HSCA_TOLAT
ID HSCA_TOLAT Reviewed; 616 AA.
AC C4L7J8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Tola_2015;
OS Tolumonas auensis (strain DSM 9187 / TA4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Tolumonas.
OX NCBI_TaxID=595494;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA Beller H.;
RT "Complete sequence of Tolumonas auensis DSM 9187.";
RL Submitted (MAY-2009) 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; CP001616; ACQ93614.1; -; Genomic_DNA.
DR RefSeq; WP_015879082.1; NC_012691.1.
DR AlphaFoldDB; C4L7J8; -.
DR SMR; C4L7J8; -.
DR STRING; 595494.Tola_2015; -.
DR PRIDE; C4L7J8; -.
DR EnsemblBacteria; ACQ93614; ACQ93614; Tola_2015.
DR KEGG; tau:Tola_2015; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_3_6; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000009073; 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; Reference proteome.
FT CHAIN 1..616
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000212534"
SQ SEQUENCE 616 AA; 66232 MW; B3B951970C05D458 CRC64;
MALLHIAEPG LSAAPHQQKW AVGIDLGTTN SLVAVVRSGV AETLKDEQGR DILPSVVRYL
PDGLQIGAEA KHAAAEDPLN TIQSVKRFMG KALSDITQTN LPYQFTGADK GLVHINTCQG
EVNPVQVSAE ILKALQLRAT EALGAELDGV VITVPAYFND AQRQATKDAA RLAGMHVLRL
LNEPTAAAVA YGLDSGQEGV IAVYDLGGGT FDISILRLHQ GVFEVMATGG DSALGGDDFD
HLLADWIAEQ ADLIAPFTPR VQRQLLDLAC DVKQQLSSQD TVAVSFAQWS GSIDRTQFED
LITPLVKKTL MSCRRAIKDA GVEADEVLEV VMVGGSTRVP LVRQLVGDFF GRTPLTSIDP
DKVVAVGAAI QADILVGNKP ESEMLLLDVI PLSLGLETMG GLVEKIIPRN TTIPAARAQD
FTTFKDGQTA MMIHVLQGER ELVSDCRSLA RFVLKGIPPL AAGAAHIRVT FQVDADGLLS
VSAMEKSTGV QAAIEVKPSY GLQEEDMLRM LRESVEFAEK DIKARMLVEQ KVEADRVLES
LRQALSKDGD ALLSPEERSV INDAIQNLVN IQQGDDTDAI KAAITALDEA TSEFAARRMD
SSIRQALQGH KIDEVN
