ID   HSCA_AZOVD              Reviewed;         621 AA.
AC   C1DE64;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Avin_40360;
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303;
RX   PubMed=19429624; DOI=10.1128/jb.00504-09;
RA   Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
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; CP001157; ACO80172.1; -; Genomic_DNA.
DR   RefSeq; WP_012702547.1; NC_012560.1.
DR   AlphaFoldDB; C1DE64; -.
DR   SMR; C1DE64; -.
DR   STRING; 322710.Avin_40360; -.
DR   EnsemblBacteria; ACO80172; ACO80172; Avin_40360.
DR   KEGG; avn:Avin_40360; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002424; 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..621
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000212527"
SQ   SEQUENCE   621 AA;  66248 MW;  0D0E6A792EA19C56 CRC64;
     MALLQIAEPG QSPQPHQRRL AVGIDLGTTN SLVATLRSGL AESLKDTEGE TILPSAVRYL
     PDGRVEVGRA AKAAAAVDPL NTVLSVKRLM GRGIADVKLL GEQLPYRFAE GESHMPFIET
     VQGPKSPVEV SAEILRVLRR RAEEALGGEL VGAVITVPAY FDEAQRQATK DAARLAGLDV
     LRLLNEPTAA AVAYGLDRGA EGVVAIYDLG GGTFDISILR LTRGVFEVLA TGGDSALGGD
     DFDHAIANWI VEQAGLSADL DPGVQRHLLQ LACAAKEALS DSGSVALAYG PWQGELSRER
     FEALIEPLVA RSLKACRRAL RDAGIEPQEI AAVVMVGGST RVPRVRRAAA ELFDRQPLTD
     IDPDQVVAIG AALQADTLAG NGRDGEELLL LDVNPLSLGL ETMGRLMEKV IPRNTTLPVA
     RAQEFTTYKD GQTAMLIHVL QGERELVKDC RSLARFELRG IPPMVAGAAK IRVTFQVDAD
     GLLNVSAREL GSGIEASVQV KPSYGLTDGE IARMLKDSFE YAGGDKAARA LREQQVEAQR
     LLEAVQAALE ADGEALLSPA ERAAIEAQMQ ALRGVLDGPD AAVIETHVRH LTQVTDAFAA
     RRLDASVKAA LSGRRLNEIE E