ID   HSCA_ACTP7              Reviewed;         617 AA.
AC   B3GXS0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=APP7_0983;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) 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: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; CP001091; ACE61635.1; -; Genomic_DNA.
DR   RefSeq; WP_005617409.1; NC_010939.1.
DR   AlphaFoldDB; B3GXS0; -.
DR   SMR; B3GXS0; -.
DR   EnsemblBacteria; ACE61635; ACE61635; APP7_0983.
DR   KEGG; apa:APP7_0983; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   BioCyc; APLE537457:APP7_RS05000-MON; -.
DR   Proteomes; UP000001226; 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..617
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000131662"
SQ   SEQUENCE   617 AA;  66688 MW;  6AD7174D5B3F3AE9 CRC64;
     MALLQIAEPG QTAAPHQHRL AVGIDLGTTN SLVASVRSGQ TQVLLDDQER ALVPSVVHYG
     EQQKTVGIEA FTQASLDPQN TVISAKRLIG RSLADVQTRY PDLPYQFIAS DNGLPLIQTK
     QGNKSPVEVS ADILSHLNRF AEQRLGGELS GVVITVPAYF DDAQRQSTKD AARLAGLNVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SRGVFEVLAT GGDTALGGDD
     FDHLLADWIA QQANYKPQNA NEQRELLTLA TQTKVALSQA VETEVKFANW QGTVSREQFN
     ELIQPLVKRS LMTCRRALKD AGVEGEEIRE VVMVGGSTRV PFVREQVGEF FGKQPLTSID
     PDKVVALGAA IQADILVGNK PDSEMLLLDV VPLSLGIETM GGLVEKIIPR NTTIPVARAQ
     EFTTAKDGQT AMSVHVLQGE RELVEDCRSL GRFTLRGIPP MVAGAATIRV TYQVDADGLL
     SVTAMEKSTK VQASIQIKPS YGLTDEEVTQ MIKSSMTNAK EDMEARQLAE QRVEADRTID
     TVISALQQDG AEVLSVEEFK LIEAEIAKLI QLKQGTDRQA IAQGVKDLDL ATQTFAAKRM
     NLSIQKALAG KAVDEII