ID A0A0S9NDP6_9BURK Unreviewed; 623 AA.
AC A0A0S9NDP6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000256|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679};
GN ORFNames=ASF44_07685 {ECO:0000313|EMBL:KQP43423.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP43423.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP43423.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP43423.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP43423.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP43423.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQP43423.1}.
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DR EMBL; LMNA01000012; KQP43423.1; -; Genomic_DNA.
DR RefSeq; WP_056900239.1; NZ_LMNA01000012.1.
DR AlphaFoldDB; A0A0S9NDP6; -.
DR STRING; 1736318.ASF44_07685; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000051759; 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: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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00679}; Chaperone {ECO:0000256|HAMAP-Rule:MF_00679};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00679}; Reference proteome {ECO:0000313|Proteomes:UP000051759}.
SQ SEQUENCE 623 AA; 65079 MW; D45E8C874DF0833F CRC64;
MALLQISEPG FSPDPHQRRI AVGIDLGTTH SLVAAVRNGV AECLPDAQGR VILPSVVRYL
APSAGGSGRQ IGHEALAAQT TDPENTIASV KRLMGRGPAD VAAAELPYRL VATEGAGMLR
IETAAGPKTP VEISAEILAT LRFRAEDSFA DDLHGAVITV PAYFDDAQRQ ATKDAAQLAG
LHVLRLINEP TAAAIAYGLD NASEGIYAVY DLGGGTFDIS ILRLSRGVFE VVAAGGDSAL
GGDDYDHALA GWAQQASGLQ AEGAQQQVAL RRAARAAKER LTDDDRAALR VQLGDTELAV
DVARADFEAS TAALTARTMA AVRKALRDAK LTPADVQGTV LVGGATRMPQ VRRAVEAFFG
KPPLTNLNPD EVVALGAAIQ ADQLAGNSGA ADLLLLDVIP LSLGIETMGG LVERIVPRNQ
TIPTAMAQDF TTYQDGQTAL ALHVVQGERD LVADCRSLAR FVLRGIPPMA AGAARIRVTF
TVDADGLLTV SAREQGSGVE ASVDVKPSYG LSDDEIARML QDSFSTAGQD MQARALVEAR
VELDRMLLAT RSALDADGDL LPAPERAAID ALVASAEQAR AADQLQPMTA ATEGLAKGTE
AFAALRMNAG IRNALSGKNI ESV
//
