HSCA_AROAE
ID HSCA_AROAE Reviewed; 622 AA.
AC Q5NYT1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=AZOSEA36580;
GN ORFNames=ebA6396;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI09783.1; -; Genomic_DNA.
DR RefSeq; WP_011239436.1; NC_006513.1.
DR AlphaFoldDB; Q5NYT1; -.
DR SMR; Q5NYT1; -.
DR STRING; 76114.ebA6396; -.
DR PRIDE; Q5NYT1; -.
DR EnsemblBacteria; CAI09783; CAI09783; ebA6396.
DR KEGG; eba:ebA6396; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_4; -.
DR OMA; IRVEVTF; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000006552; 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_0000078614"
SQ SEQUENCE 622 AA; 66724 MW; FE37AC5DFBC267A0 CRC64;
MALLQIAEPG QSAEPHKHRL AVGIDLGTTN SLVATVRNGI AVCLADEAGR SMLPSIVRYH
ADGRIEVGQT AAAAHTTDPK NTIMSVKRFM GRGLKDVSHV ESTPYDFIDA GGMVRLRTVQ
GVKTPVEISA EILKTLGARA EASLGGPLTG AVITVPAYFD DAQRQATKDA AKLAGLNVLR
LLNEPTAAAV AYGLDNASEG VYAIYDLGGG TFDLSILKLS RGIFEVLATN GDAALGGDDF
DHRLFCWILD KAAIEPPTSD DSRRLLMKAR EAKELLTASE EAPIRARLSS DEEVNLVVTR
EEFATMTQHL IAKTMAPMRK VLRDAGLGPE DVKGVVMVGG ATRMPHVQRA VAEFFGQEPL
TNLDPDKVVA LGAAIQANVL AGNRKDEDEW LLLDVIPLSL GLETMGGLTE KVVPRNSTLP
IARAQEFTTF KDGQTAMAFH VVQGEREMVK DCRSLARFEL RGIPPMVAGA ARIRVAFQVD
ADGLLSVSAR EMSSGVEASV LVKPSYGLTD DEIASMLKEG VEHVGDDMHA RALREQQVEA
ERVIEATTHA LEQDGALLNA DERASIEVAI AELKQLAAGD DPRIVKKGIE ALARATDEFA
ARRMDNSIRS ALAGHKVDEI QV
