ID   HSCA_BORPD              Reviewed;         620 AA.
AC   A9IQZ6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Bpet2773;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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; AM902716; CAP43115.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IQZ6; -.
DR   SMR; A9IQZ6; -.
DR   STRING; 94624.Bpet2773; -.
DR   EnsemblBacteria; CAP43115; CAP43115; Bpet2773.
DR   KEGG; bpt:Bpet2773; -.
DR   eggNOG; COG0443; Bacteria.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000001225; 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_1000131665"
SQ   SEQUENCE   620 AA;  65618 MW;  130D479324BD6F7E CRC64;
     MALLQISEPG ESPAPHQRKL AVGIDLGTTN SLVAAVRSST PEVLRDAEGQ ALLPSAVRYC
     ADGKVVIGRQ ALAQQAADPF NTVVSVKRFM GRSLDEARAS GAPYEFVDAP GMVRLRTAQG
     ELSPVEVSAQ ILAVLRQRAE DVLGDDLVGA VITVPAYFDD AQRQATRDAA RLAGLNVLRL
     LNEPTAAAIA YGLDQAAEGT YAVYDLGGGT FDVSILRLTK GVFEVVATGG DTALGGDDFD
     WSISEFARAS LGDAPLAPAD RRTVLVAARA AREALSQASE APLRATLQDG RQLNLTLTQA
     QFEQLAEPLV RRTLDRARSA LRDAGLAVGD INGVVMVGGA TRMPVVRRAV GELFGTEPLV
     DLDPDQVVAL GAALQANLLA GNRLPGEDWL LLDVIPLSLG LETMGGLVER IIPRNSTIPV
     ARAQEFTTFK DGQGAMSVHV VQGERELVSD CRSLARFELR GIPPMVAGAA RIRVTFQVDA
     DGLLSVTARE QSTGVEAAVS VKPSYGLSDD EITRMLADSV AQADSDARAR MLREQQVEAR
     QLVESVRAAL AADGDLLDAD ERRVVDERLQ AAAAAQDADD ADAVRAAVQA LSAATEDFAA
     RRMDRGIRAA LAGRKLDEIA