ID   HSCA_PHOPR              Reviewed;         617 AA.
AC   Q6LU58;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=PBPRA0754;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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; CR378665; CAG19167.1; -; Genomic_DNA.
DR   RefSeq; WP_011217509.1; NC_006370.1.
DR   AlphaFoldDB; Q6LU58; -.
DR   SMR; Q6LU58; -.
DR   STRING; 298386.PBPRA0754; -.
DR   PRIDE; Q6LU58; -.
DR   EnsemblBacteria; CAG19167; CAG19167; PBPRA0754.
DR   KEGG; ppr:PBPRA0754; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000593; Chromosome 1.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..617
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000078638"
SQ   SEQUENCE   617 AA;  66562 MW;  DBE7238D0597D016 CRC64;
     MALLQIAEPG QSAAPHQHRL AVGIDLGTTN SLVAAVRSGV PETLKDDKGR SILPSIVHYG
     EESLLVGHEA RELAQQDPSN TIFSVKRMMG RSLADIQQRY PHLPYQFEAS DNGLPQLMTP
     TGKVNPVQVS AEILKTLNAR AVATLGGDLE GVVITVPAYF DDAQRAGTKD AAKLANLNVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISVLRL SKGVFEVLAT GGDSALGGDD
     FDHLLADWIK EQAGYIGDLT AQQMRMVQDA ATDAKIALTD ADTAQIDVLN WQGIVTREQF
     NALIQPLVKK TLMSCRRAIK DSGIEISDTI ETVMVGGSTR VPLVREMVGN YFGKEPLTSI
     DPDKVVAIGA SIQADILVGN KPDSDMLLLD VIPLSLGIET MGGMIEKIIP RNTTIPVARA
     QEFTTFKDGQ TAMSVHVVQG EREMVSDCRS LARFTLRGIP AMTAGAAHIR VTYQVDADGL
     LSVTAMEKSS NVQSSIQVKP SYGLSDNEVA TMIRESMTHA QDDKDARTLA EQYVEADRVL
     EGLITALAID GDTLLSKEER ETLEGVMMEL VQLRKGTDYR SIEQGIKKTD KASQEFASRR
     MDKSIRQALA GQSIDEV