HSCA_BURA4
ID HSCA_BURA4 Reviewed; 622 AA.
AC B1YT24;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN OrderedLocusNames=BamMC406_2032;
OS Burkholderia ambifaria (strain MC40-6).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=398577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC40-6;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6.";
RL Submitted (APR-2008) 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; CP001025; ACB64513.1; -; Genomic_DNA.
DR RefSeq; WP_012364218.1; NC_010551.1.
DR AlphaFoldDB; B1YT24; -.
DR SMR; B1YT24; -.
DR EnsemblBacteria; ACB64513; ACB64513; BamMC406_2032.
DR KEGG; bac:BamMC406_2032; -.
DR HOGENOM; CLU_005965_2_4_4; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001680; Chromosome 1.
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..622
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000131666"
SQ SEQUENCE 622 AA; 66162 MW; FFD4477D33CA790D CRC64;
MALLQISEPG MAPAPHQRRL AVGIDLGTTN SLVAAVRNSV PEVLPDEAGR ALLPSVVRYL
EKGGRRIGHE AKEQAATDPR NTIVSVKRFM GRGKAEVEGA ANAPYEFVDA PGMVQIRTID
GVKSPVEVSA EILATLRYRA EDTLGDELVG AVITVPAYFD DAQRQATKDA ARLAGLNVLR
LLNEPTAAAI AYGLDNAAEG LYAVYDLGGG TFDLSILKLT KGVFEVLAAG GDSALGGDDF
DHVLFGHVLA QAGIDAKALA PEDVRLLLDR VRVLKEALSS APQASLDVTL SNGARLVQTI
SHDTFASLVE PLVQRTLTPT RKALRDAQVT PADIKGVVLV GGATRMPVIR DAVAKYFGQP
PLVNLDPDQV VALGAAIQAD LLAGNRGSGD DWLLLDVIPL SLGVETMGGL VEKIIPRNST
IPIARAQEFT TFKDGQTAMA IHVVQGEREL VADCRSLARF ELRGIPPMTA GAARIRVTYQ
VDADGLLSVF AREQHSGVEA SVVVKPSYGL ADDDIAKMLE DSFKTAEIDM RARALREAQV
EAQRMIEATQ AALSADGELL DDAERTQVDA LVAALRTIAQ GDDADAIETA TKALADGTDE
FAARRMDKSI KRALSGRRLD EI
