ID A0A0E3V128_9BURK Unreviewed; 621 AA.
AC A0A0E3V128;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000256|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679};
GN ORFNames=CL55_00014560 {ECO:0000313|EMBL:AKD25789.1};
OS Polynucleobacter duraquae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=1835254 {ECO:0000313|EMBL:AKD25789.1, ECO:0000313|Proteomes:UP000061135};
RN [1] {ECO:0000313|EMBL:AKD25789.1, ECO:0000313|Proteomes:UP000061135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-MoK4 {ECO:0000313|EMBL:AKD25789.1,
RC ECO:0000313|Proteomes:UP000061135};
RA Hahn M.W.;
RT "Genome of Polynucleobacter strain MWH-MoK4.";
RL Submitted (MAR-2014) 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}.
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DR EMBL; CP007501; AKD25789.1; -; Genomic_DNA.
DR RefSeq; WP_046330503.1; NZ_CP007501.1.
DR AlphaFoldDB; A0A0E3V128; -.
DR STRING; 1835254.CL55_00014560; -.
DR KEGG; pdq:CL55_00014560; -.
DR PATRIC; fig|576611.7.peg.1481; -.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000061135; 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; 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}; Chaperone {ECO:0000256|HAMAP-Rule:MF_00679};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00679}.
SQ SEQUENCE 621 AA; 66817 MW; 9865DF00EFA199B4 CRC64;
MALLQISEPG KSLAPHQRRI AVGIDLGTTN SLVAIVRDAL PQVLPDSEGR ELLPSVVRYL
PNGRTQAGFE AAESIVSDPK NTIVSVKRFM GRGIVDVENI ESTPYDFVDE PGMLKIKTVA
GDKSPIEVSA EILARLRQLA EDSVNDDIVG AVITVPAYFD DAQRQATKDA AKLAGIEVLR
LLNEPTAAAI AYGLDNASEG IYAVYDLGGG TFDISILRMS RGVFEVLSTG GDSALGGDDF
DHRLYCWVIE QAKLPPLSIQ DHRKLLLSCK HAKEQLSHNP LARVHEALAD GTVINVGVSQ
AQFFEITQNL INKTLVAVKK ALRDAGLKTD EVKGVVMVGG ATRMPQVQRA VGELFGTKPL
NNLNPDQVVA LGAAMQADLL AGNQSKDDEW LLLDVIPLSL GIETMGGLVE KIIPRNTPIP
VARAQDFTTF KDGQTALAIQ VVQGERELAQ DCRSLGKFEL RGIPPMAAGA ARIRVTYQVD
ADGLLSVSAM EQGSGVQASI DIKPSYGLTD AEIARMLQDG FASAKIDLLS RSLREEQVNA
QRLLDAVQTA LDSDRGLLNS QEQAEVDQEM AVLQKLLTEE ADSAILRKAV DHAAKATDEF
AQKRMNASIK RALAGKNVAE I
//
