HSCA_HAEI8
ID HSCA_HAEI8 Reviewed; 619 AA.
AC Q4QNG9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=NTHI0493;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX87428.1; -; Genomic_DNA.
DR RefSeq; WP_011272011.1; NC_007146.2.
DR AlphaFoldDB; Q4QNG9; -.
DR SMR; Q4QNG9; -.
DR EnsemblBacteria; AAX87428; AAX87428; NTHI0493.
DR KEGG; hit:NTHI0493; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002525; 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.
FT CHAIN 1..619
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044858"
SQ SEQUENCE 619 AA; 66939 MW; 875FC3D6EA4F9EFF CRC64;
MALLQIAEPG QAAAPHQHRL AVGIDLGTTN SLVASVRSGQ SVILNDEQER SLVPSVVHYG
VEEKKVGLEA FEQASLDPKN TVISVKRLIG RSLPDVQSRY SSLPYEFVAS ENGLPLIITA
QGPKSPIEVS SDILSRLNHI AEQRLGGELS GVVITVPAYF DDAQRQSTKD AARLAGLNVL
RLLNEPTAAA LAYGLDSGQE GIIAVYDLGG GTFDISILRL SKGIFEVLAT GGDTALGGDD
FDHLIADWVI EQTKLKPQTA NQQRELITLA NQAKITLTNE KSAVISWQDF SVEISREQFN
ELIYPLVKRS LLTCRRALKD ANVESEEVQA VVMVGGSTRV PYVREQVGEF FGKTPLTSID
PDKVVALGAA IQADILVGNK TDSDMLLLDV VPLSLGIETM GGLVEKIIPR NTTIPVARAQ
EFTTFKDGQT AMSVHVLQGE RELVDDCRSL GRFTLRGIPP MAAGAAHIRV TYQVDADGLL
SVTAMEKSTK VQASIQIKPS YGLTDEEVTA MIKSSFDNAQ EDLQARELAE QRVEADRVIE
SVIVALQADG AELLSTDEFH HIETVLKQLM DVKQGSDRDA IAQGIKALDT ATQEFAARRM
NASINKALTG KNLSDIENP