HSCA_POLAQ
ID HSCA_POLAQ Reviewed; 621 AA.
AC A4SYY9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Pnuc_1489;
OS Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=312153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX PubMed=22675600; DOI=10.4056/sigs.2395367;
RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT "Complete genome sequence of Polynucleobacter necessarius subsp.
RT asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP34703.1; -; Genomic_DNA.
DR RefSeq; WP_011903326.1; NC_009379.1.
DR AlphaFoldDB; A4SYY9; -.
DR SMR; A4SYY9; -.
DR STRING; 312153.Pnuc_1489; -.
DR PRIDE; A4SYY9; -.
DR EnsemblBacteria; ABP34703; ABP34703; Pnuc_1489.
DR GeneID; 31481880; -.
DR KEGG; pnu:Pnuc_1489; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_3_4; -.
DR OMA; PDPHQRR; -.
DR Proteomes; UP000000231; 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..621
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000082983"
SQ SEQUENCE 621 AA; 66798 MW; 0706F8306C27F151 CRC64;
MALLQISEPG KSLAPHQRRI AVGIDLGTTN SLVAIVQDAL PKVLPDEQGR ELLPSVVRYL
PNGRTQAGFE ALESVVIDPK NTILSVKRFM GRGISDVENI ESAPYDFVDQ PGMLKLRTVA
GDKSPIEVSA EILARLRQLA EDSVNDDIVG AVITVPAYFD DAQRQATKDA AKLAGIEVLR
LLNEPTAAAI AYGLDNATEG VYAVYDLGGG TFDISILRMS KGVFEVLSTG GDSALGGDDF
DHRLYCWVIE QAKLPPLSIH DHRTLLQACK HAKELLSHNP LARVHETLAD GTVVNVGISQ
AQLFEITQNL VSKTLVACKK ALRDAGLKAE DIKGVVMVGG STRMPNVQRA VGELFGTKPL
NNLNPDQVVA LGAAMQADLL AGNQSKDDEW LLLDVIPLSL GIETMGGLVE KIIPRNTPIP
VARAQDFTTF KDGQTALAIQ VVQGERELAQ DCRSLGRFEL RGIPPMAAGA ARIRVTFQVD
ADGLLSVSAT EIGSGVKASI DIKPSYGLTD GEITRMLQEG FSSAKEDLLA RSLREEQVSA
QRLLDAVQTA LSTDRALLNE QEQAAIDQEM AQLQKILNEE TDSSVVRKAV DHAAKATDEF
AQKRMNASIQ KALSGKNVAE I