ID   HSCA_ACIF5              Reviewed;         621 AA.
AC   B5ENY5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Lferr_0826;
OS   Acidithiobacillus ferrooxidans (strain ATCC 53993 / BNL-5-31)
OS   (Leptospirillum ferrooxidans (ATCC 53993)).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=380394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53993 / BNL-5-31;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Borole A.P.;
RT   "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993.";
RL   Submitted (AUG-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; CP001132; ACH83076.1; -; Genomic_DNA.
DR   RefSeq; WP_012536278.1; NC_011206.1.
DR   AlphaFoldDB; B5ENY5; -.
DR   SMR; B5ENY5; -.
DR   GeneID; 66431836; -.
DR   KEGG; afe:Lferr_0826; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_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..621
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000131661"
SQ   SEQUENCE   621 AA;  66063 MW;  8E866632ABE54A01 CRC64;
     MALMQIAEPG TAADPHQRRL AIGIDLGTTH SLVASVLSAV PTVMRDHDGK YLLPSVVRYL
     GGGGIHVGYP AVAAAGQDPH NTIASAKRLM GRGHGDVQTL AGHLPYDLVP GEGMVRLRTV
     AGEKSPVEVS AEILRVLKER AVETLGGEPE GAVITVPAYF DEAQRQATKD AARLAGLNVL
     RLLAEPTAAA VAYGLDKGSE GIFAIYDLGG GTFDISILRL QAGVFEVLAT AGDSALGGDD
     MDHALAEWLM QEEGGDASDP LWRRQVLQQA RTAKEALSAV AETMIVLTPS GRAAREIKLS
     RGRLESLIQP VIQRSLPACR RALRDAGLKL DEIEGVVLVG GATRVPAVRA MVEEFFRQKP
     LTDIDPDQVV AIGAAIQADA LVGNQREDLL LMDVLPLSLG LETMGGLVEK IIPRNTPIPV
     ARAQEFTTFK DGQTAMSIHV VQGERDLVQD CRSLARFSLR GIPPMVAGAA RIRVTFQVDA
     DGLLAVRAEE TSTGVRSEVV VKPSYGLNDE EIARMLQDSF IHGAEDVVRR RLSEAKVEGE
     RVREALRTAL AADADLLDPA EREALDKAGT ALTNALSGDD AGVITAAAEA VETAAEPLVQ
     RRMDSALRRA ITGRSIDELG D