ID HSCA_SHELP Reviewed; 620 AA.
AC A3QFD1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Shew_2313;
OS Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=323850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1088 / PV-4;
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., Serres G.,
RA Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella loihica PV-4.";
RL Submitted (MAR-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; CP000606; ABO24179.1; -; Genomic_DNA.
DR RefSeq; WP_011866110.1; NC_009092.1.
DR AlphaFoldDB; A3QFD1; -.
DR SMR; A3QFD1; -.
DR STRING; 323850.Shew_2313; -.
DR KEGG; slo:Shew_2313; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000001558; 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; 3.30.420.40; -; 2.
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 NCBIfam; TIGR01991; HscA; 1.
DR PANTHER; PTHR19375:SF176; CHAPERONE PROTEIN HSCA; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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..620
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044889"
SQ SEQUENCE 620 AA; 65714 MW; 6B22804C70328367 CRC64;
MALLQIAEPG QSAAPHQHRL AVGIDLGTTN SLVAAVRSGV ADTLADESGR HALASVVRYS
EDGVQVGVDA ERFSAQDPLN TVVSVKRFMG RSLSDIQAKD ASLPYNFSAS ENGLPLFNTQ
AGQFNPIQIS ADILRPLVDR AEKTLGGSLE GVVITVPAYF DDAQRQGTKE AASLLGVKVL
RLLNEPTAAA IAYGLDSGQE GVIAIYDLGG GTFDISILRL NKGVFEVLAT GGDSALGGDD
FDHALAAHLQ ESWQLTSLTA SERRALLIES RRVKEALTEQ ASVTASLTLE QGIVHEQVVD
KAQFDALIES LVKKTIASCR RALRDAAISN DEVLETVMVG GSTRVPLVRE RVEGFFGKAP
LTSIDPDRVV AIGAAIQADI LVGNKPESDL LLLDVIPLSL GIETMGGLVE KVVSRNTTIP
VARAQEFTTF KDGQTAMAFH VVQGERELVA DCRSLARFTL KGIPPMAAGA AHIRVTFQVD
ADGLLSVTAM EKSSGVQASI QVKPSFGLTD EEIGTMLKDS MAHAKEDIER RMLAEQQVEA
ARVLESLSAA LAKDGDLLDE AEAATIQAGM ANLAQVASQS DTDAIEKAIA ALDDASQDFA
AKRMDNSIRL ALKGQSVDNI
//
