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