ID   HSCA_POLNS              Reviewed;         621 AA.
AC   B1XTR3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Pnec_0473;
OS   Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=452638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STIR1;
RX   PubMed=24167248; DOI=10.1073/pnas.1316687110;
RA   Boscaro V., Felletti M., Vannini C., Ackerman M.S., Chain P.S.,
RA   Malfatti S., Vergez L.M., Shin M., Doak T.G., Lynch M., Petroni G.;
RT   "Polynucleobacter necessarius, a model for genome reduction in both free-
RT   living and symbiotic bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:18590-18595(2013).
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; CP001010; ACB43740.1; -; Genomic_DNA.
DR   RefSeq; WP_012357507.1; NC_010531.1.
DR   AlphaFoldDB; B1XTR3; -.
DR   SMR; B1XTR3; -.
DR   STRING; 452638.Pnec_0473; -.
DR   EnsemblBacteria; ACB43740; ACB43740; Pnec_0473.
DR   KEGG; pne:Pnec_0473; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
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.
FT   CHAIN           1..621
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000131682"
SQ   SEQUENCE   621 AA;  67003 MW;  FAA76F6AE21498ED CRC64;
     MALLQISEPG KSLAPHQRRI AVGIDLGTTN SLVAIVRDAL PKVLPDAQGR ELLPSVIRYL
     PNGRTQAGFE ALESVVIDPK NTIVSVKRFM GRGLLDVEHI ESAPYDFVDQ PGMLKLRTVA
     GDKSPIEVSA EILARLRQLA EDSVSDEIVG AVITVPAYFD DAQRQATKDA AKLAGIEVLR
     LLNEPTAAAI TYGLDNASEG VYAVYDLGGG TFDISILRMS RGVFEVLATG GDSALGGDDF
     DHRLYCWVIE QAKLPPLSIH DHRTLLQACK HAKEQLSHNP LARVHETLAD GTVVNVGISQ
     AQFFEITQNL VTKTLMTCKK ALRDAGLKAE DVKGVVMVGG STRMPNVQRA VAELFGTQPL
     NNLNPDQVVA LGAAMQADLL AGNQSKDDEW LLLDVIPLSL GIETMGGLVE KSIPRNTPIP
     VARAQDFTTF KDGQTALAIQ VVQGERELAQ DCRSLGRFEL RGIPAMAAGA ARIRVTFQVD
     ADGFLSVSAT EQGSGVKASI DIKPSYGLTD AEITRMLQDG FASAKEDLLS RSLREEQVNA
     QRLLDAVQTA LDSDRSLLNA EEQAAIDREM TTLQKILNEE TNSAVVRKAV DQAVKATDDF
     AQKRMNASIQ KALSGKNVTE I