HSCA_DELAS
ID HSCA_DELAS Reviewed; 622 AA.
AC A9BWU9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Daci_3995;
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000884; ABX36626.1; -; Genomic_DNA.
DR RefSeq; WP_012205820.1; NC_010002.1.
DR AlphaFoldDB; A9BWU9; -.
DR SMR; A9BWU9; -.
DR STRING; 398578.Daci_3995; -.
DR PRIDE; A9BWU9; -.
DR EnsemblBacteria; ABX36626; ABX36626; Daci_3995.
DR KEGG; dac:Daci_3995; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_3_4; -.
DR OMA; PDPHQRR; -.
DR Proteomes; UP000000784; 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; Reference proteome.
FT CHAIN 1..622
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000131671"
SQ SEQUENCE 622 AA; 65633 MW; FAB5BA8138223E8A CRC64;
MALLQISEPG QSPDPHQRRI AVGIDLGTTH SLVAAVRNGV AECLPDDQGR VLLPSVVRYL
PQGRREIGHA AQAALSTDAG NTIASAKRFM GRTLADIDAP EKLPYRFAEQ EAGRGVIGIE
TVDGTKTAVE VSAEILATLR FRAEDTFNDD IHGAVITVPA YFDDAQRQAT KDAAKLAGIN
LLRLINEPTA AAIAYGLDNG SEGVYAVYDL GGGTFDISIL RLSQGVFEVV STGGDSALGG
DDYDAALAEW VAQQTGVVPQ TAEDKARWRM AARLCKQALT DAQVATLTAE LSTGAVHFDV
KRSDFDASTA HLTARSLAAV RRALKDAGLA RDEVQGVVLV GGSTRMPQVR EAVAEFFGRD
PLINLNPDEV VALGAAIQAN QLAGNSSSGD MLLLDVIPLS LGVETMGGLV ERIISRNETI
PTARAQDFTT YKDGQTALAV HVVQGERDLV ADCRSLARFE LRGIPPMAAG AARIRVTFTV
DADGLLSVGA KEQTSGVEAH IHVKPSYGLS DDEVARMLQD GFATAQQDMQ ARALVEARVD
ADRMLMATES ALQADGDVLA ADQRAAIDAL IDALRASVGS EDAAVIEAAT QALAKGTESF
AAERMNRSIQ QALAGKSVQS LS
