ID   HSCA_PSEMY              Reviewed;         621 AA.
AC   A4XY39;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Pmen_3507;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) 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; CP000680; ABP86255.1; -; Genomic_DNA.
DR   RefSeq; WP_012019506.1; NC_009439.1.
DR   AlphaFoldDB; A4XY39; -.
DR   SMR; A4XY39; -.
DR   STRING; 399739.Pmen_3507; -.
DR   EnsemblBacteria; ABP86255; ABP86255; Pmen_3507.
DR   KEGG; pmy:Pmen_3507; -.
DR   PATRIC; fig|399739.8.peg.3553; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
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..621
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044874"
SQ   SEQUENCE   621 AA;  66272 MW;  7883B63BC8964DA7 CRC64;
     MALLQIAEPG QSPQPHQRRL AVGIDLGTTN SLVAAVRSGL AEPLADGDGK VILPSAVRYH
     PQHVEVGESA KLAAASDPFN TVLSVKRLMG RGIADVHQLG EQLPYRFAAG ESHMPFIETV
     QGAKSPVEVS AEILKTLRLR AEQTLGGELV GAVITVPAYF DDAQRQATKD AARLAGLNVL
     RLLNEPTAAA VAYGLDQKAE GVVAIYDLGG GTFDISILRL TGGVFEVLAT GGDSALGGDD
     FDHAIADWII QQAGISSDLD PSAQRSLLQA ACAAKEGLTN ADHVELSHGD WRGTLSREQF
     EALIEPMVAR SLKACRRALR DSGVELEEVS AVVMVGGSTR VPRVREAVGE LFGRTPLTNI
     DPDQVVAIGA AIQADTLAGN QRGEGEELLL LDVIPLSLGL ETMGGLMEKL IPRNTTIPVA
     RAQDFTTYKD GQTAMMIHVL QGERELIADC RSLARFELRG IPPMVAGAAK IRVTFQVDAD
     GLLSVAAREL GSGVEASIQV KPSYGLTDGE IARMLQDSFQ NAGDDKAARA LREQQVDAQR
     LIEAVEAALQ ADGERLLDAE EREVIELQVQ ELRDLLASND GLAIERQSKR LSQVTDAFAA
     RRLDSTVKAA LAGRNLNEIE E