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 27-MAR-2024, entry version 101.
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; Pseudomonadota; 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 KEGG; ppr:PBPRA0754; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
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; 3.30.420.40; -; 2.
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 NCBIfam; TIGR01991; HscA; 1.
DR PANTHER; PTHR19375:SF176; CHAPERONE PROTEIN HSCA; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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
//
