ID   HSCC_ECOLI              Reviewed;         556 AA.
AC   P77319;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 164.
DE   RecName: Full=Chaperone protein HscC {ECO:0000305};
DE   AltName: Full=Hsc62 {ECO:0000303|PubMed:9735342};
GN   Name=hscC {ECO:0000303|PubMed:12054669}; Synonyms=ybeW;
GN   OrderedLocusNames=b0650, JW0645;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9735342; DOI=10.1006/bbrc.1998.9255;
RA   Yoshimune K., Yoshimura T., Esaki N.;
RT   "Hsc62, a new DnaK homologue of Escherichia coli.";
RL   Biochem. Biophys. Res. Commun. 250:115-118(1998).
RN   [6]
RP   FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=12054669; DOI=10.1016/s0006-291x(02)00403-5;
RA   Yoshimune K., Yoshimura T., Nakayama T., Nishino T., Esaki N.;
RT   "Hsc62, Hsc56, and GrpE, the third Hsp70 chaperone system of Escherichia
RT   coli.";
RL   Biochem. Biophys. Res. Commun. 293:1389-1395(2002).
RN   [7]
RP   FUNCTION, AND OVEREXPRESSION.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=12059959; DOI=10.1046/j.1365-2443.2002.00545.x;
RA   Arifuzzaman M., Oshima T., Nakade S., Mori H.;
RT   "Characterization of HscC (Hsc62), homologue of Hsp70 in Escherichia coli:
RT   over-expression of HscC modulates the activity of house keeping sigma
RT   factor sigma70.";
RL   Genes Cells 7:553-566(2002).
RN   [8]
RP   FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, DOMAIN, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=12183460; DOI=10.1074/jbc.m206520200;
RA   Kluck C.J., Patzelt H., Genevaux P., Brehmer D., Rist W.,
RA   Schneider-Mergener J., Bukau B., Mayer M.P.;
RT   "Structure-function analysis of HscC, the Escherichia coli member of a
RT   novel subfamily of specialized Hsp70 chaperones.";
RL   J. Biol. Chem. 277:41060-41069(2002).
RN   [9]
RP   DOMAIN.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=14734171; DOI=10.1016/s0378-1097(03)00863-2;
RA   Arifuzzaman M., Oshima T., Mori H.;
RT   "The ATPase domain of HscC (DnaK homolog) is essential for interfering
RT   sigma70 activity in E. coli.";
RL   FEMS Microbiol. Lett. 230:99-104(2004).
CC   -!- FUNCTION: Chaperone that exhibits ATPase activity (PubMed:12054669,
CC       PubMed:12183460, PubMed:9735342). It interacts with the RNA polymerase
CC       sigma factor RpoD (sigma-70) and inhibits its activity
CC       (PubMed:12059959). HscC may function under specific conditions where
CC       the transient inhibition of sigma-70 is required (PubMed:12059959). It
CC       does not inhibit the activity of sigma-32 (PubMed:12059959). Binds
CC       peptides and can prevent aggregation of denatured substrates
CC       (PubMed:12183460). However, HscC may not have general chaperone
CC       activity as it does not assist refolding of a denatured model substrate
CC       (PubMed:12183460). {ECO:0000269|PubMed:12054669,
CC       ECO:0000269|PubMed:12059959, ECO:0000269|PubMed:12183460,
CC       ECO:0000269|PubMed:9735342}.
CC   -!- ACTIVITY REGULATION: The ATPase activity is stimulated by DjlC (Hsc56)
CC       (PubMed:12054669, PubMed:12183460). The activity is not influenced by
CC       GrpE, a nucleotide exchange factor for DnaK, or by a combination of
CC       GrpE and DnaJ (PubMed:12183460). However, the ATPase activity was
CC       proposed to be stimulated by GrpE in the presence of DjlC
CC       (PubMed:12054669). Activity is not stimulated by DnaJ (PubMed:12183460,
CC       PubMed:9735342). {ECO:0000269|PubMed:12054669,
CC       ECO:0000269|PubMed:12183460, ECO:0000269|PubMed:9735342}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.64 mM for ATP {ECO:0000269|PubMed:12054669};
CC         KM=0.112 mM for ATP {ECO:0000269|PubMed:12183460};
CC         Note=kcat is 3.84 min(-1) with ATP as substrate (PubMed:12054669).
CC         kcat is 0.0046 sec(-1) with ATP as substrate (PubMed:12183460).
CC         {ECO:0000269|PubMed:12054669, ECO:0000269|PubMed:12183460};
CC       Temperature dependence:
CC         ATPase activity increases with increase in temperature up to 40
CC         degrees Celsius, but decreases inversely at temperatures higher than
CC         45 degrees Celsius. {ECO:0000269|PubMed:9735342};
CC   -!- INTERACTION:
CC       P77319; P37649: pdeK; NbExp=3; IntAct=EBI-562084, EBI-562146;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12183460}.
