HSCA_THIDA
ID HSCA_THIDA Reviewed; 620 AA.
AC Q3SEX4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Tbd_1168;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ97121.1; -; Genomic_DNA.
DR RefSeq; WP_011311680.1; NC_007404.1.
DR AlphaFoldDB; Q3SEX4; -.
DR SMR; Q3SEX4; -.
DR STRING; 292415.Tbd_1168; -.
DR EnsemblBacteria; AAZ97121; AAZ97121; Tbd_1168.
DR KEGG; tbd:Tbd_1168; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_4; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000008291; 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; 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..620
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044899"
SQ SEQUENCE 620 AA; 65960 MW; 55A6F56F20488365 CRC64;
MALLQISEPG MSSAPHQHRL AVGIDLGTTN TLVATVRSGL AVVLDDEAGR SLLPSVVRYR
PDGAIDVGYP AQAAQNVDPH NTIVSVKRFM GRGIADIDDI ASLPYRFVDA PGMVQLKTAA
GVKSPVEISA EILKLMRERA EASMGGELVG AVITVPAYFD DAQRQATKDA AQLAGLNVLR
LLNEPTAAAI AYGLDNASEG VYAVYDLGGG TFDISILRLA RGVFEVLATN GDSALGGDDF
DQRVFCWMLE QGRFAPLSAS DARLLLTKAR DAKEALTEHS EVRVTAVLST GEMMDATLTQ
RDFNAMTASL VAKTLAPTRK ALRDAGLAAD EVKGVVMVGG STRMPCIRQA VADFFKQTPL
TNLDPDKVVA LGAAMQADVL AGNRGGDDWL LLDVIPLSLG LETMGGLTEK VIPRNTTIPT
ARAQDFTTFK DGQTAMSVHV LQGERELAAN CRSLARFELR GIPPMVAGAA RIRVTFQVDA
DGLLAVSARE QSTGVEASIQ VKPSYGLADE DITRMLKDAF THAKDDMYAR ALNEQIVEAQ
GLIAATRAAL AEDGALLDDA EMAAIEAGIA GLEKLMAGPD HQAIKRGIEA LNATTTGFAQ
RRMDRNVRRA MAGQKLETFD
