HSCC_ECOLI
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 03-AUG-2022, entry version 148.
DE RecName: Full=Chaperone protein HscC;
DE AltName: Full=Hsc62;
GN Name=hscC; Synonyms=ybeW; OrderedLocusNames=b0650, JW0645;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 CHARACTERIZATION.
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).
CC -!- FUNCTION: Probable chaperone. Has ATPase activity. Not stimulated by
CC DnaJ.
CC -!- INTERACTION:
CC P77319; P37649: pdeK; NbExp=3; IntAct=EBI-562084, EBI-562146;
CC -!- INDUCTION: By heat shock. Activated up to a temperature of 40 degrees
CC Celsius, after which levels decrease.
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; BAA35297.1; -; Genomic_DNA.
DR PIR; H64799; H64799.
DR RefSeq; NP_415183.1; NC_000913.3.
DR RefSeq; WP_000367875.1; NZ_SSZK01000037.1.
DR AlphaFoldDB; P77319; -.
DR SMR; P77319; -.
DR BioGRID; 4263357; 10.
DR BioGRID; 849603; 1.
DR DIP; DIP-9942N; -.
DR IntAct; P77319; 33.
DR STRING; 511145.b0650; -.
DR PaxDb; P77319; -.
DR PRIDE; P77319; -.
DR EnsemblBacteria; AAC73751; AAC73751; b0650.
DR EnsemblBacteria; BAA35297; BAA35297; BAA35297.
DR GeneID; 945218; -.
DR KEGG; ecj:JW0645; -.
DR KEGG; eco:b0650; -.
DR PATRIC; fig|1411691.4.peg.1618; -.
DR EchoBASE; EB3417; -.
DR eggNOG; COG0443; Bacteria.
DR InParanoid; P77319; -.
DR OMA; RKQTRFA; -.
DR PhylomeDB; P77319; -.
DR BioCyc; EcoCyc:G6357-MON; -.
DR PRO; PR:P77319; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10235; HscC_like_NBD; 1.
DR Gene3D; 2.60.34.10; -; 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; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
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; 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