CC   -!- DOMAIN: Contains an N-terminal ATPase domain, a substrate-binding
CC       domain and a C-terminal domain (PubMed:12183460, PubMed:14734171). The
CC       ATPase domain is the key factor for determination of the functional
CC       specificity of HscC and the substrate-binding domain might assist the
CC       physiological function, probably through stabilization of binding to
CC       the target proteins (PubMed:14734171). {ECO:0000269|PubMed:12183460,
CC       ECO:0000269|PubMed:14734171}.
CC   -!- DISRUPTION PHENOTYPE: Can be deleted, is not essential for viability
CC       under laboratory conditions (PubMed:12183460). Deletion of the gene
CC       causes a slow growth phenotype that is suppressed after several
CC       generations (PubMed:12183460). The deletion mutant shows
CC       hypersensitivity to Cd(2+) ions and UV irradiation, suggesting roles of
CC       HscC in the cellular response to these stress treatments
CC       (PubMed:12183460). {ECO:0000269|PubMed:12183460}.
CC   -!- MISCELLANEOUS: Overexpression of hscC causes severe growth inhibition,
CC       probably due to the reduced activity of sigma-70 (PubMed:12059959).
CC       HscC cannot replace DnaK in vitro in protein refolding and in vivo in
CC       heat-treated dnaK mutants (PubMed:12183460).
CC       {ECO:0000269|PubMed:12059959, ECO:0000269|PubMed:12183460}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; U82598; AAB40851.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73751.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35297.2; -; Genomic_DNA.
DR   PIR; H64799; H64799.
DR   RefSeq; NP_415183.1; NC_000913.3.
DR   RefSeq; WP_000367875.1; NZ_CP009789.1.
DR   AlphaFoldDB; P77319; -.
DR   SMR; P77319; -.
DR   BioGRID; 4263357; 38.
DR   BioGRID; 849603; 1.
DR   DIP; DIP-9942N; -.
DR   FunCoup; P77319; 75.
DR   IntAct; P77319; 33.
DR   STRING; 511145.b0650; -.
DR   PaxDb; 511145-b0650; -.
DR   EnsemblBacteria; AAC73751; AAC73751; b0650.
DR   GeneID; 945218; -.
DR   KEGG; ecj:JW0645; -.
DR   KEGG; eco:b0650; -.
DR   KEGG; ecoc:C3026_03250; -.
DR   PATRIC; fig|1411691.4.peg.1618; -.
DR   EchoBASE; EB3417; -.
DR   eggNOG; COG0443; Bacteria.
DR   InParanoid; P77319; -.
DR   OMA; RFMGTEK; -.
DR   OrthoDB; 9766019at2; -.
DR   PhylomeDB; P77319; -.
DR   BioCyc; EcoCyc:G6357-MONOMER; -.
DR   PRO; PR:P77319; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P77319; -.
DR   GO; GO:0005737; C:cytoplasm; EXP:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0006950; P:response to stress; IMP:EcoCyc.
DR   CDD; cd10235; ASKHA_NBD_HSP70_HscC; 1.
DR   FunFam; 2.60.34.10:FF:000015; Molecular chaperone HscC; 1.
DR   FunFam; 3.30.420.40:FF:000144; Molecular chaperone HscC; 1.
DR   FunFam; 3.90.640.10:FF:000024; Molecular chaperone HscC; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.90.640.10; Actin, Chain A, domain 4; 1.
DR   Gene3D; 2.60.34.10; Substrate Binding Domain Of DNAk, Chain A, domain 1; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR042030; HscC_NBD.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..556
FT                   /note="Chaperone protein HscC"
FT                   /id="PRO_0000078659"
SQ   SEQUENCE   556 AA;  61986 MW;  899EBAC81F69EF8F CRC64;
     MDNAELAIGI DLGTTNSLIA VWKDGAAQLI PNKFGEYLTP SIISMDENNH ILVGKPAVSR
     RTSHPDKTAA LFKRAMGSNT NWRLGSDTFN APELSSLVLR SLKEDAEEFL QRPIKDVVIS
     VPAYFSDEQR KHTRLAAELA GLNAVRLINE PTAAAMAYGL HTQQNTRSLV FDLGGGTFDV
     TVLEYATPVI EVHASAGDNF LGGEDFTHML VDEVLKRADV ARTTLNESEL AALYACVEAA
     KCSNQSPLHI RWQYQEETRE CEFYENELED LWLPLLNRLR VPIEQALRDA RLKPSQIDSL
     VLVGGASQMP LVQRIAVRLF GKLPYQSYDP STIVALGAAI QAACRLRSED IEEVILTDIC
     PYSLGVEVNR QGVSGIFSPI IERNTTVPVS RVETYSTMHP EQDSITVNVY QGENHKVKNN
     ILVESFDVPL KKTGAYQSID IRFSYDINGL LEVDVLLEDG SVKSRVINHS PVTLSAQQIE
     ESRTRLSALK IYPRDMLINR TFKAKLEELW ARALGDEREE IGRVITDFDA ALQSNDMARV
     DEVRRRASDY LAIEIP
//