HSCA_SHEPC
ID HSCA_SHEPC Reviewed; 620 AA.
AC A4Y7D3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN OrderedLocusNames=Sputcn32_2145;
OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=319224;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN-32 / ATCC BAA-453;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella putrefaciens CN-32.";
RL Submitted (APR-2007) 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; CP000681; ABP75866.1; -; Genomic_DNA.
DR RefSeq; WP_011919389.1; NC_009438.1.
DR AlphaFoldDB; A4Y7D3; -.
DR SMR; A4Y7D3; -.
DR STRING; 319224.Sputcn32_2145; -.
DR GeneID; 45042605; -.
DR KEGG; spc:Sputcn32_2145; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
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.
FT CHAIN 1..620
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044890"
SQ SEQUENCE 620 AA; 66629 MW; 55D764E3CA7A6F0C CRC64;
MALLQIAEPG QSAAPHQHRL AVGIDLGTTN SLVAAVRSGE TATLPDEDGQ HSLPSIVRYT
QDTVEVGALA ALSSAQDPKN TIVSVKRFMG RSLTDIQTGE QSFPYEFAES ENGLPLFVTP
QGLVNPVQVS AEILRPLIAR AEKTLGGELQ GVVITVPAYF DDAQRQGTKD AAALLGVKVL
RLLNEPTAAA IAYGLDSKQE GVIAIFDLGG GTFDISVLRL NRGVFEVLAT GGDSALGGDD
FDHLLQEHMQ QVWLLGDIDV QLRRQLLIEA RRVKEALTDA NETEARIILA DGSELKQVVT
KRDFDSLISP LVKKTIASCR RTLRDAGVTA EEVLETVMVG GSTRVPLVRE QVEAFFGKPP
LTSIDPDRVV AIGAAIQADI LVGNKPESDL LLLDVIPLSL GIETMGGLVE KVVSRNTTIP
VARAQEFTTF KDGQTAMAFH VVQGERELVA DCRSLARFTL KGIPPLAAGA AHIRVTFQVD
ADGLLSVTAM EKSTGVQSSI QVKPSFGLSD TEIATMLKDS MKYAKDDISR RMLAEQQVEA
ARVLESLHAA LAKDGDLLND DERGQIDATM ANVAQLATGD DAEAIKQAIE RLDEQTQDFA
ARRMDNSIRV AFKGQSIDNI