ID   HSCA_RUTMC              Reviewed;         614 AA.
AC   A1AWL7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Rmag_0573;
OS   Ruthia magnifica subsp. Calyptogena magnifica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Ruthia.
OX   NCBI_TaxID=413404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17303757; DOI=10.1126/science.1138438;
RA   Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA   Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA   Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT   "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL   Science 315:998-1000(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; CP000488; ABL02324.1; -; Genomic_DNA.
DR   RefSeq; WP_011737949.1; NC_008610.1.
DR   AlphaFoldDB; A1AWL7; -.
DR   SMR; A1AWL7; -.
DR   STRING; 413404.Rmag_0573; -.
DR   EnsemblBacteria; ABL02324; ABL02324; Rmag_0573.
DR   KEGG; rma:Rmag_0573; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002587; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..614
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044883"
SQ   SEQUENCE   614 AA;  67093 MW;  88C39F181672E970 CRC64;
     MALLQISEPG QVSAIHQHKL AIGIDLGTTN SLVASVMSGQ SKVLIHENNE TILPSVVHCG
     KDNKLTVGCN AYHYAKTDPT NTIISVKRFM GMSYKEVSTF KNCPYQLLEN GNNVLFHTAT
     GDLSAVEISA SILASLKQCA EKSLGGALFG AVITVPAYFN DAQRQATKDA ATLAGLKTLR
     LLNEPTAAAV AYGLESGEEG VHAIYDLGGG TFDISILSFS KGVFKVLAIS GDSTLGGDDF
     DALIVDDCIK QLGINKLTPT QMQKIKQFSR TAKETLSNHE FAKFNCIEKS YRITKKKFEI
     LAKVLIKRTL LLTKRAIRDA QVDVEDIKDI IMVGGSTRMP LVRFMVSDLF NKPVLCSINP
     DEVVAKGAAI QANILAGNKS QGDVLLLDVL PLSLGLETMG GLVEKVIHRN TTIPIIRAQE
     FTTFKDGQTA MSVHVLQGER ELVKDCRSLA KFDLQGIPPM VAGSARIQIE FQVDTDGLLS
     VSAVEQISGV KTNITIKPSY GLTDVQMEKM LKDSILFAKT DIQTRQLHET QVEANRTIQA
     IDLALKKDKH MLDVKMLNNI LTARTILFNM AHSDDEKAIK TALENLENTC SKFVEMRMNN
     TVMKAMQGHN VDEF