean D.R.;
RT   "Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx
RT   gene cluster from Azotobacter vinelandii.";
RL   J. Biol. Chem. 273:13264-13272(1998).
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   -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC       {ECO:0000269|PubMed:9582371}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00679}.
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DR   EMBL; AF010139; AAC24478.1; -; Genomic_DNA.
DR   PIR; T44285; T44285.
DR   AlphaFoldDB; O69221; -.
DR   SMR; O69221; -.
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_0000078615"
SQ   SEQUENCE   619 AA;  66108 MW;  2ACFEEFE68837D4E CRC64;
     MALLQIAEPG QSPQPHQRRL AVGIDLGTTN SLVATLRSGL AESLKTPRGN DPASAVRYLP
     DGRRVGRAAK AAAAVDPLNT VLSVKRLMGR GIADVKLLGE QLPYRFAEGE SHMPFIETVQ
     GPKSPVEVSA EILRVLRRRA EEALGGELVG AVITVPAYFD EAQRQATKDA ARLAGLDVLR
     LLNEPTAAAV AYGLDRGAEG VVAIYDLGGG TFDISILRLT RGVFEVLATG GDSALGGDDF
     DHAIANWIVE QAGLSADLDP GVQRHLLQLA CAAKEALSDS GSVTLAYGPW QGELSRERFE
     ALIEPLVARS LKACRRALRD AGIEPQEIAA VVMVGGSTRV PRVRRAAAEL FDRQPLTDID
     PDQVVAIGAA LQADTLAGNG RDGEELLLLD VNPLSLGLET MGRLMEKVIP RNTTLPVARA
     QEFTTYKDGQ TAMLIHVLQG ERELVKDCRS LARFELRGIP PMVAGAAKIR VTFQVDADGL
     LNVSARELGS GYEASVQVKP SYGLTDGEIA RMLKDSFEYA GGDKAARALR EQQVEAQRLL
     EAVQAALEAD GEALLSPAER AAIEAQMQAL RGVLDGPDAA VIETHVRHLT QVTDAFAARR
     LDASVKAALS GRRLNEIEE