HSCA_JANMA
ID HSCA_JANMA Reviewed; 620 AA.
AC A6SXE9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=mma_1256;
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille;
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR89750.1; -; Genomic_DNA.
DR RefSeq; WP_012079113.1; NC_009659.1.
DR AlphaFoldDB; A6SXE9; -.
DR SMR; A6SXE9; -.
DR STRING; 375286.mma_1256; -.
DR EnsemblBacteria; ABR89750; ABR89750; mma_1256.
DR KEGG; mms:mma_1256; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_4; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR BioCyc; JSP375286:MMA_RS06540-MON; -.
DR Proteomes; UP000006388; 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; Reference proteome.
FT CHAIN 1..620
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044863"
SQ SEQUENCE 620 AA; 66073 MW; 18ED05BFB759336F CRC64;
MALLQIAEPG MSTAPHQHRL AVGIDLGTTN SLVATVRNSI PEVLTDEEGR ALLPSVVHYM
KNGHAQIGYK ALAAQNTDPK NTIASVKRFM GRGLKDIAYV ENLPYDFLDT PGMVQLKTVA
GVKSPVEISA EILATLRQQA EDALGDELVG AVITVPAYFD DAQRQATKDA AKLAGLNVLR
LLNEPTAAAI AYGLDNGSEG VFAVYDLGGG TFDVSILKLT KGVFEVLSTG GDSALGGDDF
DHRLLCWIIE QAKLSPLSDE DLSVLMVKSR EAKELLSTKA ETHIDAALGS GEEVHLTVTA
ADFVKMTQHL VAKTITPTKK ALRDADLTVD DVDGVVMVGG ATRMPHIRKA VGEFFQATPL
ANIDPDKVVA LGAAVQANLL AGNRAAGDDW LLLDVIPLSL GIETMGGLVE KVIPRNSTIP
CARAQEFTTF KDGQTAMAIH IVQGERELVS DCRSLARFEL RGIPPMAAGA ARIRVTYQVD
ADGLLSVSAR ELRSGVEASI SVKPSYGLAD DQIAQMLQDS FKSADVDMAL RALREEQVEA
ERIVLATQSA LDADGALLTD DERNAVTSLL AAVQQSSKGD DHHAIKAAVE ALAQGTEEFA
ARRMDRSVRT ALSGKKLDEI
