HSCA_RICAE
ID HSCA_RICAE Reviewed; 595 AA.
AC C3PMP2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=RAF_ORF0245;
OS Rickettsia africae (strain ESF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=347255;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ESF-5;
RX PubMed=19379498; DOI=10.1186/1471-2164-10-166;
RA Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B.,
RA Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.;
RT "Analysis of the Rickettsia africae genome reveals that virulence
RT acquisition in Rickettsia species may be explained by genome reduction.";
RL BMC Genomics 10:166-166(2009).
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; CP001612; ACP53202.1; -; Genomic_DNA.
DR RefSeq; WP_012719465.1; NC_012633.1.
DR AlphaFoldDB; C3PMP2; -.
DR SMR; C3PMP2; -.
DR EnsemblBacteria; ACP53202; ACP53202; RAF_ORF0245.
DR KEGG; raf:RAF_ORF0245; -.
DR HOGENOM; CLU_005965_2_4_5; -.
DR OMA; IRVEVTF; -.
DR Proteomes; UP000002305; 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 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; 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 PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Stress response.
FT CHAIN 1..595
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000212532"
SQ SEQUENCE 595 AA; 65967 MW; 30DF858A47FB2918 CRC64;
MQIIEIREPE QADFKQERQI AVGIDFGTTN SLIAIAANRQ VKVIKSIDDK ELIPTTIDFT
SNNFTIGNNK GLRSIKRLFG KTLKEILNTP ALFSLVKDYL DVNSSELKLN FANKQLRVPE
IAAEIFIYLK NQAEEQLKTN LTKAVITVPA HFNDAARGEV MLAAKIAGFE VLRLIAEPTA
AAYAYGLNKN QKGCYLVYDL GGGTFDVSIL NIQEGIFQVI ATNGDNMLGG NDIDVVITQY
LCNKFDLPNS IDTLQLAKKA KETLTYKDSF NNDNVSINKQ TLEQLILPLV ERTINIAQEC
LEQAGNPNID GVILVGGATR IPLIKDELYK AFKIDILSDI DPDKAVVWGA ALQAENLIAP
HTNSLLIDVA PLSLGMELYG GIVEKIIMHN TPIPISVVKE FTTYVDNQTG IQFHILQGER
EMAADCRSLA RFELKGLPPM KAGYIRAEVT FSIDADGILS VSAYEKISNT SHAIEVKPNH
GIDKTEIDIM LENAYKNAKI DYTTRLLQEA VIEAEALIFS IERAIAELTT LSSESEISII
NSLLDNIKEA VHARDWILIN NSIKEFKSKI KKSIDTKFNI IINDLLKGKN INQIK