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HSCA_RICFE
ID   HSCA_RICFE              Reviewed;         637 AA.
AC   Q4UKL3;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Chaperone protein HscA homolog;
GN   Name=hscA; OrderedLocusNames=RF_1063;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; CP000053; AAY61914.1; -; Genomic_DNA.
DR   RefSeq; WP_011271375.1; NC_007109.1.
DR   AlphaFoldDB; Q4UKL3; -.
DR   SMR; Q4UKL3; -.
DR   STRING; 315456.RF_1063; -.
DR   EnsemblBacteria; AAY61914; AAY61914; RF_1063.
DR   KEGG; rfe:RF_1063; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; IRVEVTF; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008548; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 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; IPR022437; RPE3.
DR   PANTHER; PTHR19375; PTHR19375; 2.
DR   Pfam; PF00012; HSP70; 2.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR03775; RPE3; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Stress response.
FT   CHAIN           1..637
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_0000288745"
FT   REGION          335..376
FT                   /note="Insert"
SQ   SEQUENCE   637 AA;  70859 MW;  83BD2FC0106D2F9D CRC64;
     MQIIEITEPE QADFKQERQI AVGIDFGTTN SLIAIATNRK VKVIKSRDDK ELIPTTIDFT
     NENFIIGNNK GLRSIKRLFG KTLKEILNTP ALFSLIKDYL EANSSELKLN FANKQLRISE
     IAAEVFIYLK NQAEEQLKTN ITKAVITVPA HFNDAARGEV MLAAKIAGFE VLRLIAEPTA
     AAYAYGLNKN QKGCYLVYDL GGGTFDVSIL NIQEGIFQVI ATNGDNMLGG DDIDVVITQY
     LCNKFDLPNS VDTLQLAKKA KETLTYKDSF NNDNISINKQ TLEQLILPLV ERTINIAKEC
     LEQAGNPKID GIILVGGATR TPLIKTELSK AFKVQHISKR FRQDEFKGEP AGRIKIREHR
     QVLQNSLVSN FMEYAVDILS DIDPDKAVVW GAALQAENLT APHTNSLLID VVPLSLGVEL
     YGGIVEKIIM RNTPIPISVV KEFTTYADNQ TGIQFHILQG EREMAVDCRS LARFELKGLP
     PMKAGNIRAE VTFAIDADGI LSVSAYEKIS NTSHTIEVKP NHGIDKTEID IMLENAYKNA
     KIDYTTRLLQ EAIIEAEALI FSIERAIAEL TALLSESEIS IINSLLDNIK EAAHARDRIL
     INNSIKEFKS KIKKSMNTKL NIIINDLLKG KNINQTK
 
 
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