HSCA_BURCM
ID HSCA_BURCM Reviewed; 622 AA.
AC Q0BDQ8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Bamb_2159;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) 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; CP000440; ABI87715.1; -; Genomic_DNA.
DR RefSeq; WP_011657375.1; NZ_CP009798.1.
DR AlphaFoldDB; Q0BDQ8; -.
DR SMR; Q0BDQ8; -.
DR STRING; 339670.Bamb_2159; -.
DR EnsemblBacteria; ABI87715; ABI87715; Bamb_2159.
DR GeneID; 44692822; -.
DR KEGG; bam:Bamb_2159; -.
DR PATRIC; fig|339670.21.peg.2776; -.
DR eggNOG; COG0443; Bacteria.
DR OMA; PDPHQRR; -.
DR Proteomes; UP000000662; 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_1000044845"
SQ SEQUENCE 622 AA; 66188 MW; 1FE1EC43B489AFB9 CRC64;
MALLQISEPG MAPAPHQRRL AVGIDLGTTN SLVAAVRNSV PEVLPDEAGR ALLPSVVRYL
EKGGRRIGHE AKEQAATDPR NTIVSVKRFM GRGKAEVEGA ANAPYEFIDA PGMVQIRTID
GVKSPVEVSA EILATLRYRA EDTLGDELVG AVITVPAYFD EAQRQATKDA ARLAGLNVLR
LLNEPTAAAI AYGLDNAAEG LYAVYDLGGG TFDLSILKLT KGVFEVLAAG GDSALGGDDF
DHLLFGHVLA QAGIDAKALA PEDVRLLLDR VRVLKEALSS APQASLDVTL SNGTRLVQTI
SHDTFASLVE PLVQRTLTPT RKALRDAQVT PADIKGVVLV GGATRMPVIR DAVAKYFGQP
PLVNLDPDQV VALGAAIQAD LLAGNRGGGD DWLLLDVIPL SLGVETMGGL VEKIIPRNST
IPIARAQEFT TFKDGQTAMA IHVVQGEREL VADCRSLARF ELRGIPPMTA GAARIRVTYQ
VDADGLLSVF AREQHSGVEA SVVVKPSYGL ADDDIAKMLE DSFKTAEIDM RARALREAQV
EAQRMIEATQ AALAADGELL DDAERTQVDA LVAALRTIAQ GDDADAIETA TKALADGTDE
FAARRMDKSI KRALSGRRLD EI
