HSCA_SALSV
ID HSCA_SALSV Reviewed; 616 AA.
AC B4TRB1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Chaperone protein HscA {ECO:0000255|HAMAP-Rule:MF_00679};
DE AltName: Full=Hsc66 {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=SeSA_A2779;
OS Salmonella schwarzengrund (strain CVM19633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=439843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CVM19633;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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. Involved in the maturation of IscU.
CC {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; CP001127; ACF91003.1; -; Genomic_DNA.
DR RefSeq; WP_001196652.1; NC_011094.1.
DR AlphaFoldDB; B4TRB1; -.
DR SMR; B4TRB1; -.
DR EnsemblBacteria; ACF91003; ACF91003; SeSA_A2779.
DR KEGG; sew:SeSA_A2779; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
DR Proteomes; UP000001865; 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.
FT CHAIN 1..616
FT /note="Chaperone protein HscA"
FT /id="PRO_1000131693"
SQ SEQUENCE 616 AA; 65637 MW; 715FD111CB605851 CRC64;
MALLQISEPG LSAAPHQRRL AAGIDLGTTN SLVATVRSGQ AETLPDHEGR HLLPSVVHYQ
QQGHTVGYAA RDNAAQDTAN TISSVKRMMG RSLADIQARY PHLPYRFKAS VNGLPMIDTA
AGLLNPVRVS ADILKALAAR ASESLSGELD GVVITVPAYF DDAQRQGTKD AARLAGLHVL
RLLNEPTAAA IAYGLDSGKE GVIAVYDLGG GTFDISILRL SRGVFEVLAT GGDSALGGDD
FDHLLADYIR EQAGIADRSD NRVQRELLDA AIAAKIALSD ADTVRVNVAG WQGEITREQF
NDLISALVKR TLLACRRALK DAGVDPQDVL EVVMVGGSTR VPLVRERVGE FFGRTPLTAI
DPDKVVAIGA AIQADILVGN KPDSEMLLLD VIPLSLGLET MGGLVEKVIP RNTTIPVARA
QDFTTFKDGQ TAMSIHVMQG ERELVQDCRS LARFALRGIP PLPAGGAHIR VTFQVDADGL
LSVTAMEKST GVEASIQVKP SYGLTDSEIA SMIKDSMSFA EQDVKARMLA EQKVEAARVL
ESLTGALTAD AALLSAAERQ CIDDAAAHLS AVAQGDDVDA IEQAIKNVDK QTQEFAARRM
DQSVRRALKG HSVDEV