HSCA_SHEWM
ID HSCA_SHEWM Reviewed; 620 AA.
AC B1KNI7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Swoo_1780;
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-2008) 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; CP000961; ACA86064.1; -; Genomic_DNA.
DR RefSeq; WP_012324410.1; NC_010506.1.
DR AlphaFoldDB; B1KNI7; -.
DR SMR; B1KNI7; -.
DR STRING; 392500.Swoo_1780; -.
DR PRIDE; B1KNI7; -.
DR EnsemblBacteria; ACA86064; ACA86064; Swoo_1780.
DR KEGG; swd:Swoo_1780; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002168; 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; Reference proteome.
FT CHAIN 1..620
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000131695"
SQ SEQUENCE 620 AA; 66245 MW; 50C59E6C7D13B910 CRC64;
MALLQIAEPG QSAAPHQHRL AVGIDLGTTN SLVAAVRSGV ANTLPDDKSH HSLPSVVRYT
QEGVEVGVDA EANSAKDPQN TIISVKRFMG RSLSDIRSGV QDLPYQLETS ENGLPVFVTE
QGKVNPIQVS AEILKPLVSR AEKTLGGELE GVVITVPAYF DDAQRQGTKD AAGLLGVKVL
RLLNEPTAAA IAYGLDSGQE GVIAIYDLGG GTFDISILRL HKGVFEVLAT GGDSALGGDD
FDHLLYQHLL NQWQLASPSA TLSRRLLIES RRVKEALTDN IQVTASIKLD DGTELTHDVA
KATFDDLISS LVKKTVSSCR RALRDAGVTN DEVLETVMVG GSTRVPLVRE LVDKFFGKEP
LTSIDPDRVV AIGAAIQADI LVGNKPESDL LLLDVLPLSL GIETMGGLVE KIVSRNTTIP
VAKAQEFTTF KDGQTAMAFH VVQGERELVD DCRSLARFTL KGIPPLAAGA AHIRVTFQVD
ADGLLSVTAM EKSTGVQSSI QVKPSFGLTD EEIGTMLKDS MANAKEDITR RMLAEQKVEA
ARVLETLSAA LQKDAVLLTE SERSDIEQAM ASLAQISSQD DADAIEKAIE ALDASTQDFA
AKRMDNSIKL ALKGQSVDSI
