HSCA_ACIAC
ID HSCA_ACIAC Reviewed; 620 AA.
AC A1TPY4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Aave_2447;
OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=397945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAC00-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL Submitted (DEC-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; CP000512; ABM33022.1; -; Genomic_DNA.
DR RefSeq; WP_011795551.1; NC_008752.1.
DR AlphaFoldDB; A1TPY4; -.
DR SMR; A1TPY4; -.
DR STRING; 397945.Aave_2447; -.
DR EnsemblBacteria; ABM33022; ABM33022; Aave_2447.
DR KEGG; aav:Aave_2447; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002596; 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..620
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044837"
SQ SEQUENCE 620 AA; 66153 MW; 9E3C100C4D6BD4F6 CRC64;
MALLQISEPG QSPNPHQRRI AVGIDLGTTH SLVAAVRNGA AECLPDAEGR LLLPSVVRYL
PQGRRQIGYA AMDSRSEDAA NTLVSVKRFM GRGLKDIDHP ERLPYAFVPG QEGDMVAMQT
VDGVKSPVEV SAEILAELRH RAEDTFDEDL YGAVITVPAY FDDAQRQATK DAARLAGLNL
LRLINEPTAA AIAYGLDNAS EGVYAVYDLG GGTFDISILR LTQGVFEVIA TGGDSALGGD
DYDAVLAEWA LQRLGIRAES AQDKAAARIA ARACKEGLTA AESALFSARI GGNEVRLDVL
RGDFDAITSA LTERTLAAVR RALRDARLQR EDIQGVVMVG GSTRMPQIQR AVAAFFGTEP
LNNLNPDEVV ALGAAIQAHQ LAGNDPAGDM LLLDVIPLSL GIETMGGLVE RIISRNETIP
TAKAQDFTTY KDGQTALAIH VVQGERDLVA DCRSLARFEL RGIPPMAAGA ARIRVTFTVD
ADGLLGVSAR EQSTGVEARV DVKPSYGLSD DQIARMLQEG FATAGEDMRA RALVEARVEA
DRMLMATRTA LEADGDILPP GERQSIDVLV QALEAVREHE DASAIDAATQ ALARGTEAFA
ARRMNRGIQQ ALAGKSVQSL
