HSCA_SHESH
ID HSCA_SHESH Reviewed; 620 AA.
AC A8FXA1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Ssed_2867;
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=425104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB3;
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., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella sediminis HAW-EB3.";
RL Submitted (AUG-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; CP000821; ABV37474.1; -; Genomic_DNA.
DR RefSeq; WP_012143204.1; NC_009831.1.
DR AlphaFoldDB; A8FXA1; -.
DR SMR; A8FXA1; -.
DR STRING; 425104.Ssed_2867; -.
DR EnsemblBacteria; ABV37474; ABV37474; Ssed_2867.
DR KEGG; sse:Ssed_2867; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002015; 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.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding.
FT CHAIN 1..620
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000082990"
SQ SEQUENCE 620 AA; 65892 MW; AD7B2BAF78E33D7D CRC64;
MALLQIAEPG QTAAPHQHRL AVGIDLGTTN SLVAAVRSGV ADTLPDENAR HSLPSIVRYT
DTGIEAGFEA EAHSAKDPQN TIVSVKRFMG RSLADIQSGI QDLPYRFQAS ENGLPLFATE
QGTVNPVQIS SEILKPLISR AESTLGGDLE GIVITVPAYF DDAQRQGTKD AAALLGVKVL
RLLNEPTAAA IAYGLDSGQE GVIAIYDLGG GTFDISILRL NKGVFEVLAT GGDSALGGDD
FDHLLHHHLL QEWQIDAPSA SVSRQLLIES RRVKEVLTDE SEVTATLLLD DGTTLTHVVT
KSLFDSLITS LVKKTVASCR RALRDAGIKA DEVLETVLVG GSTRVPLVRE LVEGFFGKAP
LTSIDPDRVV AIGAAIQADI LVGNKPESDL LLLDVLPLSL GIETMGGLVE KVVSRNTTIP
VAKAQEFTTF KDGQTAMAFH VVQGERELVD DCRSLARFTL KGIPPLAAGA AHIRVTFQVD
ADGLLSVTAM EKSTGVQSSI QVKPSFGLTD EEIGSMLKDS MANAKDDIAR RMLAEQQVEA
ARVLETLSAA LAKDGELLTA DERNAIEQSM AVLVEVGGQD DADAIEKAIE ALDASTQDFA
AKRMDNSIKL ALKGQSVDSI
