ID   HSCA_ACTPJ              Reviewed;         617 AA.
AC   B0BPK8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=APJL_0935;
OS   Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=434271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL03;
RX   PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA   Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA   Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA   Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA   Zhao G.-P., Chen H.;
RT   "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT   serotype 3 prevalent in China.";
RL   PLoS ONE 3:E1450-E1450(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; CP000687; ABY69493.1; -; Genomic_DNA.
DR   RefSeq; WP_009874858.1; NC_010278.1.
DR   AlphaFoldDB; B0BPK8; -.
DR   SMR; B0BPK8; -.
DR   EnsemblBacteria; ABY69493; ABY69493; APJL_0935.
DR   KEGG; apj:APJL_0935; -.
DR   PATRIC; fig|416269.6.peg.966; -.
DR   HOGENOM; CLU_005965_2_3_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008547; 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_1000131663"
SQ   SEQUENCE   617 AA;  66704 MW;  BEDEA547965946DC CRC64;
     MALLQIAEPG QTAAPHQHRL AVGIDLGTTN SLVASVRSGQ TQVLLDDQER ALVPSVVHYG
     EQQKTVGIEA FAQASLDPQN TVISAKRLIG RSLADVQTRY PDLPYQFIAS DNGLPLIQTK
     QGNKSPVEVS ADILSHLNRF AEQRLGGELS GVVITVPAYF DDAQRQSTKD AARLAGLNVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SRGVFEVLAT GGDTALGGDD
     FDHLLADWIA QQANYQPQNA NEQRELLTLA TQTKVALSQA VETEVKFANW QGTVSREQFN
     ELIQLLVKRS LMTCRRALKD AGVEGEEIRE VVMVGGSTRV PFVREQVGEF FGKQPLTSID
     PDKVVALGAA IQADILVGNK PDSEMLLLDV VPLSLGIETM GGLVEKIIPR NMTIPVARAQ
     EFTTAKDGQT AMSVHVLQGE RELVEDCRSL GRFTLRGIPP MVAGAATIRV TYQVDADGLL
     SVTAMEKSTK VQASIQIKPS YGLTDEEVTQ MIKSSMTNAK EDMEARQLAE QRVEADRTID
     TVISALQQDG AEVLSVEEFK LIEAEIAKLI QLKQGTDRQA IAQGVKDLDL ATQTFAAKRM
     NLSIQKALAG KAVDEII