HSCA_SHEDO
ID HSCA_SHEDO Reviewed; 619 AA.
AC Q12P79;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Sden_1462;
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000302; ABE54747.1; -; Genomic_DNA.
DR RefSeq; WP_011495905.1; NC_007954.1.
DR AlphaFoldDB; Q12P79; -.
DR SMR; Q12P79; -.
DR STRING; 318161.Sden_1462; -.
DR EnsemblBacteria; ABE54747; ABE54747; Sden_1462.
DR KEGG; sdn:Sden_1462; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_3_6; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001982; 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.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT CHAIN 1..619
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044887"
SQ SEQUENCE 619 AA; 66017 MW; C986F8A5CE54D395 CRC64;
MALLQIAEPG QSAAPHEHRL AVGIDLGTTN SLVAAVRSGE ALTLADSEGR HSLPSVVHYG
VDSTLVGHDA EALSALFPAQ TLVSVKRFMG KSLSDIQAGM QEFPYEFSVS EQGLPLFVMP
QGAVNPIQAS ADILRPLIER AEKTLGGQLQ GVVITVPAYF DDAQRQGTKD AAELLGVKVL
RLLNEPTAAA IAYGLDSKQE GVIAVYDLGG GTFDISVLRL SGGVFEVLAT GGNSALGGDD
FDHLLQQHLQ AAWGLTSASA QLSRQLLIEA RRVKEALTDN DTVTAHVSLD GSDLSLEISK
ADFEALIATL VKKTISSCRR TLRDAGISTD EVIETVMVGG STRVPLVRQQ VEQFFNKTPL
TSIDPDRVVA IGAAIQADIL VGNKPDSDLL LLDVIPLSLG IETMGGLVEK VIPRNTTIPV
ARAQEFTTFK DGQTAMAFHV VQGERELVDD CRSLARFTLT DIPALAAGAA HIRVTFQVDA
DGLLSVTAME KSTGVNTSIQ VKPSFGLSDL EIATMLKDSM KHAKDDISLR MLTEQKVEAM
RVIESLQAAL NNDGDLLELS ERESLQAALA NLGEIAKGND RDAIEQAIKA LDDKTQDFAS
LRMDNSIKAA LKGQSIDNI
