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Database: UniProt
Entry: C5T2B3_ACIDE
LinkDB: C5T2B3_ACIDE
Original site: C5T2B3_ACIDE 
ID   C5T2B3_ACIDE            Unreviewed;       623 AA.
AC   C5T2B3;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000256|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679};
GN   ORFNames=AcdelDRAFT_1043 {ECO:0000313|EMBL:EER61380.1};
OS   Acidovorax delafieldii 2AN.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=573060 {ECO:0000313|EMBL:EER61380.1, ECO:0000313|Proteomes:UP000003856};
RN   [1] {ECO:0000313|EMBL:EER61380.1, ECO:0000313|Proteomes:UP000003856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2AN {ECO:0000313|EMBL:EER61380.1,
RC   ECO:0000313|Proteomes:UP000003856};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA   Picardal F., Roden E., Emerson D.;
RT   "The draft genome of Acidovorax delafieldii 2AN.";
RL   Submitted (MAY-2009) 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:0000256|HAMAP-Rule:MF_00679}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00679,
CC       ECO:0000256|RuleBase:RU003322}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EER61380.1}.
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DR   EMBL; ACQT01000018; EER61380.1; -; Genomic_DNA.
DR   RefSeq; WP_005794100.1; NZ_ACQT01000018.1.
DR   AlphaFoldDB; C5T2B3; -.
DR   PATRIC; fig|573060.9.peg.4134; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000003856; Unassembled WGS sequence.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 3.30.420.40; -; 2.
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   NCBIfam; TIGR01991; HscA; 1.
DR   PANTHER; PTHR19375:SF176; CHAPERONE PROTEIN HSCA; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00679};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00679};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00679}; Oxidoreductase {ECO:0000313|EMBL:EER61380.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003856}.
SQ   SEQUENCE   623 AA;  65790 MW;  BFE44FD6089EF938 CRC64;
     MALLQISEPG QSPDPHQRRI AVGIDLGTTH SLVAAVRNGV AECLPDAQGR VLLPSVVRYL
     AQGGRQIGYE AVEAQSSDAR NTIASAKRFM GRGLQDVAQA GQLPYEFVQN PAQGVGGMVG
     LVTAAGVKSP VEISAEILAT LRYRAEDTFN DDLYGAVITV PAYFDDAQRQ ATKDAAQLAG
     IRLLRLINEP TAAAIAYGLD NASEGVYAVY DLGGGTFDIS VLRLTQGVFE VIATGGDSAL
     GGDDYDAALA NWVLKQQGRT AETPADKAAI RMAARACKEA LTASEIVAFT ADMAGGRLHF
     EVKRSDFDAA TADLTARSMA AVRRVLRDAK LSRDDVQGVV MVGGSTRMPQ VQRAVAEFFG
     KEPLTNLNPD EVVALGAAIQ ANQLAGNNTA GDLLLLDVIP LSLGIETMGG LVERIVGRNE
     TIPTAKAQDF TTYKDGQTAL AIHVVQGERD LVQDCRSLAR FELRGIPPIA AGAARIRVTF
     TVDADGLLSV SAREQGSGVE ARIDVKPSYG LSDDQIARML QDGFATAAQD MRTRAVVEAR
     VDADRMLMAT QSALDADGEV LEPSERVAIE VLMAALSAQR DADDAAAIEA ATQALAKGTE
     AFAAQRMNRG IREALAGKNV QAL
//
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