(data stored in SCRATCH zone)

SWISSPROT: HSCA_SALAR

ID   HSCA_SALAR              Reviewed;         616 AA.
AC   A9MHJ8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   11-DEC-2019, entry version 69.
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=SARI_00337;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-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. 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}.
DR   EMBL; CP000880; ABX20276.1; -; Genomic_DNA.
DR   RefSeq; WP_001196665.1; NC_010067.1.
DR   SMR; A9MHJ8; -.
DR   EnsemblBacteria; ABX20276; ABX20276; SARI_00337.
DR   KEGG; ses:SARI_00337; -.
DR   eggNOG; ENOG4105C9I; Bacteria.
DR   eggNOG; COG0443; LUCA.
DR   HOGENOM; HOG000228136; -.
DR   KO; K04044; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   BioCyc; SENT882884:G1GAH-328-MONOMER; -.
DR   Proteomes; UP000002084; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
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; 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   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;
DR   PRODOM; A9MHJ8.
DR   SWISS-2DPAGE; A9MHJ8.
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..616
FT                   /note="Chaperone protein HscA"
FT                   /id="PRO_1000082985"
SQ   SEQUENCE   616 AA;  65687 MW;  0F672005CA0629EE CRC64;
     MALLQISEPG LSAAPHQRRL AAGIDLGTTN SLVATVRSGQ AETLPDHEGR HLLPSVVHYQ
     QQGHTVGYAA RDNAAQDTAN TISSVKRMMG RSLADIQSRY PHLPYRFQAS ENGLPMIETA
     AGLLNPVRVS ADILKALAAR ASESLSGELD GVVITVPAYF DDAQRQGTKD AARLAGLHVL
     RLLNEPTAAA IAYGLDSGKE GVIAVYDLGG GTFDISILRL SCGVFEVLAT GGDSALGGDD
     FDHLLADYIR EQAGIADRSD NRVQRELLDA AIAAKIALSD ADTVRVNVAG WQGEITREQF
     NDLIAALVKR TLLACRRALK DADVDPQEVL EVVMVGGSTR VPLVRERVGE FFGRTPLTAI
     DPDKVVAIGA AIQADILVGN KPDSEMLLLD VIPLSLGLET MGGLVEKVIP RNTTIPVARA
     QDFTTFKDGQ TAMSIHVMQG ERELAQDCRS LARFALRGIP ALPAGGAHIR VTFQVDADGL
     LSVTAMEKST GIEASIQVKP SYGLTDSEIA SMIKDSMSFA EQDVKARMLA EQKVEAARVL
     ESLTGALTAD AALLSAAERQ CIDDAAAHLN AVAQGDDVDA IEQAIKNVDK QTQEFAARRM
     DQSVRRALKG HSVDEV
//

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