HSCA_SALPB
ID HSCA_SALPB Reviewed; 616 AA.
AC A9N1X9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=SPAB_00394;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000886; ABX65829.1; -; Genomic_DNA.
DR RefSeq; WP_001196673.1; NC_010102.1.
DR AlphaFoldDB; A9N1X9; -.
DR SMR; A9N1X9; -.
DR KEGG; spq:SPAB_00394; -.
DR PATRIC; fig|1016998.12.peg.372; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
DR BioCyc; SENT1016998:SPAB_RS01620-MON; -.
DR Proteomes; UP000008556; 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_1000082986"
SQ SEQUENCE 616 AA; 65637 MW; 0782FE2202151945 CRC64;
MALLQISEPG LSAAPHQRRL AAGIDLGTTN SLVATVRSGQ AETLPDHEGR HLLPSVVHYQ
QQGHTVGYAA RDNAAQDTTN 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 SYGLTDGEIA SMIKDSMSFA EQDVKARMLA EQKVEAARVL
ESLTGALTAD AALLSAAERQ CIDDAAAHLS AVAQGDDVDA IEQAIKNVDK QTQEFAARRM
DQSVRRALKG HSVDEV
