HSCA_ECOLI
ID HSCA_ECOLI Reviewed; 616 AA.
AC P0A6Z1; P36541; P76990; P77497;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Chaperone protein HscA;
DE AltName: Full=Hsc66;
GN Name=hscA; Synonyms=hsc; OrderedLocusNames=b2526, JW2510;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8300516; DOI=10.1128/jb.176.3.610-619.1994;
RA Kawula T.H., Lelivelt M.J.;
RT "Mutations in a gene encoding a new Hsp70 suppress rapid DNA inversion and
RT bgl activation, but not proU derepression, in hns-1 mutant Escherichia
RT coli.";
RL J. Bacteriol. 176:610-619(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B;
RX PubMed=8134349; DOI=10.1073/pnas.91.6.2066;
RA Seaton B.L., Vickery L.E.;
RT "A gene encoding a DnaK/hsp70 homolog in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2066-2070(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
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 [5]
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 [6]
RP INDUCTION.
RX PubMed=7665466; DOI=10.1128/jb.177.17.4900-4907.1995;
RA Lelivelt M.J., Kawula T.H.;
RT "Hsc66, an Hsp70 homolog in Escherichia coli, is induced by cold shock but
RT not by heat shock.";
RL J. Bacteriol. 177:4900-4907(1995).
RN [7]
RP CHARACTERIZATION.
RX PubMed=9144776; DOI=10.1002/pro.5560060511;
RA Vickery L.E., Silberg J.J., Ta D.T.;
RT "Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from
RT Escherichia coli.";
RL Protein Sci. 6:1047-1056(1997).
RN [8]
RP CHARACTERIZATION.
RX PubMed=10869428; DOI=10.1073/pnas.130201997;
RA Hoff K.G., Silberg J.J., Vickery L.E.;
RT "Interaction of the iron-sulfur cluster assembly protein IscU with the
RT Hsc66/Hsc20 molecular chaperone system of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7790-7795(2000).
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. Involved in the maturation of IscU.
CC -!- INDUCTION: By cold shock. {ECO:0000269|PubMed:7665466}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; U01827; AAA18300.1; -; Unassigned_DNA.
DR EMBL; U05338; AAD13473.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75579.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16420.1; -; Genomic_DNA.
DR PIR; E65029; E65029.
DR RefSeq; NP_417021.1; NC_000913.3.
DR RefSeq; WP_001196613.1; NZ_STEB01000011.1.
DR PDB; 1U00; X-ray; 1.95 A; A=389-615.
DR PDBsum; 1U00; -.
DR AlphaFoldDB; P0A6Z1; -.
DR SMR; P0A6Z1; -.
DR BioGRID; 4262906; 75.
DR BioGRID; 849285; 2.
DR DIP; DIP-47348N; -.
DR IntAct; P0A6Z1; 28.
DR STRING; 511145.b2526; -.
DR jPOST; P0A6Z1; -.
DR PaxDb; P0A6Z1; -.
DR PRIDE; P0A6Z1; -.
DR EnsemblBacteria; AAC75579; AAC75579; b2526.
DR EnsemblBacteria; BAA16420; BAA16420; BAA16420.
DR GeneID; 67416910; -.
DR GeneID; 944885; -.
DR KEGG; ecj:JW2510; -.
DR KEGG; eco:b2526; -.
DR PATRIC; fig|1411691.4.peg.4208; -.
DR EchoBASE; EB2051; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR InParanoid; P0A6Z1; -.
DR OMA; PDPHQRR; -.
DR PhylomeDB; P0A6Z1; -.
DR BioCyc; EcoCyc:EG12130-MON; -.
DR BioCyc; MetaCyc:EG12130-MON; -.
DR EvolutionaryTrace; P0A6Z1; -.
DR PRO; PR:P0A6Z1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990230; C:iron-sulfur cluster transfer complex; IDA:EcoCyc.
DR GO; GO:0043531; F:ADP binding; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
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:0070417; P:cellular response to cold; IEP:EcoCyc.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..616
FT /note="Chaperone protein HscA"
FT /id="PRO_0000078625"
FT VARIANT 216
FT /note="S -> F (in hsca1)"
FT CONFLICT 456..465
FT /note="LRGIPALPAG -> CVVFRRYRLA (in Ref. 1; AAA18300)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="S -> T (in Ref. 1; AAA18300)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="Missing (in Ref. 1; AAA18300)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="Q -> K (in Ref. 2; AAD13473)"
FT /evidence="ECO:0000305"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:1U00"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:1U00"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:1U00"
FT STRAND 414..424
FT /evidence="ECO:0007829|PDB:1U00"
FT STRAND 433..439
FT /evidence="ECO:0007829|PDB:1U00"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:1U00"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:1U00"
FT STRAND 448..456
FT /evidence="ECO:0007829|PDB:1U00"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:1U00"
FT STRAND 481..487
FT /evidence="ECO:0007829|PDB:1U00"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:1U00"
FT STRAND 493..498
FT /evidence="ECO:0007829|PDB:1U00"
FT HELIX 506..518
FT /evidence="ECO:0007829|PDB:1U00"
FT HELIX 520..550
FT /evidence="ECO:0007829|PDB:1U00"
FT HELIX 551..553
FT /evidence="ECO:0007829|PDB:1U00"
FT HELIX 556..572
FT /evidence="ECO:0007829|PDB:1U00"
FT HELIX 578..609
FT /evidence="ECO:0007829|PDB:1U00"
SQ SEQUENCE 616 AA; 65652 MW; 9C80E6EF1BFDAB48 CRC64;
MALLQISEPG LSAAPHQRRL AAGIDLGTTN SLVATVRSGQ AETLADHEGR HLLPSVVHYQ
QQGHSVGYDA RTNAALDTAN TISSVKRLMG RSLADIQQRY PHLPYQFQAS ENGLPMIETA
AGLLNPVRVS ADILKALAAR ATEALAGELD GVVITVPAYF DDAQRQGTKD AARLAGLHVL
RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SRGVFEVLAT GGDSALGGDD
FDHLLADYIR EQAGIPDRSD NRVQRELLDA AIAAKIALSD ADSVTVNVAG WQGEISREQF
NELIAPLVKR TLLACRRALK DAGVEADEVL EVVMVGGSTR VPLVRERVGE FFGRPPLTSI
DPDKVVAIGA AIQADILVGN KPDSEMLLLD VIPLSLGLET MGGLVEKVIP RNTTIPVARA
QDFTTFKDGQ TAMSIHVMQG ERELVQDCRS LARFALRGIP ALPAGGAHIR VTFQVDADGL
LSVTAMEKST GVEASIQVKP SYGLTDSEIA SMIKDSMSYA EQDVKARMLA EQKVEAARVL
ESLHGALAAD AALLSAAERQ VIDDAAAHLS EVAQGDDVDA IEQAIKNVDK QTQDFAARRM
DQSVRRALKG HSVDEV
