ID   HSCA_BORPA              Reviewed;         620 AA.
AC   Q7W8U9;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=BPP2032;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE37332.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX640429; CAE37332.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_010928328.1; NC_002928.3.
DR   AlphaFoldDB; Q7W8U9; -.
DR   SMR; Q7W8U9; -.
DR   EnsemblBacteria; CAE37332; CAE37332; BPP2032.
DR   KEGG; bpa:BPP2032; -.
DR   HOGENOM; CLU_005965_2_3_4; -.
DR   Proteomes; UP000001421; 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.
FT   CHAIN           1..620
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078617"
SQ   SEQUENCE   620 AA;  65310 MW;  99030B7F17B26DA9 CRC64;
     MALLQISEPG DSPAPHQRKL AVGIDLGTTN SLVAAVRSSV PEVLADAQGQ VLLPSAVRYL
     DGGAVRIGRE ALLEQARDPL NTIVSVKRFM GRSAADALAS GAPYEFVDAP GMVRLRTVQG
     DLSPVEVSAQ ILAVLRQRAE DVLGDDLVGA VITVPAYFDD AQRQATRDAA RLAGLNVLRL
     LNEPTAAAIA YGLDQAAEGI YAVYDLGGGT FDISILRLTQ GVFEVIATGG DTALGGDDFD
     SAIVAHACAG EDVAALPVAD RRALLVAARA AREALTDQAQ APFEVTLRDG RAIQATLTRA
     QFEQLAEPLV GRTLESARRA LRDAGLAVGD VRGVVMVGGA TRMPVVRQQV GALFGTEPLT
     NLDPDQVVAL GAALQANLLA GNRPPGEDWL LLDVIPLSLG LETMGGLVER IIPRNSTIPV
     ARAQEFTTFK DGQTAMSVHV VQGERDLVSD CRSLARFELR GIPPMVAGAA RIRVTFQVDA
     DGLLSVTARE QSTGVEAAVA VKPSYGLSDD EIARMLADSV TQADSDARAR MLREQQVEAR
     QLVESVGAAL AADGDLLDPA ERATVDQRLQ AAAQAQSLDD VEAVRAAVQA LSDATEEFAA
     RRMDRSIRAA LAGRKLDELA