ID   HSCA_PASMU              Reviewed;         620 AA.
AC   Q9CNV2;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=PM0322;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004439; AAK02406.1; -; Genomic_DNA.
DR   RefSeq; WP_010906587.1; NC_002663.1.
DR   AlphaFoldDB; Q9CNV2; -.
DR   SMR; Q9CNV2; -.
DR   STRING; 747.DR93_1096; -.
DR   EnsemblBacteria; AAK02406; AAK02406; PM0322.
DR   KEGG; pmu:PM0322; -.
DR   PATRIC; fig|272843.6.peg.335; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000000809; 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_0000078636"
SQ   SEQUENCE   620 AA;  66786 MW;  8640F721F2A5DAF3 CRC64;
     MALLQIAEPG QSASPHQHKL AVGIDLGTTN SLIATVRSGQ VDILLDEKER PLLPSVVHFE
     QDNVIVGYEA AELASQSPQN TIVSVKRLIG RSLADVQQRY PSLPYQFEAS ENGLPLIRTS
     KGTLSPVEIS AEILKKLTAL AEKRLAGELS GAVITVPAYF DDAQRQSTKD AAKLAGINVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SKGVFEVLAT GGDTALGGDD
     FDHQLMDWIV AQSGIAPQNA QQQRQLTELA TQIKIALTDK LETSISYQGW QGNISREQFN
     QLIQGLVKRS LLACRRALKD ADVSADEVCE VVMVGGSTRV PFVREQVAAF FQKEPLTSID
     PDKVVALGAG IQADILVGNK PDADMLLLDV IPLSLGIETM GGLVEKIIPR NTTIPVARAQ
     EFTTFKDGQT AMSVHVVQGE REMVADCRSL ARFSLRGIPA MAAGAAHVRV TYQVDADGLL
     SVTAMEKSTG VQSSIQVKPS YGLSDDEITN MLKASMLNAK EDIQARLLAE QRVEAQRVLE
     SVGSALSADQ DLLNDEELSA VKNAIISLQR LQKEGDTQEI KQGIKQLDLA TQEFASRRMD
     KSIRQALAGK AIDDVMKNAK