HSCA_VARPS
ID HSCA_VARPS Reviewed; 618 AA.
AC C5CXC5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Vapar_2146;
OS Variovorax paradoxus (strain S110).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=543728;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S110;
RX PubMed=21183664; DOI=10.1128/jb.00925-10;
RA Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA Ovchinnikova G., Goodwin L., Han C.;
RT "Complete genome sequence of the metabolically versatile plant growth-
RT promoting endophyte, Variovorax paradoxus S110.";
RL J. Bacteriol. 193:1183-1190(2011).
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; CP001635; ACS18781.1; -; Genomic_DNA.
DR RefSeq; WP_012747265.1; NC_012791.1.
DR AlphaFoldDB; C5CXC5; -.
DR SMR; C5CXC5; -.
DR STRING; 543728.Vapar_2146; -.
DR EnsemblBacteria; ACS18781; ACS18781; Vapar_2146.
DR GeneID; 45056430; -.
DR KEGG; vap:Vapar_2146; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_4; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
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..618
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000212535"
SQ SEQUENCE 618 AA; 64991 MW; E6C15434C938B5CC CRC64;
MALLQISEPG QAPDPHQRRI AVGIDLGTTH SLVAAVRNGV AECLPDDQGR VILPSAVRYL
DRERRQIGFD ALAARAQDAA NTITSVKRLM GRGLADIANR ESMSYRLVDE GGMVKVETAA
GIKSPVEISA EILATLRYRA EDTFDGELYG AVITVPAYFD EGQRQATKDA AQLAGLNVLR
LISEPTAAAI AYGLDNASEG VYAVYDLGGG TFDISILRLT QGVFEVIATG GDSALGGDDY
DHALADFVLA QTGLQVGSDA DKAAVLVAAR AAKEALTDAD SVAFHAKLAG GAARFDLARA
QFDAATKPLT DRTIAAVRKA LRDAKLKPDD LQGIVLVGGS TRMPQIRRAV AEFFGREPLV
NLNPDEVVAL GAAIQANQLA GNNGAGDLLL LDVIPLSLGI ETMGGLVERI VPRNQTIPTA
MAQDFTTYQD GQTALALHVV QGERDLVADC RSLARFTLRG IPPMAAGAAR IRVTFTVDAD
GLLSVSAKEQ GSGVEASVAV KPSYGLSDDQ IATMLQESFS TAQQDMQARA LVEARVDAER
MLLATQSALD ADGDLLGEEE RAVIDASMAK LREAAKGNDA AAIEGATKAL ANDTEAFAAQ
RMNAGIARAL SGRKLESL
