ID   HSCA_PSEA6              Reviewed;         622 AA.
AC   Q15WH0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Patl_1242;
OS   Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=342610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6c / ATCC BAA-1087;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA   Bartlett D., Higgins B.P., Richardson P.;
RT   "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL   Submitted (JUN-2006) 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; CP000388; ABG39768.1; -; Genomic_DNA.
DR   RefSeq; WP_011574096.1; NC_008228.1.
DR   AlphaFoldDB; Q15WH0; -.
DR   SMR; Q15WH0; -.
DR   STRING; 342610.Patl_1242; -.
DR   EnsemblBacteria; ABG39768; ABG39768; Patl_1242.
DR   KEGG; pat:Patl_1242; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001981; 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..622
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044868"
SQ   SEQUENCE   622 AA;  66702 MW;  1644BFD2899BA55D CRC64;
     MALLQIAEPG LSAAPHQRKL AVGIDLGTTN SLVATVRSGQ AETLGDNNNQ HLLPSVVSYT
     AEQVVVGEQA KHDASLDPAN TIVSVKRFLG RSLNDIRRSY PDLPYDFDES NPNSPLLNVT
     GRQVNPVEVS SEILTTLRLR AEQSLGEELS GAVVTVPAYF DDAQRQGTKD AAQLAGLKVL
     RLLNEPTAAA IAYGLDTAQE GVIAVYDLGG GTFDISILRL SKGVFEVLAT GGDSALGGDD
     FDHMIVKHFR QQLGLEGALS KRLHRVLLDK AKFAKESLSD NDTVTVDFAD DEQKLLSLSI
     SRETFQGLIA DLTKSTLRAC RRALKDAELE KDEVLEVVMV GGSTRVPYVR EQVGEFFGRT
     PLTSIDPDKV VAIGASIQAD ILVGNKPDGE MLLLDVLPLS LGLETMGGLV EKVIHRNTTI
     PVAKAQEFTT FKDGQTAMMI HVLQGERELV DDCRSLAKFT LHGIPPMAAG AAHIRVTFQV
     DADGLLNVMA MEKSSGVQAE IQVKPSYGLD ESQISDMLKA SMQNATGDMQ ARMLKEQQVE
     AARVHEALQA ALNADGAELL SAAEIGTIQA SLEVLDIAGK NDDIDAIKQA ISAADAASQI
     FAEKRMDHSI KKALAGHTVD SI