ID   HSCA_HERAR              Reviewed;         620 AA.
AC   A4G782;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=HEAR2235;
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1;
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.-C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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; CU207211; CAL62369.1; -; Genomic_DNA.
DR   RefSeq; WP_011871638.1; NC_009138.1.
DR   AlphaFoldDB; A4G782; -.
DR   SMR; A4G782; -.
DR   STRING; 204773.HEAR2235; -.
DR   PRIDE; A4G782; -.
DR   EnsemblBacteria; CAL62369; CAL62369; HEAR2235.
DR   KEGG; har:HEAR2235; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_4; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000006697; 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..620
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044862"
SQ   SEQUENCE   620 AA;  65884 MW;  D2A660B9CF1FA1CE CRC64;
     MALLQIAEPG MSTAPHQHRL AVGIDLGTTN SLVATVRNSI PEILTDEEGR SLLPSVVHYL
     KNGSAHIGYK AQAAQNTDPK NTIVSVKRFM GRGLKDIAYA ENLPYDFLDT PGMVQLKTVA
     GVKSPVEVSA EILATLRQQA EDALGDDLVG AVITVPAYFD DAQRQATKDA AKLAGLNVLR
     LLNEPTAAAI AYGLDNGSEG VFAVYDLGGG TFDVSILKLT KGVFEVLSTG GDSALGGDDF
     DHRLFCWIIE QAGLAPLSEI DTSVLMVKAR EAKELLSSKS ETLIDAVLTS GEEVHVTVTA
     ADFIQMTQHL VTKTITPTKK ALRDAGLSVD DVDGVVMVGG ATRMPHIRKA VGDFFQSTPL
     ANIDPDKVVA LGAAVQANLL AGNRAAGDDW LLLDVIPLSL GIETMGGLVE KVIPRNSTIP
     CARAQEFTTF KDGQTALAVH IVQGERELVT DCRSLAKFEL RGIPPMAAGA ARIRVTYQVD
     ADGLLSVSAR ELRSGVEASI SVKPSYGLAD DQIAQMLQDS FKSADVDMAA RALREEQVEA
     ERIVLATQSA LDADASLLSD NEREDIVALL DSVRQAGSGT DHLAIKAAVD ALAHGTEEFA
     ARRMDRSVRS ALSGKKLDEI